Title of Invention

THERAPEUTIC VACCINE

Abstract

The present invention is related to methods and compositions for the therapeutic and diagnostic use in the treatment of diseases and disorders which are caused by or associated with amyloid or amyloid-like proteins includmg amyloidosis, a group of disorders and abnormalities associated with amyloid protein such as Alzheimer's disease. The present invention provides novel methods and compositions comprising highly specific and highly effective antibodies having the ability to specifically recognize and bind to specific epitopes 6:0m a range of |3-amyloid proteins. The antibodies enabled by the teaching of the present invention are particularly useful for the treatment of diseases and disorders which are caused by or associated with amyloid or amyloid-like proteins including amyloidosis, a group of diseases and disorders associated with amyloid plaque formation including secondary amyloidosis and age-related amyloidosis including, but not limited to, neurological disorders such as Alzheimer's Disease (AD).

Full Text

Therapeutic Vaccine The present invention Is related to methods and compositions for the therapeutic and diagnostic use in the treatment of diseases and disorders which are caused by or associated with amyloid or amyloid-like proteins including amyloidosis, a group of disorders and abnonmalities associated with amyloid protein such as Alzheimer's Disease. Amyloidosis is not a single disease entity but rather a diverse group of progressive disease processes characterized by extracellular tissue deposits of a waxy, starch-like protein called amyloid, which accumulates in one or more organs or body systems. As the amyloid deposits build up, they begin to interfere with the normal function of the organ or body system. There are at least 15 different types of amyloidosis. The major forms are primary amyloidosis without known antecedent, secondary amyloidosis following some other condition, and hereditary amyloidosis. Secondary amyloidosis occurs in people who have a chronic infection or inflammatory disease, such as tuberculosis, a bacterial infection called familial Mediterranean fever, bone infections (osteomyelitis), rheumatoid arthritis, inflammation of the small intestine (granulomatous ileitis), Hodgkin's disease, and leprosy. Amyloid deposits typically contain three components. Amyloid protein fibrils, which account for about 90% of the amyloid material, comprise one of several different types of proteins. These proteins are capable of folding into so-called "beta-pleated" sheet fibrils, a unique protein configuration which exhibits binding sites for Congo red resulting in the unique staining properties of the amyloid protein. In addition, amyloid deposits are closely associated with the amyloid P (pentagonal) component (AP), a glycoprotein related to normal serum amyloid P (SAP), and with sulfated glycosaminoglycans (GAG), complex carbohydrates of connective tissue. Many diseases of aging are based on or associated with amyloid-like proteins and are characterized, in part, by the buildup of extracellular deposits of amyloid or amyloid-like material that contribute to the pathogenesis, as well as the progression of the disease. These diseases include, but are not limited to, neurological disorders such as Alzheimer's Disease (AD), including diseases or conditions characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI), Lewry body dementia, Down's syndrome, hereditary cerebral hemorrhage with amyloidosis (Dutch type); the Guam Parkinson-Dementia complex. Other diseases which are based on or associated with amyloid-like proteins such as progressive supranuclear palsy, multiple sclerosis; Creutzfeld Jacob disease, Parkinson's disease, HIV-related dementia, ALS (amyotropic lateral sclerosis). Adult Onset Diabetes; senile cardiac amyloidosis; endocrine tumors, and others, including macular degeneration. Although pathogenesis of these diseases may be diverse, their characteristic deposits often contain many shared molecular constituents. To a significant degree, this may be . attributable to the local activation of pro-inflammatory pathways thereby leading to the concurrent deposition of activated complement components, acute phase reactants, Immune modulators, and other inflammatory mediators (McGeer et al., 1994). Alzheimer's Disease (AD) is a neurological disorder primarily thought to be caused by amyloid plaques, an accumulation of abnormal deposit of proteins in the brain. The most frequent type of amyloid found in the brain of affected individuals is composed primarily of Ap fibrils. Scientific evidence demonstrates that an increase in the production and accumulation of beta-amyloid protein in plaques leads to nerve cell death, which contributes to the development and progression of Alzheimer's Disease. Loss of nerve cells in strategic brain areas, in turn, causes reduction in the neurotransmitters and impairment of memory. The proteins principally responsible for the plaque build up include amyloid precursor protein (APP) and two presenilins (presenilin I and presenilin II). Sequential cleavage of the amyloid precursor protein (APP), which is constitutivety expressed and catabolized in most cells, by the enzymes p and y secretase leads to the release of an 39 to 43 amino acid Ap peptide. The degradation of APPs likely increases their propensity to aggregate in plaques. It is especially the Ap(1-42) fragment that has a high propensity of building aggregates due to two very hydrophobic amino acid residues at its C-terminus. The Ap(1-42) fragment is therefore believed to be mainly involved and responsible for the initiation of neutritic plaque formation in Alzheimer's Disease and to have, therefore, a high pathological potential. There is therefore a need for specific antibodies that can target and diffuse amyloid plaque formation. The symptonr^s of Alzheimer's Disease manifest slowly and the first symptom may only be mild forgetfulness, In this stage, Individuals may forget recent events, activities, the names of familiar people or things and may not be able to solve simple math problems. As the disease progresses, symptoms are more easily noticed and become serious enough to cause people with Alzheimer's Disease or their family members to seek medical help. Mid-stage symptoms of Alzheimer's Disease include forgetting how to do simple tasks such as grooming, and problems develop with speaking, understanding, reading, or writing. Later stage Alzheimer's Disease patients may become anxious or aggressive, ma"y wander away from hom&and ultimately need total care. Presently, the only definite way to diagnose Alzheimer's Disease is to identify plaques and tangles in brain tissue in an autopsy after death of the individual. Therefore, doctors can only make a diagnosis of "possible" or "probable" Alzheimer's Disease while the person is still alive. Using current methods, physicians can diagnose Alzheimer's Disease correctly up to 90 percent of the time using several tools to diagnose "probable" Alzheimer's Disease. Physicians ask questions about the person's general health, past medical problems, and the history of any difficulties the person has carrying out daily activities. Behavioral tests of memory, problem solving, attention, counting, and language provide information on cognitive degeneration and medical tests-such as tests of blood, urine, or spinal fluid, and brain scans can provide some further information. The management of Alzheimer's Disease consists of medication-based and non-medication based treatments. Treatments aimed at changing the underlying course of the disease (delaying or reversing the progression) have so far been largely unsuccessful. Medicines that restore the deficit (defect), or malfunctioning, in the chemical messengers of the nerve cells (neurotransmitters), such as the cholinesterase inhibitors (ChEls), have been shown to improve symptoms. Medications are also available to address the psychiatric manifestations of Alzheimer's Disease. Cholinesterase inhibitors, such as Tacrine and Rrvastgmine, are currently the only class of agents that are approved by the FDA for the treatment of Alzheimer's Disease. These agents are medicines that restore the defect, or malfunctioning, in the chemical neurotransmission in the brain. ChEls impede the enzymatic degradation of neurotransmitters thereby increasing the amount of chemical messengers available to transmit the nerve signals in the brain. For some people in the early and middle stages of the disease, the drugs tacrine (COGNEX®, Morris Plains, NJ), donepezil (ARICEPT*, Tokyo, JP). rivastigmine (EXELON®, East Hanover, NJ), or galantamine (REMINYL®, New Brunswick, NJ) may help prevent some symptoms from becoming worse for a limited time. Another drug, -.memantine (NAMENDA®, New York, NY), has been approved for tceatnnsnt of moderate to severe Alzheimer's Disease. Also, some medicines may help control behavioral symptoms of Alzheimer's Disease such as sleeplessness, agitation, wandering, anxiety, and depression. Treating these symptoms often makes patients more comfortable and makes their care easier for caregivers. Unfortunately, despite significant treatment advances showing that this class of agents is consistently better than a placebo, the disease continues to progress, and the average effect on mental functioning has only been modest. ChEls also have side effects that include gastrointestinal dysfunction, liver toxicity and weight loss. Advances in the understanding of the brain abnormalities that occur in Alzheimer's Disease are hoped to provide the framework for new targets of treatment that are more focused on altering the course and development of the disease. Many compounds, including anti-inflammatory agents, are being actively investigated. Clinical trials using specific cyclooxygenase inhibitors {COX-2), such as rofecoxib and celecoxib, are also undenway. Other diseases that are based on or associated with the accumulation and deposit of amyloid-like protein are mild cognitive impalmnent, Lewy body dementia (LBD), amyotrophic lateral sclerosis (ALS), inclusion-body myositis (IBM) and macular degeneration, in particular age-related macular degeneration (AMD). Mild cognitive impairment (MCI) is a general temi most commonly defined as a subtle but measurable memory disorder A person with MCI experiences memory problems greater than nomially expected with aging, but does not stiow other symptoms of dementia, such as impaired judgment or reasoning. MCI is a condition that frequently reflects a preclinical stage of AD. The deposition of 3-amyloid within the entorhinal cortex (EC) is believed to play a key role in the development of mild cognitive impairment (MCI) in the elderly. This is in line with the observation that the CSF-A Ap(1-42) tevels decline significantly once AD becomes clinically overt. In contrast to CSF- Ap(1-42) CSF-tau levels are significantly increased in the MCI stage, and these values continue to be elevated thereafter, indicating that increased levels of CSF-tau-may help in detecting MCI subjects who are predicted to develop AD. Lewy body dementia (LBD) is a neurodegenerative disorder that can occur in persons older than 65 years of age, which typically causes symptoms of cognitive (thinking) impairment and abnormal behavioural changes. Symptoms can include cognitive impairment, neurological signs, sleep disorder, and autonomic failure. Cognitive impairment is the presenting feature of LBD in most cases. Patients have recurrent episodes of confusion that progressively worsen. The fluctuation in cognitWe ability is often associated with shifting degrees of attention and alertness. Cognitive impairment and fluctuations of thinking may vary over minutes, hours, or days. Lewy bodies are formed from phosphorylated and nonphosphorylated neurofilament proteins; they contain the synaptic protein alpha-synuclein as well as ubiquitin, which is involved in the elimination of damaged or abnormal proteins. In addition to Lewy Bodies, Lewy neurites, which are inclusion bodies in the cell processes of the nerve cells, may also be present. Amyloid plaques may fomi in the brains of patients afflicted with DLB, however they tend to be fewer in number than seen in patients with Alzheimer's disease. Neurofibrillary tangles, the other micropathological hallmark of AD, are not a main characteristic of DLB but are frequently present in addition to amyloid plaques. Amyotrophic lateral sclerosis (ALS) is characterized by degeneration of upper and lower motor neurons. In some ALS patients, dementia or aphasia may be present (ALS-D). The dementia is most commonly a frontotemporal dementia (FTD), and many of these cases have ubiquitin-positive, tau-negative inclusions in neurons of the dentate gyrus and superficial layers of the frontal and temporal lobes. Inclusion-body myositis (IBM) is a crippling disease usually found in people over age 50, in which muscle fibers develop inflammation and begin to atrophy—but in which the brain is spared and patients retain their full intellect. Two enzymes involved in the production of amyloid-B protein were found to be increased inside the muscle cells of patients with this most common, progressive muscle disease of older people. In which amyloid-ll is also increased. Another disease that is based on or associated with the accumulation and deposit of amyloid-like protein is macular degeneration. Macular degeneration is a common eye disease that causes deterioration of the macula, which is the central area of the retina (the paper-thin tissue at the back of the eye where light-sensitive cells send visual signals to the brain). Sharp, clear, 'straight ahead' vision is processed by the macula. Damage to the macula results in the development of blind spots and blurred or distorted vision. Age-related macular degeneration (AMD) Is a major cause of visual impaiment in the United States and for people over age 65 it is the leading cause of legal blindness among Caucasians. Approximately 1.8 million Americans age 40 and older have advanced AMD, and another 7.3 million people with intermediate AMD are at substantial risk for vision loss. The government estimates that by 2020 there will be 2.9 miliion people with advanced AMD. Victims of AMD are often surprised and fnjstrated to find out how little is known about the causes and treatment of this blinding condition. There are two forms of macular degeneration: dry macular degeneration and wet macular degeneration. The dry forni, in which the cells of the macula slowly begin to break down, is diagnosed in 85 percent of macular degeneration cases. Both eyes are usually affected by dry AMD, although one eye can lose vision while the other eye remains unaffected, Drusen, which are yellow deposits under the retina, are common early signs of dry AMD. The risk of developing advanced dry AMD or wet AMD increases as the number or size of the drusen increases. It is possible for dry AMD to advance and cause loss of vision without turning Into the wet fonn of the disease; however, it Is also possible for early-stage dry AMD to suddenly change into the wet form. The wet form, although it only accounts for 15 percent of the cases, results in 90 percent of the blindness, and is considered advanced AMD (there is no early or intermediate stage of wet AMD). Wet AMD is always preceded by the dry form of the disease. As the dry form worsens, some people begin to have abnormal blood vessels growing behind the macula. These vessels are very fragile and will leak fluid and blood (hence 'wet' macular degeneration), causing rapid damage to the macula. ^^ The dry form of AMD will initially often cause slightly blurred vision. The center of vision in particular may then become blurred and this region grows larger as the disease progresses. No symptoms may be noticed if only one eye is affected. In wet AMD, straight lines may appear wavy and central vision loss can occur rapidly. Diagnosis of macular degeneration typically involves a dilated eye exam, visual acuity test, and a viewing of the back of the eye using a procedure called fundoscopy to help diagnose AMD, and—if wet AMD Is suspected—fluorescein angiography may also be performed. If dry AMD reaches the advanced stages, there is no current treatment to prevent vision loss. However, a specific high dose formula of antioxidants and zinc may delay or prevent intennediate AMD from progressing to the advanced stage. Macugen® (pegaptanib sodium injection), laser photocoagulation and photodynamic therapy can control the abnormal blood vessel growth and bleeding in the macula, which Is helpful for some people who have wet AMD; however, vision that is already lost will not be restored by these techniques. If vision is already lost, low vision aids exist that can help improve the quality of life. One of the earliest signs of age-related macular degeneration (AMD) is the accumulation of extracellular deposits known as dmsen between the basal lamina of the retinal pigmented epithelium (RPE) and Bruch's membrane (BM). Recent studies conducted by Anderson et al. have confirmed that drusen contains amyloid beta, (Experimental Eye Research 78 (2004) 243-256). Ongoing research continues with studies exploring environmental, genetic, and dietary factors that may contribute to AMD. New treatment strategies are also being explored, including retinal cell transplants, drugs that will prevent or slow down the progress of the disease, radiation therapy, gene therapies, a computer chip implanted in the retina that may help stimulate vision and agents that will prevent the growth of new blood vessels under the macula. What is needed therefore, are effective therapeutic vaccine compositions and methods for addressing the complications associated with amyloidosis, a group of diseases and- -disorders associated with amyloid plaque formation including secondary amyloidosis and age-related amyloidosis including, but not limited to, neurological disordere such as Alzheimer's Disease (AD), including diseases or conditions characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI), Lewy body dementia, Down's syndrome, hereditary cerebral hemorrhage with amyloidosis (Dutch type); the Guam Parkinson-Dementia complex; as well as other diseases which are based on or associated with amyloid-like proteins such as progressive supranuclear palsy, multiple sclerosis; Creutzfeld Jacob disease, Parkinson's disease, HIV-related dementia, ALS (amyotropic lateral sclerosis). Adult Onset Diabetis; senile cardiac amyloidosis; endocrine tumors, and others, including macular degeneration. In particular what Is need are specialized and highly effective therapeutic vaccines and compositions comprising said vaccines, which are capable of counteracting the physiological manifestations of the disease such as the formation of plaques associated with aggregation of fibers of the amyloid or amyloid-like peptide. The present invention provides novel methods and compositions for eliciting a highly specific and highly effective immune response in an organism, but particularly within an animal, particularly a mammal or a human, which is capable of preventing or alleviating amyloidosis, or the symptoms associated with amyloidosis, a group of diseases and disorders associated with amytaid plaque formation including secondary amyloidosis and age-related amyloidosis including, but not limited to, neurological disorders such as Alzheimer's Disease (AD), including diseases or conditions characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI), Lewy body dementia, Down's syndrome, hereditary cerebral hemorrhage with amyloidosis (Dutch type); the Guam Parkinson-Dementia complex; as well as other diseases which are based on or associated with amyloid-like proteins such as progressive supranuclear palsy, multiple sclerosis; Creutzfeld Jacob disease. Parkinson's disease, HlV-related dementia, ALS (amyotropic lateral sclerosis), Adult Onset Diabetes; senile cardiac amyloidosis; endocrine tumors, and others, including macular degeneration. In particular, the present invention provides novel methods and compositions for retaining or improving, but particularly for restoring, more particularly for completely festering the cognitive memory capacity io^ marnmgtexhibiting an amyioid-associ,ated.. disease or condition. It is an object of the invention to provide a therapeutic vaccine composition and a method of producing such a composition for the treatment of diseases and disorders which are caused by or associated with amyloid or amyloid-like proteins including amyloidosis, a group of diseases and disorders associated with amyloid plaque formation including secondary amyloidosis and age-related amyloidosis including, but not limited to, neurological disorders such as Alzheimer's Disease (AD), particularly a disease or condition characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impaimrient (MCI) comprising a peptide fragment from the N-terminal part of the Ap peptide, particulariy an Ap peptide fragment consisting of a single or repetitive stretch of between 13 and 15 contiguous amino acid residues from the N-terminal part of the Ap peptide, but particularly an Ap peptide fragment consisting of amino acid residues selected from the group consisting of residues 1-15, 1-14, and 1-ISfrom the N-terminal part of the Ap peptide, more particularly of residue 1-15 as given in SEQ ID NO: 1, including functionally equivalent fragments thereof, but especially a Ap peptide fragment as mentioned herein before attached to, or incorporated or reconstituted in a carrier particle/adjuvant such as, for example, a liposome. This contiguous stretch of 13 to 15 amino acid residues may be obtained from the N-temiinal fragment 1-16, 1-17, 1-18 or 1-20 of the Ap peptide but particularly from the N-terminal fragment 1-16 or 1-17 of the Ap peptide as given in SEQ ID NO: 2 and SEQ ID t^lO: 5, respectively and may be interrupted by the deletion of one to three amino acid residues to result in a stretch of between 13 and 15 amino acid residues, wherein the deleted amino acid residues may be adjacent amino acid residues or residues separated from each other by at ieast 1 amino acid residue, but particularly amino acid residues which are not negatively charged residues, if it is desired for the overall net charge of the antigenic peptide molecule to be negative, or amino acid residues which are not positively charged, if it is desired for the overall net charge of the antigenic peptide molecule to be positive. This contiguous stretch of 13 to 15 amino acid residues may be repeated in the antigenic construct according to the invention between 2 and 50 times, particularly between 2 and 30 t4mes, more particularly between 2 and-2Q,time^ -_:.: even more particularly between 2 and 16 times, but especially between 2 and 10 times. In a specific embodiment of the invention, the contiguous stretch of 13 to 15 amino acid residues is used in form of a polymer selected from the group consisting of a 2-mer, a 3-mer, a 4-tramer, a 5-mer, a 6-mer, a 7-mer, a 8-mer, a 9-mer, a 10-mer, a 11-mer, a 12-mer, a 13-mer, a 14-mer, a 15-mer, a 16-mer, a 20-mer, a 30-merand a 50-mer. In a further embodiment, the invention provides a therapeutic vaccine composition and a method of producing such a composition for the treatment of diseases and disorders which are caused by or associated with amyloid or amyloid-like proteins including amyloidosis, a group of diseases and disorders associated with amyloid plaque formation including secondary amyloidosis and age-related amyloidosis including, but not limited to, neurological disorders such as Alzheimer's Disease (AD), particularly a disease or condition characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI) as further specified herein below using an Ap peptide fragment from the N-termlnal part of the Ap peptide, but particularly an Ap peptide fragment consisting of amino acid residues selected from the group consisting of 1-15, 2-15, 3-15, 1-14, 2-14, 1-13; 1-16(A2), 1-16(A4), 1-16(A5), 1-16(A6). 1-16(A8), 1-16(A9), 1-16(A10); 1-16{A12), 16(A13), 16{A14), 1-16(A15), 1-15(A2), 1-15(A4), 1-15(A5), 1-15(A6). 1-15(A8), 1-15(A9), 1-15(A10); 1-15(A12), 15(A13), 15(A14), more particularly an Ap peptide fragment consisting of amino acid residues 1-15 as given in SEQ ID NO: 1, and 1-16(A14) as given in SEQ ID NO: 3. Also comprised by the present invention is a peptide fragment which is essentially identical to the above mentioned fragments and has substantially the same biological activity of said fragments, but particular a peptide fragment that is a consen/atively modified variant of said fragments in that the alterations result in the substitution of one or more amino acid, particularly of between one to 10 amino acids, more particularly of betw/een one to 6 amino acids, even more particularly of t)etween one to 4 amino acids, but especially of between one to 3 amino acids, with a chemically simitar amino acid. Conservative substitution tables providing functionally similar amino acids are well known In the art and disclosed herein below. The conservative substitution is preferably to be made such that the overallnet charge ofJhe,pepttde and also the charge, distribution over the peptide molecule remains essentially the same. In a specific embodiment of the invention at least one, particularly 2, more particularly 3 or even all of the negatively charged amino acid residues 1, 3, 7. 11 may be replaced with a chemically similar negatively charged amino acid. Particularly, the Asp in position 1 and 7, respectively, may be replaced with a Glu and the Glu in position 9 and 11, respectively, may be replaced with an Asp. In a specific embodiment of the invention, a therapeutic vaccine composition and a method of producing such a composition is provided comprising an Ap peptide fragment from the N-terminal part of the Ap peptide, but particularly an Ap peptide fragment consisting of amino acid residues selected from the group consisting of 1-15, 2-15, 3-15, 1-14.2-14, 1-13; 1-16(A2), 1-16(A4), 1-16(A5), 1-16{A6), 1-16(A8), 1-16(A9), 1-16{A10); 1-16(A12), 16(A13), 16(A14), 1-16(A15), 1-15(A2). 1-15(A4). 1-15(A5), 1-15(A6), 1-15(A8), 1-15(A9), 1-15(A10); M5{A12), 15(A13), 15(A14), an Api.i6(ai5) peptide antigen, more particularly a Api.ietiu) or Api.i6(ai3) peptide antigen, even more particularly a Api. 14 peptide antigen, specifically a Api.15 peptide antigen, but especially an Ap peptide fragment consisting of amino acid residues 1-15 as given in SEQ ID NO: 1, and 1-16(A14) as given in SEQ ID NO: 3, for the treatment of diseases and disorders which are caused by or associated with amyloid or amyloid-iike proteins including amyloidosis, a group of diseases and disorders associated with amyloid plaque formation including secondary amyloidosis and age-related amyloidosis including, but not limited to, neurological disorders such as Alzheimer's Disease (AD), particularly a disease or condition characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI). In a specific embodiment the invention provides a therapeutic vaccine composition and a method of producing a therapeutic vaccine composition for retention or improvement, particularly for complete restoration of the cognitive memory capacity of an animal, particularly a mammal or a human, suffering from memory impairment using an Ap peptide fragment from the N-temninal part of the Ap peptide, but particularly an Ap peptide fragment consisting of amino acid residues selected from the group consisting Qi 1-15,2-15, 3-15, 1-14, 244, :M3; M6(A2), 1-16(A4), 1-16(A5), .■1-16(A&>, 1-16(A8); , ,j 1-16(A9), 1-16(A10); 1.16(A12), 16(A13), 16(A14). M6(A15). 1-15(A2), 1-15(A4), 1-15(A5), 1-15(A6), 1-15(A8), 1-15(A9), 1-15(A10); 1-15(A12), 15(A13), 15(A14), particularly an Api-ie^is) peptide antigen, more particularty a Api.i6{Ai4} or Api-i6(Ai3) peptide antigen, even more particularly a Api.^ peptide antigen, specifically a ApMs peptide antigen, but especially an Ap peptide fragment consisting of amino acid residues 1-15 as given in SEQ ID NO: 1,and 1-16(A14) as given in SEQ ID NO: 3. It is also an object of the invention to provide a method for the treatment of diseases and disorders which are caused by or associated with amyloid or amyloid-like proteins including amyloidosis, a group of diseases and disorders associated with amyioid plaque fomiation including secondary amyloidosis and age-related amyloidosis including, but not limited to, neurological disorders such as Alzheimer's Disease (AD), particularly a disease or condition characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI) by administering to an animal, particularly a mammal or a human, a vaccine composition according to the invention and as described herein. In a specific embodiment the invention provides a method for retaining or increasing cognitive memory capacity but, particularty, for fully restoring the cognitive memory capacity of an animal, particularly a mammal or a human, suffering from memory impairment by administering to an animal, particularly a mammal or a human, a vaccine composition according to the invention and as described herein. It is a further object of the invention to provide a therapeutic vaccine composition and a method of producing such a composition as well as a method for the treatment of diseases and disorders which are caused by or associated with amyloid or amyloid-like proteins including amyloidosis, a group of diseases and disorders associated with amyloid plaque fonnation including secondary amyloidosis and age-related amyloidosis including, but not limited to, neurological disorders such as Alzheimer's Disease (AD), particuiariy a disease or condition characterized by a loss of cognitive memory capacity sucti as, for example, mild cognitive impaimront (MCI), using an A^ peptide antigen according to the invention and as described herein before, but particularly an Ap . peptide fragment from the N-termJnalpartof the Ap peptide, but particularly an Ap peptide fragment consisting of amino acid residues selected from the group consisting of 1-15, 2-15, 3-15, 1-14, 2-14, 1-13; 1-16(A2), 1-16(A4), 1-16(A5), 1-16(A6), 1-16(A8), 1-16(A9), M6{A10); 1-16(A12). 16(A13), 16(A14), 1-16(A15), 1'15(A2), 1-15(A4). 1-15(A5), 1-15(A6), 1-15{A8), 1-15(A9), 1-15(A10); 1-15(A12), 15(A13), 15{A14), particularly an Apvieiais) peptide antigen, more particularly a Api-i6(fii4) or Api.i6(ai3> peptide antigen, even more particularly a Api-u peptide antigen, specifically a Api-is peptide antigen, but especially an Ap peptide fragment consisting of amino acid residues 1-15 as given in SEQ ID NO: 1, and 1-16{A14) as given in SEQ ID NO: 3, wherein the Ap peptide antigen is modified such that it is capable of maintaining and stabilizing a defined conformation characterized by a balanced proportion of a-helical and/or p-sheet and/or random coil portions and of inducing a highly specific immune response in the treated animal. The vaccine composition according to the invention and as described hereinbefore upon administration to an animal, particularly a mammal, but especially a human, results mainly in the generation of antibodies of non-inflammatory Th2 subtypes such as, for example, Isotype IgGI and lgG2b and/or antibodies of the T-cell independent IgG subclass such as, for example, lgG3 and/or does not lead to a significant increase in inflammation markers in the the brain, particularly of inflammation markers selected from the group consisting of lL-1 p, lL-6,1F^4-Y and TNF a. In a further embodiment of the invention the vaccine according to the present invention as described herein before, upon administration to an animal, particularly a mammal, but especially a human, leads to a significant decrease of insoluble, plaque-related-A|31-40andAp1-42 In the brain. In still a further emfc>odimer\t of the invention the vaccine according to the present invention as described herein before, upon administration to an animal, particulariy a mammal, but especially a human, leads to a significant reduction in the level of soluble Ap1-42 in the brain. Further provided is a vaccine according to the invention and as described herein before, which, upon adnmnistration to an animatr particularly a mammal or a human,.suffering, from an amyloid-associated condition characterized by a loss of cognitive memory capacity leads to an increase in the retention of cognitive memory capacity. The invention further relates to a vaccine according to the present invention and as described herein before, w/hich, upon administration to an animal, particularly a mammal or a human, suffering fronn an amyloid-associated condition characterized by a loss of cognitive memory capacity leads to a complete restoration of cognitive memory capacity. in particular, the Ap peptide antigen according to the invention and as described herein before, specifically an Ap peptide fragment from the N-terminal part of the Ap peptide, but particularly an Ap peptide fragment consisting of amino acid residues selected from the group consisting of 1-15, 2-15, 3-15, 1-14, 2-14, 1-13; 1-16(A2), 1-16(A4), 1-16(&5), 1-16(A6), 1-16(A8), 1-16(A9), 1-16(A10); 1-16(A12), 16{A13), 16(A14), 1-16(A15), 1-15(A2), 1-15(A4), 1-15(A5), 1-15(A6), 1-15(A8), 1-15(A9), 1-15(A10); 1-15(A12), 15(A13), 15(A14), particularly an Api.i6(Ai5) peptide antigen, more particularly a Api. i6(Ai4) or Api.i6(Ai3) peptide antigen, even more particularly a Api.u peptide antigen, specifically a APi.15 peptide antigen, but especially an Ap peptide fragment consisting of amino acid residues 1-15 as given in SEQ ID NO: 1, and 1-16(A14) as given in SEQ ID NO: 3, is presented attached to, or incorporated or reconstituted in a carrier such as, for example, a vesicle, a particulate body or molecule but, particulariy, a liposome. The immunogenic compositions of the present invention may comprise liposomes made by reconstituting liposomes in the presence of purified or partially purified or modified antigenic peptides according to the invention. Additionally, peptide fragments may be reconstituted into liposomes. The present invention also includes antigenic peptide fragments modified so as to increase their antigenicity. For example, antigenic moieties and adjuvants may be attached to or admixed with the peptide. Examples of antigenic moieties and adjuvants include, but are not limited to, lipophilic muramyl dipeptide derivatives, nonionjc block polymers, aluminum hydroxide or aluminum phosphate adjuvant, and mixtures thereof. In another embodiment of ttie Invention the AP peptide antigen according to the invention and as described herein before, specifically an Ap peptide fragment from the ^ N-terminal-part of4he Ap peptide, but particularly.aiAp peptide fragmeoLconaisting. of amino acid residues selected from the group consisting of 1-15, 2-15, 3-15, 1-14, 2-14, 1-13; 1-16(A2), 1-16(A4), 1-16(A5), 1-16(A6). 1-16(A8), 1-16(A9), 1-16(A10); 1-16(A12), 16(A13), 16CA14), 1-16(A15), 1-15(A2), 1-15(A4), 1-15(A5), 1-15{A6), 1-15(A8), 1-15(A9), 1-15(A10); 1-15(A12), 15(A13), 15(A14). particularly an Apviewis) peptide antigen, more particularly a Api.i6(Ai4) or Api.i6(Ai3) peptide antigen, even more particularly a APi.14 peptide antigen, specifically a AP1-15 peptide antigen, but especially an Ap peptide fragment consisting of amino acid residues 1-15 as given in SEQ ID NO: 1, and 1-16(A14} as given in SEQ ID NO; 3, is modified by a lipophilic or hydrophobic moiety, that facilitates insertion into the lipid bilayer of the liposome carrier/immune adjuvant, particularly by a lipophilic or hydrophobic moiety w/hich functions as an anchor for the peptide in the liposome bilayer and has a dimension that leads to the peptide being positioned and stabilized in close proximity to the liposome surface. In a further embodiment of the invention, the lipophilic or hydrophobic moiety is a fatty acid, a triglyceride or a phospholipid, but especially a fatty acid, a triglyceride or a phospholipid, virhereln the fatty acid carbon back bone has at least 10 carbon atoms. Particularly, the lipophilic or hydrophobic moiety is a fatty acid W\th a carbon backbone of at least approximately 14 carbon atoms and up to approximately 24 carbon atoms, with each individual number of carbon atom falling within this range also being part of the present invention. More particularly, the lipophilic or hydrophobic moiety has a carbon backbone of at least 14 carbon atoms, but especially 16 carbon atoms. Examples of hydnDphobic moieties include, but are not limited to, palmitic acid, stearic acid, myristic acid, lauric acid, oleic acid, linoleic acid, and linolenic acid. In a specific embodiment of the present invention the lipophilic or hydrophobic moiety is palmitic acid. In still a further embodiment of ttie invention the hydrophobic moiety is palmitic acid and the liposome preparation may in addition contain an adjuvant such as, for example, lipid A, alum, calcium phosphate, interleukin 1, and/or microcapsules of polysaccharides and proteins, but particularly a detoxified lipid A, such as monophosphoryl or diphosphoryl lipid A, or alum. It is a further object of the invention to provide a therapeutic vaccine composition and a method:of producing, such ^a composition .using.,an immunogenic antigenic .pej^de -according to the invention and as described herein before, for the treatment of diseases and disorders which are caused by or associated with amyloid or amyloid-like proteins including amyloidosis, a group of diseases and disorders associated with amyloid plaque foonation including secondary amyloidosis and age-related amyloidosis including, but not limited to, neurological disorders such as Alzheimer's Disease (AD), particularly for retention, increase or restoration of the cognitive memory capacity of an animal, particularly a mammal or a human, suffering from memory Impairment, as well as a method for the treatment of said amyloidosis, wherein the p-amyloid peptide antigen is a palmitoylated Ap peptide antigen according to the invention and as described herein before reconstituted in a liposome, specifically a palmitoylated A(3 peptide fragment from the N-terminal part of the Ap peptide, but particularly a palmitoylated Af3 peptide fragment consisting of amino acid residues selected from the group consisting of 1-15, 2-15, 3-15, 1-14, 2-14, 1-13; 1-16(A2), 1-16(A4), 1-16(A5), 1-16(A6), 1-16(A8). 1-16{A9), 1-ie(A10); 1-16(A12), 16(A13), 16(A14), 1-16(A15), 1-15(A2), 1-161A4), V15(A5), 1-15(A6>, 1-15(A8), 1-15(A9), 1-15(A1Q); 1-15(A12), 15(A13), 15(A14), particularly a palmitoylated Api.i6(£.i5> peptide antigen, more particularly a palmitoylated ApMSfau) or Api-i6{Ai3) peptide antigen, even more particularly a palmitoylated Api.i^ peptide antigen, specifically a palmitoylated ApMs peptide antigen, but especially a palmitoylated Ap peptide fragment consisting of amino acid residues 1-15 as given in SEQ ID NO: 1, and 1-16(A14) as given in SEQ ID NO: 3, modified by covalently attached palmitoyi residues, particularly between 2 and 4 palmitoyi residues, more particularly 4 palmitoyi residues, coupled to each terminus of the peptide antigen via one or more, but particularly via one or two suitable amino acid residues such as lysine, glutamic acid or cystein, or any other amino acid residue that can be suitably used for coupling a palmitoyi residue to the antigenic peptide. In a specific embodiment of the invention, 2 or more of the palmitoylated Ap peptide antigen molecules modified by covalently attached palmitoyi residues at each end of the peptide are reconstituted in a single liposome. The present invention provides novel methods and immunogenic compositions comprising an immunogenic antigenic peptide, which, upon administration to an animal, particularly aLmamrpal or_a human, suffering from ao amyloid-sssoc^ted-.condition,-... particularly from a condition characterized by a loss of cognitive memory capacity such as, for example, mild cc^nitive impairment (MCI), induces an immune response in said animal or human. The treatment with the therapeutic vaccine according to the invention leads to a retention or an increase in cognitive memory capacity but, particulariy, to a complete restoration of cognitive memory capacity. It is another object of the invention to provide a therapeutic vaccine composition and a method of producing such a composition using a immunogenic antigenic peptide, for inducing an immune response in an animal, particularly a mammal or a human, as well as a method for inducing an immune response in an animal, particularly a mammal or a human, said animal or human suffering from an amyloid-associated condition characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI), by administering to said animal or human a therapeutic vaccine composition comprising an Ap peptide antigen according to the invention and as described herein before, but specifically a palmitoylated Ap peptide fragment from the N-terminal part of the Ap peptide, but particularly a palmitoylated Ap peptide fragment consisting of amino acid residues selected from the group consisting of 1-15, 2-15, 3-15, 1-14, 2-14, 1-13; M6(A2), 1-16{A4), 1-16(A5), 1-16(A6). 1-16(A8), 1-16(A9), 1-16(A10); 1-16(A12), 16(A13), 16(A14), 1-16(A15), 1-15(A2), 1-15(A4), 1-15(A5), 1-15(A6), 1-15(A8), 1'15(A9), 1-15(A10); 1-15(A12), 15CA13), 15(A14), particularly a palmitoylated APi-i6(ii5) peptide antigen, more particularly a palmitoylated Api-i6{Ai4) or Api.i6(Ai3) peptide antigen, even more particularly a palmitoylated Api.14 peptide antigen, specifically a palmitoylated Api.is peptide antigen, but especially 3 palmitoylated Ap peptide fragment consisting of amino acid residues 1-15 as given in SEQ ID NO: 1, and 1-16(A14) as given in SEQ ID NO: 3, such that the cognitive memory capacity of the treated animal or human is retained or increased but, particularly, completely restored. The antigenic peptide as described herein before, but specifically an Ap peptide fragment from the N-terminal part of the Ap peptide, but particularly an Ap peptide fragment consisting of amino acid residues selected from the group consisting of 1-15, 2-15, 3-15, 1-14, 2-14, 1-13; 1-16(A2), 1-16(A4). 1-16(A5), 1-16(A6), 1-16(A8). 1-16(A9), 1-16(A10); M6(A12), 16(A13), 16(A14). 1-16{A15), 1-15(A2), 1-15(A4), 1-15(A5), 1-15(A6), 1-15(A8). 1-15(A9), 1-T5{A1D); 1.1S{A12),. 15CA13), 15(A14), particularly, an - - -Api-i6(Ai5) peptide antigen, more particularly a Api.is(ai4) or Api.i6(Ai3) peptide antigen, even more particularly a Apvu peptide antigen, specifically a Apvis peptide antigen, but especially an Ap peptide fragment consisting of amino acid residues 1-15 as given in SEQ ID NO: 1, and 1-16(A14) as given In SEQ ID NO: 3, is also part of the present invention. Also part of the invention is a palmitoylated AP peptide antigen according to the invention and as described herein before, specifically a palmitoylated Ap peptide fragment from the N-terminal part of the Ap peptide, but particularly a palmitoylated AP peptide fragment consisting of amino acid residues selected from the group consisting of 1-15, 2-15, 3-15, 1-14, 2-14, 1-13; 1-16(A2), 1-16(A4), 1-16(A5), 1-16(A6). 1-16(A8), 1-16(A9), 1-16(A10); 1-16(A12), 16(A13), 16(A14), 1-16(A15), 1-15(A2), 1-15{A4), 1-15(A5), 1-15(A6), 1-15(A8), 1-15(A9), 1-15(A10); 1-15(A12), 15(A13), 15(A14), particularly a palmitoylated Api.i6(ii5) peptide antigen, more particularly a palmitoylated Api-i6(Ai4) or Api-i6(Ai3) peptide antigen, even more particularly a palmitoylated Api.u peptide antigen, specifically a palmitoylated Api.is peptide antigen, but especially a palmitoylated Ap peptide fragment consisting of amino acid residues 1-15 as given in SEQ ID NO: 1, and 1-16(A14) as given in SEQ ID NO: 3, modified by covalently attached palmitoyi residues, particularly between 2 and 4 patmitoyi residues, more particularly 4 palmitoyi residues, coupled to each terminus of the peptide antigen via one or more, but particularly via one or two suitable amino acid residues such as lysine, glutamic acid or cystein, or any other amino acid residue that can be suitably used for coupling a palmitoyi residue to the antigenic peptide. tn a specific embodiment of the invention, 2 or more of the palmitoyiated Ap peptide antigen molecules modified by covalently attached palmitoyi residues at each end of the peptide are reconstituted in a single liposome. Further comprised by the present invention is a antigenic peptide presented attached to, nr incorporated or reconstituted in a carrier such as, for example, a vesicle, a particulate / or molecule but, particularly, a liposome, as described herein before, but ;ifica!ly an Ap peptide fragment from the N-tenninal part of the Ap peptide, but cularly an Ap peptide fragment .consisting of amino acid residues selected from the , p consisting of 1-15, 2-15, 3-15, 1-14, 2-14, 1-13; 1-16(A2), 1-16(A4), 1-16(A5). 1-L6), 1-16(A8), 1-16(A9), 1-16(A10); 1-16(A12). 16(A13). 16(A14), 1-16(A15), 1-2), 1-15(A4), 1-15(A5), 1-15{A6), 1-15(A8), 1-15(A9), 1-15(A10); 1-15(A12), ,13), 15(A14), particularly an Api,i6(Ai5) peptide antigen, more particularly a Api-i) or Api-i6(ai3) peptide antigen, even more particularly a Api.u peptide antigen, ifically a Api.15 peptide antigen, but especially an Ap peptide fragment consisting of 10 acid residues 1-15 as given in SEQ ID NO: 1, and 1-16(A14) as given in SEQ ID 3 presented attached to, or incorporated or reconstituted in a cairier such as, for iple, a vesicle, a particulate body or molecule as described herein before. Dut intending to be bound by a specific hypothesis, it is reasonable to assume that nmune response induced by the therapeutic vaccine composition of the invention lead in the animal or human to a stimulation of T-cells and other reactive immune directed against an immunogenic agent, but particularly to the generation of highly ific and highly effective antibodies having the ability to specifically recognize and specific epitopes from a range of p-amyloid antigens, wrhich antibody, upon binding antigen, mediates and/or induces the observable effect of retention, increase and, particularly, complete restoration of cognitive memory capacity in the treated animal or human. The present invention further provides a vaccine composition, which, upon administration to an animal, particularly a mammal or a human, induces the generation of an antibody in the treated animal or human that directly and specifically binds to p-amyloid fibers such as, for example, fibers comprising Aβ monomeric peptides 1-39; 1-40, 1-41, 1-42 or 1-43, but especialiy to fibers comprising Aβ^2 monomeric peptides and/or is capable of inducing solubilization of preformed high molecular polymeric amyloid fibrils or filaments formed by the aggregation of amyloid monomeric peptides, particularly p-amyloid monomeric peptides such as, for example, Ap monomeric peptides 1-39; 1-40, 1-41, 1-42 or 1-43, but especially Aβ2 monomeric peptides, by targeting and specifically binding to an epitope within an epitopic region of the p-amyloid protein, particularly an epitopic region of the Ap polypeptide confined by amino acid residues aan-aam with n being an Integer between 2 and 15, particularly between 5 and 15, more particularly between 8-and 15, even more particularly between 10 and 15 and m being an integer between 3 and 17, particularly between 6 and 17. more particularly between 9 and 17, even more particularly between 11 and 17, wherein n and m cannot be identical numbers and n must always be a smaller number than m, with the difference between n and m >2. In a specific embodiment of the invention, the antibody binds to an epitope within an epitopic region of the p-amyloid protein comprising amino acid residues 1-10, but particulariy amino acid residues 1-9. Said antibody also specifically binds to soluble amyloid monomeric and oligomeric peptides, particularly p-amyloid monomeric or oligomeric peptides selected from the group consisting of Ap peptides 1-39; 1-40, 1-41, 1-42 or 1-43, but especially Aβ1-2, and inhibits the aggregation of the Ap monomers or oligomers into high molecular polymeric fibrils. In a further embodiment, the invention provides an antibody, pari:icularly a monoclonal antibody, including any functionally equivalent antibody or functional parts thereof, which antibody incorporates at least one of the properties selected from the group consisting of aggregation inhibition, disaggregation, induction of conformational transition, recognition of and direct binding to an epitope in the 4-16 region, particulariy in the 1-9 region, but especially a combination of two or more of said properties. More specifically, an antibody is provided, particularly a monoclonal antibody, including any functionally equivalent antibody or functional parts thereof, which antibody shows a combined reactivity against the 1-16 and 29-40 region, more particularly against the 1-16 and 22-35 region in that it is capable of recognizing and binding to both said regions, the 1-16 and the 29-40 region and the 1-16 and 22-35 region, respectively, and Incorporates at least one of the properties mentioned herein before, that is aggregation inhibition, disaggregation, induction of confonnational transition, but especially a combination of two or more of said properties. The antibodies which are induced by the vaccine composition according to the invention and which can be obtained from an immunized animal or a hybridoma cell line producing said antibodies, are also part of the invention. In a specific embodiment, the invention provides an antibody including any functionally equivalent antibody or functional parts thereof particularly a monoclonal antibody Including any functionally equivalent antibody or functional parts thereof obtainable by immunizing a suitable animal with a vaccine composition according to the invention and as described herein before, particularly a vaccine composition comprising an Aβi.i6(ai5) peptide antigen, more particularly an Aβ6(Ai4) or Aβi.iBfais) peptide antigen, even more particularly an Aβi.i4 peptide antigen, but especially an AβMs peptide antigen, which antibody is a bifunctional antibody and, upon co-incubation with amyloid monomeric peptides, particularly p-amyloid monomeric peptides such as, for example, Ap monomeric peptides 1-38, 1-39; 1-40, 1-41, 1-42 or 1-43, but especially Aβi-42 monomeric peptides, inhibits the aggregation of the Ap monomers into high molecular polymeric fibrils and, in addition, upon co-incubation with prefomned high molecular polymenc amyloid fibrils or filaments fomned by the aggregation of amyloid monomeric peptides, particularly p-amyloid monomeric peptides such as, for example, Ap monomeric peptides 1-38, 1-39; 1-40, 1-41, 1-42 or 1-43, but especially Aβ^2 monomeric peptides, is capable of disaggregating the preformed polymeric fibrils or filaments. In a specific embodiment, the invention provides an antibody, particularly a bifunctional antibody, but especially a monoclonal antibody, particularly a bifunctional monoclonal antibody. Including any functionally equivalent antibody or functional parts thereof, which exhibits high specificity to APi-}2 monomeric peptides but show^s essentially no or only minor cross-reactivity to Aμ .ss. AP1.39, Api_4o, and/or Ap 1^1 monomeric peptides, particularly an antibody, but especially a monoclonal antibody, including any functionally equivalent antibody or functional parts thereof, which antibody is up to 100 fold, particularly 50 to 100 fold, more particularly 80 to 100 fold, but especially 100 fold more sensitive to amyloid peptide Api^2 as compared to Api.38, Apvas, Apuo, Api^i and up to 1000 fold, particularly 500 to 1000 fold, more particularly 800 to 1000 fold, but especially 1000 fold more sensitive to amyloid peptide Api^2 as compared to Api.38, and thus capable of Inhibiting, in vitro and In vivo, the aggregation of amyloidogenic monorrreric pe^tidesi t>ut especially of amyloid peptide Apiw(2 -.^ ^- - In another specific embodiment of the invention an antibody, particularly a bifunctional antibody, but especially a monoclonal antibody, particularly a bifunctional monoclonal antibody, including any functionally equivalent antibody or functional parts thereof, which has a high binding sensitivity to amyloid peptide Api-42 and is capable of detecting Apn2 fibers in a concentration of down to at least 0.001 pg, but particularly in a concentration range of between 0.5 pg and 0.001 pg, more particularly between 0.1 pg and 0.001 pg, but especially in a concentration of 0.001 pg. In a very specific embodiment of the Invention an antibody is provided, particularly a monoclonal antibody, including any functionally equivalent antibody or functional parts thereof, which antibody is capable of detecting AP1-42 fibers down to a minimal concentration of 0,001 pg and APi^o fibers down to a minimal concentration of 0.1 pg and Api.38 fibers down to a minimal concentration of 1 pg amount of fibers. Binding of the antibodies according to the invention and as described herein before to amyloidogenic monomeric peptides but, particularly, to the amyloid form (1-42) leads to an inhibition of aggregation of monomeric amyloidogenic peptides to high molecular fibrils or filaments. Through the inhibition of the aggregation of amyloidogenic monomeric peptides the antibodies according to the present invention are capable of preventing or slowing down the fomriation of amyloid plaques, pamcuiany me amyloid form (1-42), which is know to become insoluble by change of confomiation and to be the major part of amyloid plaques in brains of diseased animals or humans. In a specific embodiment the present invention relates to a monoclonal antibody Including any functionally equivalent antibody or functional parts thereof which antibody has the characteristic properties of an antibody produced by hybridoma ce]f line EJ 7H3, deposited December 08, 2005 as DSM ACC27S6. More particularly, the invention relates to a monoclonal antibody including any functionally equivalent antibody or functional parts thereof produced by hybridoma cell line EJ 7H3, deposited December 08, 2005 as DSM ACC2758. It is also an objective of the present invention to provide a method for preventing, treating or alleviating the effects of amyloidosis, a group of diseases and disorders associated with amyioid plaque formation including secondary amyloidosis and age-related amyloidosis including, but not limited to, neurological disorders such as Alzheimer's Disease (AD), including diseases or conditions characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI), Lewry body dementia, Down's syndrome, hereditary cerebral hemorrhage with amyloidosis (Dutch type); the Guam Parkinson-Dementia complex; as well as other diseases which are based on or associated with amyloid-like proteins such as progressive supranuclear palsy, multiple sclerosis; Creutzfeld Jacob disease, Parkinson's disease, HIV-related dementia, ALS (amyotropic lateral sclerosis). Adult Onset Diabetes; senile cardiac amyloidosis; endocrine tumors, and others, including macular degeneration, but particularly a disease or condition characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI), by administering a supramolecular antigenic constmct according to the present invention, but particularly a vaccine composition comprising such a supramolecular antigenic constructs according to the invention to an animal, particulariy a mammal or a human, affected by such a disorder and thus in need of such a treatment. In another embodiment of the present invention a method is provided for the preparation of a vaccine composition for inducing an immune response in an organism, in particular an animal or human affected by such a disorder, disease or condition and thus in need of such a treatment, for preventing, treating or alleviating the effects of amyloidosis, a group of diseases and disorders associated with amyloid plaque fomiation including secondary amyloidosis and age-related amyloidosis including, but not limited to, neurological disorders such as Alzheimer's Disease (AD), including diseases or conditions characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI), Lewy body dementia, Dowm's syndrome, hereditary cerebra\ hemorrhage with amyloidosis (Dutch type); the Guam Paritinson-Dementia complex; as well as other diseases which are based on or associated with amyloid-like proteins such as progressive supranuclear palsy, multiple sclerosis; Creutzfeld Jacob disease, Parkinson's disease, HIV-related dementia, ALS (amyotropic lateraLsclerosis), -^ Adult Onset Diabetes; senile cardiac amyloidosis; endocrine tumors, and others, including macular degeneration, but particularly a disease or condition characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI) In still a further embodiment of the present invention a method is thus provided for the preparation of a therapeutic vaccine composition for preventing, treating or alleviating the effects of amyloidosis, a group of diseases and disorders associated with amyloid plaque formation including secondary amyloidosis and age-related amyloidosis including, but not limited to, neurological disorders such as Alzheimer's Disease (AD), Including diseases or conditions characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI), Lewy body dementia, Down's syndrome, hereditary cerebral hemorrhage with amyloidosis (Dutch type); the Guam Paritinson-Dementia complex; as well as other diseases which are based on or associated with amyloid-like proteins such as progressive supranuclear palsy, multiple sclerosis; Creutzfeld Jacob disease, Parkinson's disease, HIV-related dementia, ALS (amyotropic lateral sclerosis). Adult Onset Diabetes; senile cardiac amyloidosis; endocrine tumors, and others, including macular degeneration, but particularly a disease or condition characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impaimient (MCI), comprising formulating an antibody according to the invention rn a pharmaceutically acceptable form. In a specific embodiment, the present invention makes use of an antigen presentation that results in enhanced exposure and stabilization of a preferred antigen confomiation, which uftimately leads to a highly specific immune response and results in the generation of antibodies vi/ith unique properties. In one embodiment, the present invention provides immunogenic compositions comprising a supramolecular antigenic construct comprising a p-amyloid peptide antigen according to the invention and as described herein before representative of the N-temninal part of the ^amyloid peptide, vi/hich antigenic peptide Is modrfied such that it is capable of maintaining and stabilizing- a -defined conformation of the antigen, -particularly a conformation which is characterized by a balanced proportion of random coil, a-helical and p-sheet portions. This defined confomiation leads to the induction of a strong and highly specific immune response upon introduction into an animal or a human. In another embodiment of the invention the vaccine composition according to the invention may comprise in addition to an Ap peptide antigen, particularly the Ap peptide antigen of the invention as described herein before, an inhibitor of complement activation. The invention thus relates to a vaccine composition and a method of producing such a composition for the treatment of diseases and disorders which are caused by or associated with amyloid or amyloid-like proteins including amyloidosis, a group of diseases and disorders associated with amyloid plaque fonnation including secondary amyloidosis and age-related amyloidosis Including, but not limited to, neurological disorders such as Alzheimer's Disease (AD), particularly a disease or condition characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment {MCI) comprising a peptide fragment from the N-terminal part of the Ap peptide, particularly an Ap peptide fragment consisting of a single or repetitive stretch of between 7 and 16 contiguous amino acid residues, especially of between 13 and 16 contiguous amino acid residues, particularly from the N-tem^i^al part of the Ap peptide, but particularly an Ap peptide fragment consisting of amino acid residues selected from the group consisting of residues 1-16, 1-15, 1-14, and 1-13 from the N-terminal part of the Ap peptide, more particularly of residue 1-15 as given in SEQ ID NO: 1, Including functionally equivalent fragments thereof, but especially a Ap peptide - fragment as mentioned herein before attached to, or incorporated or reconstituted in a carrier particle/adjuvant such as, for example, a liposome together with an inhibitor of the complement system, particularly an Inhibitor of the complement pathway selected from the group consisting of soluble versions of membrane regulatory proteins, humanized antibodies to complement proteins, small molecule inhibitors acting at various stages of the complement pathway and human complement regulators expressed In transgenic animals. This contiguous stretch of 13 to 15 amino acid residues may be repeated In the construct according to the invention between 2 and 50 times, particularly between.2 and. . - -30 times, more particularly between 2 and 20 times, even more particularly between 2 and 16 times, but especially between 2 and 10 times. In a specific embcxliment of the invention, the complement activation inhibitor which is a component of the therapeutic vaccine composition as mentioned herein before is a compound selected from the group consisting of soluble human complement Receptor 1, anti- human complement protein C5 such as, for example, a humanized anti C5 monoclonal antibody or a single-chain fragment of a humanized monoclonal antibody, C1-esterase inhibitor-N and Natural human CI Inhibitor. Further comprised by the present invention is a vaccine composition according to the invention as mentioned herein before, comprising in addition to an Ap peptide fragment, particularly the Ap peptide fragment according to the Invention, an allosteric effector of hemoglobin, which once in the red blood cells triggers a decrease of the 02/hemogJobin affinity such that oxygen is released in a regulated manner subsequently to the tissues. The invention thus relates to a vaccine composition and a method of producing such a composition for the treatment of diseases and disorders which are caused by or associated with amyloid or amyloid-like proteins including amyloidosis, a group of diseases and disorders associated with amyloid plaque formation including secondary amyloidosis and age-related amyloidosis including, but not limited to, neurological disorders such as Alzheimer's Disease (AD), particularly a disease or condition characterized by a loss of cognitive memory capacity such as, for example, miJd cognitive impairment (MCI) comprising a peptide fragment from the N-temninal part of the Ap peptide, particularly an Ap peptide fragment consisting of a single or repetitive stretch of between 7 and 16 contiguous amino acid residues, especially of between 13 and 16 contiguous amino acid residues, particularly from the N-terminal part of the A^ peptide, but particularly an A{3 peptide fragment consisting of amino acid residues selected from the group consisting of residues 1-16, 1-15, 1-14, and 1-13 from the N-terminat partof the Ap peptide, more particularly of residue 1-15 as given inSEQ ID NO: 1, Including lunctionally equivalent fragments thereof, but particularly a AP peptide fragment as mentioned herein before which is modified by covalently attached palmitoyi residues at each end-of the peptide to result in between 2 and 4. particularly 4 palmitoyJ, residues, but especially a Ap peptide fragment as mentioned herein before attached to, or incorporated or reconstituted in a carrier particle/adjuvant such as, for example, a liposome together with a compound which triggers a decrease of the 02/hemoglobin af^nity such that oxygen is released subsequently to the organ tissues. This contiguous stretch of 13 to 15 amino acid residues may be repeated in the constnjct according to the invention between 2 and 50 times, particularly between 2 and 30 times, more particularly between 2 and 20 times, even more particularly between 2 and 16 times, but especially between 2 and 10 times. In particular, compounds that can be suitably used within a composition according to the invention are those selected from the group consisting of an antilipidemic drug such as, for example, clofibric acid or bezafibrate including the bezafibrate derivatives LR16 and L35, urea derivatives such as. for example, [2-[4[[{arylamino)carbonyI]-amino]phenoxy]-2-methylpropionic acid, an allosteric effector of haemoglobin. The Oz/^emogtobin affinity modulating compound may further be a compound comprising an anionic ligand for an allosteric site of hemoglobin, wherein the anionic ligand comprises an internal pyrophosphate ring, optionally together with a nontoxic cation such as, for example, Ca^* and Na'. More specifically, the invention relates to a therapeutic vaccine composition according to the Invention as mentioned herein before, comprising in addition to the Ap peptide fragment according to the invention inositol hexaphosphate (IHP) derivatives comprising an interna! pyrophosphate ring, optionally together with a nontoxic cation such as, for example, Ca^* and Na*. In still another embodiment a vaccine composition according to the invention and as mentioned herein before is provided comprising, iii addition to an Ap peptide fragment, particularly the Ap peptide fragment according to the invention, a combination of an inhibitor of the complement activation system, particularly an inhibitor of the complement pathway selected from the group consisting of soluble versions of membrane regulatory proteins, humanized antibodies to complement proteins, small molecule inhibitors acting at-various stages of the complement pathway and.human „ . ^ complement regulators expressed in transgenic animals and an allosteric effector of hemoglobin which reduces the 02/hemoglobin affinity such that more oxygen is released subsequently to the tissues, in a regulated manner. The invention thus further relates to a vaccine composition and a method of producing such a composition for the treatment of diseases and disorders which are caused by or associated with amyloid or amyloid-like proteins including amyloidosis, a group of diseases and disorders associated with amyloid plaque formation Including secondary amyloidosis and age-related amyloidosis including, but not limited to, neurological disorders such as Alzheimer's Disease (AD), particularly a disease or condition characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI) comprising a peptide fragment from the N-terminal part of the Ap peptide, particulariy an Ap peptide fragment consisting of a single or repetitive stretch of between 7 and 16 contiguous amino acid residues, especially of between 13 and 16 contiguous amino acid residues, particularly from the N-terminal part of the Ap peptide, but particularly an Ap peptide fragment consisting of amino acid residues selected from the group consisting of residues 1-16, 1-15, 1-14, and 1-13 from the N-terminal part of the Ap peptide, more particularly of residue 1-15 as given in SEQ ID NO: 1, including functionally equivalent fragments thereof, particularly a Ap peptide fragment as mentioned herein before which is modified by covalently attached palmitoyi residues at each end of the peptide to result in between 2 and 4, particularly 4 palmitoyi residues, but especially a Ap peptide fragment as mentioned herein before attached to, or incorporated or reconstituted in a carrier particle/adjuvant such as, for example, a liposome together with an inhibitor of the complement system, particularly an inhibitor of the complement activation selected from the group consisting of soluble versions of membrane regulatory proteins, humanized antibodies to complement proteins, small molecule inhrbitore acting at various stages of the complement pathway and human complement regulators expressed in transgenic animals and a compound, particulariy an allosteric effector of hemoglobin, which decreases the Oz/hemoglobin affinity such that more oxygen is released subsequently to the tissues, in a regulated manner.. This contiguous stretch of 13 to 15 amino acid residues may be repeated in the cofiStructaccording to the inventiori between 2 and 50 times; partlculafly between 2 and 30 times, more particularly between 2 and 20 times, even more particulariy between 2 and 16 times, but especially between 2 and 10 times. In still another embodiment, a method for the treatment of an amyloid-associated disease or condition is provided comprising administering to an animal, particularly to a mammal, but especially to human suffering from such a disease or condition a therapeutic vaccine composition according to the invention and as described herein before, particularly a vaccine composition comprising an ApMs peptide antigen, more particularly a palmltoylated A^i-is peptide antigen. In a specific embodiment of the invention administration of said vaccine composition results mainly in the generation of antibodies of non-inflammatory subtypes, particularly the non-inflammatory Th2 subtype such as, for example, isotype IgGI and lgG2b. In a further specific embodiment, administration of said vaccine composition results mainly in the generation of antibodies of the T-ce!l independent IgG subclass, particulariy of the lgG3 isotype. In still another embodiment of the invention, administration of said vaccine composition does not lead to a significant increase In Inflammation markers in the brain, particularly of inflammation markers selected from the group consisting of IL-1 p, IL-6, IFN-y and TNFa. in still another embodiment of the invention, administration of said vaccine composition leads to a significant decrease of insoluble, plaque-related- Ap1-40 and Api-42 in the brain. In stifl another embodiment of the invention, administration of said vaccine composition leads to a significant reduction in the level of soluble Api-42 in the brain. In particular, the amyloid-associated disease or condition is one selected from the group consisting of diseases including, but not limited to, neurological disorders such as " Alzhrefmer's Disease (AD),-incfading diseases er conditions characterized-by-a toss of . cognitive memory capacity such as, for example, mild cognitive impairment (MCI), Lewy body dementia, Down's syndrome, hereditary cerebral hemorrhage w/ith amyloidosis (Dutch type); the Guam Parkinson-Dementia complex; as well as other diseases which are based on or associated with amyloid-like proteins such as progressive supranuclear palsy, multiple sclerosis; Creutzfeld Jacob disease, Parkinson's disease, HlV-related dementia, ALS (amyotropic lateral sclerosis), Adult Onset Diabetes; senile cardiac amyloidosis; endocrine tumors, and others, including macular degeneration. More particularly, the amyloid associated disease or condition is Alzheimer's Disease. in still another specific embodiment of the invention, a method for the treatment of an amyloid-associated disease or condition is provided according to the invention and as described herein before, wherein administration of said vaccine composition to an animal, particulariy a mammal or a human, suffering from an amyloid-associated condition characterized by a loss of cognitive memory capacity leads to an increase, particularly to a complete restoration in the retention of cognitive memory capacity. In still another embodiment, a method for the treatment of an amyloid-associated disease or condition is provided comprising administering to an animal, particularly to a mammal, but especially to a human suffering from such a disease or condition, a therapeutic vaccine composition comprising an antigenic construct according to the invention and as described herein before and an inhibitor of the compfement system, wherein said vaccine composition Is particutarly administered such that the complement inhibitor and the antigenic construct are administered concomitantly, intermittently or sequentially. In a specific embodiment, the comptement inhibitor is administered prior to the vaccination with the antigenic construct, particulariy wfthin a time window starting up to 20 hours before the vaccination and ending immediately before the vaccination. In another specific embodiment, the complement Inhibitor Is administered subsequent to the vaccination with the antigenic construct within a time window starting immediately a'fte'rthe vaccinatTdnand ending 1 day-aftervacdne application, In still another embodiment of the invention a method is provided for the preparation of a medicament for the treatment of an amyloid-associated disease or condition comprising using a vaccine composition according to the invention and as described herein before. These and other objects, features and advantages of the present invention will become apparent after a review of the following detailed description of the disclosed embodiment and the appended claims. The terms "polypeptids", "peptide", and "protein", as used herein, are interchangeable and are defined to mean a biomolecule composed of amino acids linked by a peptide bond. The term "peptides," are chains of amino acids (typically L-amino acids) whose alpha carbons are linked through peptide bonds formed by a condensation reaction between the carboxyl group of the alpha carbon of one amino acid and the amino group of the alpha carbon of another amino acid. The terminal amino acid at one end of the chain (i.e., the amino terminal) has a free amino group, while the terminal amino acid at the other end of the chain (I.e., the carboxy terminal) has a free carboxyl group. As such, the term "amino terminus" {abbreviated N-temiinus) refers to the free alpha-amino group on the amino acid at the amino terminal of the peptide, or to the alpha-amino group (imino group when participating in a peptide bond) of an amino acid at any other location within the peptide. Similarly, the term "carboxy terminus" (abbreviated C-terminus) refers to the free carboxyl group on the amino actd at the carboxy terminus of a peptide, or to the carboxyl group of an amino acid at any other location within the peptide. Typically, the amino acids making up a peptide are numbered in order, starting at the amino temninal and increasing in the direction toward the carboxy terminal of the peptide. Thus, when one amino acid is said to 'Yodow" another, that amino acid is positioned closer to the carboxy temiinal of the peptide than the preceding amino acid. The term "residue" is used herein to refer to an amino acid that is incorporated into a peptide by an amide bond. As such, the amino acid may be a naturally occurring amino acid or, unless otherwise limited, may encompass known analogs of natural amino acids that function in a manner similar to the naturally occurring amino acids (i.e., amino acid mimefics). Moreover, an amide bond mimetic includes peptide backbone modifications well known to those skilled in the art. The phrase "consisting essentially of is used herein to exclude any elements that would substantially alter the essential properties of the peptides to which the phrase refers. Thus, the description of a peptide "consisting essentially of . . ," excludes any amino acid substitutions, additions, or deletions that would substantially alter the biological activity of that peptide. Furthermore, one of skill will recognize that, as mentioned above, individual substitutions, deletions or additions which alter, add or delete a single amino acid or a small percentage of amino acids (typically less than 5%, more typically less than 1%) in an encoded sequence are conservatively modified variations where the alterations result in the substitution of an amino acid with a chemically similar amino acid. Conservative substitution tables providing functionally similar amino acids are well known in the art. The following six groups each contain amino acids that are conservative substitutions for one another: 1) Alanine (A), Serine (S), Threonine (T); 2} Aspartic acid (D), Glutamic acid (E); 3) Asparagine (N), Glutamine (Q); 4) Arginine (R), Lysine (K); 5) Isoleucine (I), Leucine (L), Methionine (M), Valine (V); and 6) Phenylalanine (F), Tyrosine (Y), Tryptophan (W). The phrases "isolated" or "biologically pure" refer to material which is substantially or essentially free from components which normally accompany it as found in its native state. Thus, the peptides described herein do not contain materials normally associated with their in situ environment. Typically, the isolated, immunogenic peptides described . ,-. herein are at least about 80% pure, usually at least about 90%, and preferably at least about 95% as measured by band intensity on a sifver stained gel. Protein purity or homogeneity may be indicated by a number of methods well known in the art, such as pofyacrylamide gel electrophoresis of a protein sample, followed by visualization upon staining. For certain purposes high resolution will be needed and HPLC or a similar means for purification utilized. When the immunogenic peptides are relatively short in length (i.e., less than about 50 amino acids), they are often synthesized using standard chemical peptide synthesis techniques. Solid phase synthesis in which the C-terminal amino acid of the sequence is attached to an insoluble support followed by sequential addition of the remaining amino acids in the sequence is a preferred method for the chemical synthesis of the immunogenic peptides described herein. Techniques for solid phase synthesis are known to those skilled in the art. Alternatively, the immunogenic peptides described herein are synthesized using recombinant nucleic acid methodology. Generally, this involves creating a nucleic acid sequence that encodes the peptide, placing the nucleic acid in an expression casseue under the control of a particular promoter, expressing the peptide in a host, isolating the expressed peptide or polypeptide and, if required, renaturing the peptide. Techniques sufficient to guide one of skill through such procedures are found in the literature. Once expressed, recombinant peptides can be purified according to standard procedures, including ammonium sulfate precipitation, affinity columns, column chromatography, gel electrophoresis and the like. Substantially pure compositions of about 50% to 95% homogeneity are preferred, and 80% to 95% or greater homogeneity are most preferred for use as therapeutic agents. One of skill in the art will recognize that after chemical synthesis, biological expression or purification, the immunogenic peptides may possess^a conformation substantially different than the native conformations of the constituent peptides. In this case, it is often necessary to denature and reduce the antiproliferafive peptide and then to cause the peptide to re~foid into the preferred conformation. Methods of reducing and denaturing proteins and inducing re-folding are well known to those of skill in the art. Antigenicity of the purified protein may be confirmed, for example, by demonstrating reaction with immune serum, or with antisera produced against the protein itself. The terms "a", "an" and "the" as used herein are defined to mean "one or more" and include the plural unless the context is inappropriate. The terms "detecting" or "detected" as used herein mean using known techniques for detection of biologic molecules such as immunochemical or histological methods and refer to qualitatively or quantitatively determining the presence or concentration of the biomolecute under investigation. By "isolated" is meant a biological molecule free from at least some of the components with which it naturally occurs. The terms "antibody" or "antibodies" as used herein is an art recognized term and is understood to refer to molecules or active fragments of molecules that bind to known antigens, particularly to immunoglobulin molecules and to immunologically active portions of immunoglobulin molecules, i.e molecules that contain a binding site that immunospecifically binds an antigen. The immunogtobulin according to the invention can be of any type (IgG, IgM, IgD, IgE, IgA and IgY) or class (lgG1, lgG2, lgG3, lgG4, lgA1 and lgA2) or subclasses of immunoglobulin molecule. "Antibodies" are intended within the scope of the present invention to include monoclonal antibodies, polyclonal, chimeric, single chain, bispecific, simianized, human and humanized antibodies as well as active fragments thereof. Examples of active fragments of molecules that bind to known antigens include Fab and F(ab')2 fragments, including the products of an Fab immunoglobulin expression library and epitope-binding , -. fragments of any of the antibodies and fragments mentioned above. These active fragments can be derived from an antibody of the present invention by a number of techniques. For example, purified monoclonal antibodies can be cleaved with an enzyme, such as pepsin, and subjected to HPLC gel filtration. The appropriate fraction containing Fab fragments can then be collected and concentrated by membrane filtration and the iik&. For furtfier description of general techniques for the isolation of active fragments of antibodies, see for example, Khaw, B. A. et al. J. Nucl. Med. 23:1011-1019 (1982); Rousseaux et al. Methods Enzymology. 121:663-69, Academic Press, 1986. A "humanized antibody" refers to a type of engineered antibody having its CDRs derived from a non-human donor immunoglobulin, the remaining immunoglobulin-derived parts of the molecule being derived from one {or more) human immunoglobulin(s). In addition, frameworl Functionally equivalent antibody" is understood-within the scope of the present invention to refer to an antibody which substantially shares at least one major functional property with an antibody mentioned above and herein described comprising: binding specificity to the p-amyloid protein, particularly to the Api.42 protein, and more particularty to the 4-16 epitopic region of the Api^2 protein, immunoreactivity in vitro, inhibition of aggregation of the APi-t2 monomers Into high molecular polymeric fibrils and/or disaggregation of preformed Api-42 polymeric fibrils, and/or a p-sheet breaking property and alleviating the effects of disorders associated with amyloidosis, a group of diseases and disorders associated with amyloid plaque formation including secondary amyloidosis and age-related amyloidosis including, but not limited to, neurological disorders such as Alzheimer's Disease (AD), including diseases or conditions characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI), Levi^ body dementia, Down's syndrome, hereditary cerebral hemorrhage with amyloidosis (Dutch type); the Guam Parkinson-Dementia complex; as well as other diseases which are based on or associated with amyloid-like proteins such as progressive supranuclear palsy, multiple sclerosis; Creutzfeld Jacob disease, Parkinson's disease, HIV-related dementia, ALS (amyotropic lateral sclerosis), Adult Onset Diabetes; senile cardiac amyloidosis; endocrine tumors, and others, including macular degeneration., when administered prophylactically or therapeutically. The antibodies can be of any class such as IgG, IgM, or IgA, etc or any subclass such as lgG1, lgG2a, etc and other subclasses mentioned herein above or known in the art. Further, the antibodies can be produced by any method, such as phage display, or produced in any organism or cell line, including bacteria, insect, mammal or other type of cell or cell line which produces antibodies with desired characteristics, such as humanized antibodies. The antibodies can also be formed by combining a Fab portion and an Fc region from different species. The term "antigen" refers to an entity or fragnwnt thereof which can induce an immune response in an organism, particularly an animal, more particulariy a mammal including a human. The term includes Immunogens and regions responsible for antigenicity or antigenic detenninants. An immune response occurs when an individual produces sufficient antibodies, T-cells and other reactive immune cells against administered immunogenic compositions of the present invention to moderate or alleviate the disorder to be treated. The term "hybridoma" is art recognized and is understood by those of ordinary skill in the art to refer to a cell produced by the fusion of an antibody-producing cell and an immortal cell, e.g. a multiple myeloma cell. This hybrid cell is capable of producing a continuous supply of antibody. See the definition of "monoclonal antibody" above and the Examples below for a more detailed description of the method of fusion. The tenn "carrier" as used herein means a structure in which antigenic peptide or supramolecuiar construct can be incorporated into or can be associated with, thereby presenting or exposing antigenic peptides or part of the peptide to the immune system of a human or animal. Any particle that can be suitably used in animal or human therapy such as, for example, a vesicle, a particle or a particulate body may be used as a carrier within the context of the present invention. The temi "carrier" further comprises methods of delivery wherein supramoiecular antigenic construct compositions comprising the antigenic peptide may be transported to desired sites by delivery mechanisms. One example of such a delivery system utilizes colloidal metals such as colloidal gold. Camer proteins that can be used in the supramoiecular antigenic construct compositions of the present invention Include, but are not limited to, maltose binding protein "MBP"; bovine serum albumin "BSA"; keyhole lympet hemocyanin "KLH"; ovalbumin; flagellin; thyroglobulin; serum albumin of any species; gamma globulin of any-species; syngeneic cells; syngeneic c^ls bearing la antigens; and,polymers of D-and/or L- amino acids. In the supramoiecular antigenic construct according to the present invention, the liposome may have a dual function in that it can be used as a carrier comprising the supramoiecular constnjct as described herein before and, at the same time, function as an adjuvant to increase or stimulate the immune response within the target animal or human to be treated with the therapeutic vaccine according to the invention. It is also to be understood that the supramoiecular antigenic construct compositions of the present invention can further comprise additional adjuvants including, but not limited to, keyhole limpet hemocyanin (KLH), bovine serum albumin (BSA) and other adjuvants such as, for example, lipid A, alum, calcium phosphate, interleukin 1, and/or microcapsules of polysaccharides and proteins, but particularly a detoxified lipid A, such as monophosphoryl or diphosphoryl lipid A, or alum, further preservatives, diluents, emulsifiers, stabilizers, and other components that are knovm and used in vaccines of the prior art. Moreover, any adjuvant system known in the art can be used in the composition of the present invention. Such adjuvants include, but are not limited to, Freund's incomplete adjuvant, Freund's complete adjuvant, polydispersed B-(1,4) linked acetylated mannan ("Acemannan"), TITERMAX® (polyoxyethylene-potyoxypropylene copolymer adjuvants from CytRx Corporation), modified lipid adjuvants from Chiron Corporation, saponin derivative adjuvants from Cambridge Biotech, killed Bordetella pertussis, the lipopolysaccharide (LPS) of gram-negative bacteria, large polymeric anions such as dextran sulfate, and inorganic gels such as alum, aluminum hydroxide, or aluminum phosphate. Further, the term "effective amount" refers to the amount of antigenic/immunogenic composition which, when administered to a human or animal, elicits an immune response. The effective amount is readily determined by one of skill in the art following routine procedures. The temn "supramolecular antigenic construct" refers to an antigenic constnjct according to the present invention and as described herein t>efore. tn particular, "supramolecular antigenic construct" refers to an antigenic constaict comprising an Ap peptide antigen according to the invention and as describechfterein t>efore, specifically an-Ap peptide -fragment from the N-terminal part of the AP peptide, but particularly an Ap peptide fragment consisting of amino acid residues selected from the group consisting of 1-15, 2-15, 3-15, 1-14, 2-14, 1-13; 1-16(A2), 1-16(A4), 1-16{A5), 1-16(A6), 1-16(A8), 1-16(A9), 1-16(A10); 1-16(A12), 16(A13), 16(A14), 1-16(A15), 1-15(A2), 1-15(A4). 1-15(A5), 1-15(A6), 1-15{A8), 1-15{A9), 1-15(A10); 1-15(A12), 15(A13), 15(A14), particularly an Api-i6(ii5) peptide antigen, more particularly a Api.iewu) or API-I6{AI3) peptide antigen, even more particularly a Api.14 peptide antigen, specifically a Api.15 peptide antigen, but especially an Ap peptide fragment consisting of amino acid residues 1-15 as given in SEQ ID NO; 1, and 1-16(A14) as given in SEQ ID NO: 3, which antigenic peptide is presented attached to, or incorporated or reconstituted in a carrier such as, for example, a vesicle, a particulate body or molecule but, particularly, a liposome. More particularly, the antigenic peptide according to the invention is modified by a lipophilic or hydrophobic moiety, that facilitates insertion into the lipid bilayer of the liposome carrier/immune adjuvant, particularly by a lipophilic or hydrophobic moiety including, but not limited to, a fatty acid, a triglyceride or a phospholipid, but especially a fatty acid, a triglyceride or a phospholipid, wherein the fatty acid carbon back bone has at least 10 carbon atoms which functions as an anchor for the peptide in the liposome bilayer and has a dimension that leads to the peptide being positioned and stabilized in close proximity to the liposome surface. For example, the supramolecular antigenic construct compositions according to the invention may be administered parenterally, but particularly intra-peritoneally, intra-veneously, subcutaneously and intra-muscularly in a range of approximately 1.0 pg to 10.0 mg per patient, though this range is not intended to be limiting. The actual amount of the composition required to elicit an immune response will vary for each individual patient depending on the immunogenicity of the composition administered and on the immune response of the individual. Consequently, the specific amount administered to an individual will be determined by routine experimentation and based upon the training and experience of one skilled in the art. The supramolecular antigenic constructs according to the present invention may be used for the preparation of a vaccine composition for inducing an immune response in an orgariisrhT in particular an animal or human, for preventing, treating or alleviating flie effects of amyloidosis, a group of diseases and disorders associated with amyloid plaque formation including secondary amyloidosis and age-related amyloidosis including, but not limited to, neurological disorders such as Alzheimer's Disease (AD), including diseases or conditions characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI), Lew^ body dementia, Down's syndrome, hereditary cerebral hemon-hage with amyloidosis (Dutch type); the Guam Parltinson-Dementia complex; as well as other diseases which are based on or associated with amyloid-like proteins such as progressive supranuclear palsy, multiple sclerosis; Creutzfeld Jacob disease, Parkinson's disease, H!V-related dementia, ALS (amyotropic lateral sclerosis), Adult Onset Diabetes; senile cardiac amyloidosis; endocrine tumors, and others, including macular degeneration, but particularly a disease or condition characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impain7ient(MCI). It is thus an objective of the present invention to provide a method for preventing, treating or alleviating the effects of amyloidosis, a group of diseases and disorders associated with amyloid plaque formation including secondary amyloidosis and age-related amyloidosis including, but not limited to, neurological disorders such as Alzheimer's Disease (AD), including diseases or conditions characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI), Lewy body dementia, Down's syndrome, hereditary cerebral hemon-hage with amyloidosis (Dutch type); the Guam Parkinson-Dementia complex; as well as other diseases which are based on or associated with amyloid-lilce proteins such as progressive supranuclear paisy, multiple sclerosis; Creutzfeld Jacob disease, Parkinson's disease, HlV-related dementia, ALS (amyotropic lateral sclerosis), Adult Onset Diabetes; senile cardiac amyloidosis; endocrine tumors, and others, including macular degeneration, but particularly a disease or condition characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI), by administering a supramolecular antigenic construct according to the present invention, but particularly a vaccine composition comprising such a supramolecular antigenic constructs according to the invention to a an animal, particularly a mammal or a human, affected by such a disorder and thus in need of such a treatment. In another embodiment of the present invention a method is provided for the preparation of a vaccine composition for inducing an immune response in an organism, in particular an animal or human affected by such a disorder, disease or condition and thus in need of such a treatment, for preventing, treating or alleviating the effects of amyloidosis, a group of diseases and disorders associated with amyloid plaque formation including secondary amyloidosis and age-related amyloidosis including, but not limited to, neurological disorders such as Alzheimer's Disease (AD), including diseases or conditions characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI), Lewy body dementia, Down's syndrome, hereditary cerebral hemorrhage with amyloidosis (Dutch type); the Guam Parkinson-Dementia complex; as well as other diseases which are based on or associated with amyloid-like proteins such as progressive supranuclear palsy, multiple sclerosis; Creutzfeld Jacob disease, Parkinson's disease, HlV-related dementia, ALS (amyotropic lateral sclerosis), Adult Onset Diabetes; senile cardiac amyloidosis; endocrine tumors, and others, including macular degeneration, but particularly a disease or condition characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impaimient (MC!) In still a further embodiment of the present invention a method is thus provided for the preparation of a composition for preventing, treating or alleviating the effects of amyloidosis, a group of diseases and disorders associated with amyloid plaque formation including secondary amyloidosis and age-related amyloidosis including, but not limited to, neurological disorders such as Alzheimer's Disease (AD), including diseases or conditions characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI), Lewy body dementia, Down's syndrome, hereditary cerebral hemorrhage with amyloidosis (Dutch type); the Guam Parkinson-Dementia complex; as welt as other diseases which are based on or associated with amyloid-like proteins such as progressive supranuclear palsy, multiple sclerosis; Creutzfeld Jacob disease, Parkinson's disease, HIV-related dementia, ALS (amyotropic lateral sclerosis), Adult Onset Diabetes; senile cardiac amyloidosis; endocrine tumors, and others, including macular degeneration, but particularly a disease or condition characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impaimnent (MCi), comprising formulating an antibody according .to Jtip_ invention in a pharmaceutically acceptable fomn. In a specific embodiment, the present invention makes use of an antigen presentation that results in enhanced exposure and stabilization of a preferred antigen confonnation, which ultimately leads to a highly specific immune response and results in the generation of antibodies with unique properties. In one embodiment, the present invention provides immunogenic compositions comprising a supramolecular antigenic construct comprising a 3-amyloid peptide antigen according to the invention and as described herein before representative of the N-temiinal part of the P-amyloid peptide, which antigenic peptide is modified such that it is capable of maintaining and stabilizing a defined confonnation of the antigen, particularly a conformation which is characterized by a balanced proportion of random coil, a-helical and g-sheet portions. This defined conformation leads to the induction of a strong and highly specific immune response upon introduction into an animal or a human. One way of achieving the formation and stabilization of the desired conformation of the antigenic peptide is by presenting the antigenic peptide attached to, or incorporated or reconstituted, partially or fully, into a carrier such as, for example, a vesicle, a particulate body or molecule or any other means that can suitably serve as a carrier/adjuvant for the antigenic peptide. In a specific embodiment of the invention, the antigenic peptide is attached to, or incorporated or reconstituted in the carrier through weak interactions such as, for example, van der Waal's, hydrophobic or electrostatic interaction, or a combination of two or more of said interactions, such that the peptide is presented with a specific conformation, which is maintained and stabilized by restricting said antigenic peptide in its three dimensional freedom of movement so that conformational changes are prevented or severely restricted. comprised in the antigenic peptide. This results in a presentation of the antigenic construct such that is freely accessible to the immune defense machinery of the target organism and thus capable of inducing a strong and highly specific immunogenic response upon administration to an animal or a human. The immunogenic response may be further increased by using a liposome as a carrier, which liposome may function as an adjuvant to increase or stimulate the immune response within the target animal or human to be treated with the therapeutic vaccine according to the invention. Optionally, the liposome may, in addition, contain a further adjuvant such as, for example, lipid A, alum, calcium phosphate, interleukin 1, and/or microcapsules of polysaccharides and proteins, but particularly a detoxified lipid A, such as monophosphoryl or diphosphoryl lipid A, or alum. in a specific embddiftiehT'of the invention an antigenic peptide according to the invention and described herein before, particularly an antigenic peptide the overall net charge of which is negative, is used reconstituted in a liposome, particularly a liposome the constituents of which are chosen such that the net overall charge of the liposome head group Is negative. In particular, the liposome is composed of constituents selected from the group consisting of dimyristoyl phosphatidyl choline (DMPC), dimyristoyi phosphatidyl ethanolamine (DMPEA), dimyristoyl phosphatidyl glycerol (DMPG) and cholesterol and, optionally, further contains monophosphoryl lipid A or any other adjuvant that can be suitably used within the scope of the present invention such as, for example, alum, calcium phosphate, interleukin 1, and/or microcapsules of polysaccharides and proteins. In another specific embodiment of the invention a modified peptide antigen according to the invention and as described herein before is provided covalently bound to an anchor-type molecule which is capable of inserting into the carrier/adjuvant thereby fixing the peptide to the carrier/adjuvant and presenting it on or in close proximity to the surface of a carrier/adjuvant molecule such that electrostatic forces can become effective as described herein before. When liposomes are used as a carrier/adjuvant, the antigenic peptide construct generally has a hydrophobic tail that inserts into the liposome membrane as it is formed. Additionally, antigenic peptides can be modified to contain a hydrophobic tail so that it can be inserted into the liposome. The supramolecular antigenic constructs of the present invention generally comprise peptides modified to enhance antigenic effect wherein such peptides may be modified via pegylation (using polyethylene glycol or modified polyethylene glycol), or modified via other methods such by palmitic acid as described herein before, poly-amino acids (eg poly-glycine, poly-histidine), poly-saccharides (eg poiygalacturon'tc acid, polylactic acid, polyglycolide, chitin, chitosan), synthetic polymers (polyamides, polyurethanes, polyesters) or co-polymers (eg. poly(methacrylic acid) and N-(2-hydroxy) propyl methacrylamide) and the like. Palmitoylation, while providing an anchor for the peptide in the liposome bilayer, due to the relative reduced length of the Ci6:o fatty acid moiety leads to the peptide being presented exposed on or in close proximity to the liposome surface. Therefore, the cells processing the antigen will have to take up the entire liposome with the peptide. In another embodiment of the invention, PEG is used in the preparation of a supramolecular construct, wherein the free PEG terminus is covalently attached to a molecule of phosphatidylethanolamine (where the fatty acid can be: myristic, palmitic, stearic, oleic etc. or combination thereof). This suprafr)o\ecuiar structure may be reconstituted in liposomes consisting of phospholipids and cholesterol (phosphatidytethanol amine, phosphatidyl glycerol, cholesterol in varied mo\ar ratios, Other phospholipids can be used. Lipid A Is used at a concentration of approximately 40 pg/pmole of phospholipids. Yet another object of the present invention is to provide vaccine compositions comprising supramolecular antigenic constructs comprising an antigenic peptide according to the Invention and as described herein before, w/hich peptide is modified so as to enhance the antigenic effect wherein such peptide, particularly an A^ peptide fragment from the N-terminal part of the A|3 peptide, but particularly an A^ peptide fragment consisting of amino acid residues selected from the group consisting of 1-15,. 2-15, 3-15, 1-14, 2-14, 1-13; M6(A2). 1-16{A4), 1-16(A5), 1-16(A6), 1-16{A8), 1-16(A9), 1-16{A10); 1-16(A12), 16(A13), 16(A14), 1-16(A15), 1.15(A2), 1-15(A4), 1-15(A5), 1-15(A6), 1-15{A8), 1-15(A9), 1-15(A10); 1-15(A12), 15(A13), 15(A14). an APi.i6(ii5) peptide antigen, more particularly a Api.i6(ai4) or APi.i6(ai3) peptide antigen, even more particularly a A^i.u peptide antigen, specifically a ApMg peptide antigen, but especially an Ap peptide fragment consisting of amino acid residues 1-15 as given in SEQ ID NO: 1, and 1-16(A14) as given in SEQ ID NO: 3, is modified via pegylation (using polyethylene glycol or modified polyethylene glycol), or modified via other methods such by poly-amino acids (e.g. poly-glycine, poly-histidine), poly-saccharides (e.g. polygalacturonic acid, polylactic acid, polyglycolide, chitin, chitosan), synthetic polymers (polyamides, polyurethanes, polyesters) or co-polymers (poly(methacrylic acid) and N-(2-hydroxy) propyl methacrylamide) and the like. Liposomes that can be used in the compositions of the present invention include those known to one skilled in the art. Any of the standard lipids useful for making liposomes may be used. Standard bilayer and multi-layer liposomes may be used to make compositions of the present invention. While any method of making liposomes known to one skilled in the art may be used, the most preferred liposomes are made according to the method of Alving et al.. Infect. Immun. 60:2438-2444, 1992, hereby incorporated by reference. The liposome can optionally contain an adjuvant or and immunomodulator or both. A preferred immunomodulator is lipid A, particularly a detoxified lipid A such as, for example, monophosphoryl or diphosphoryl lipid A. The liposome may have a dual function in that it can be used as a carrier comprising the supramolecular construct as described herein before and, at the same time, function as an adjuvant to increase or stimulate the imnnune response within the target animal or human to be treated with the therapeutic vaccine according to the invention. Optionally, the liposome may, in addition, contain a further adjuvant or and immunomodulator or both such as, for example, lipid A, alum, calcium phosphate, interieukin 1. and/or microcapsules of polysaccharides and proteins, but particularly a lipid A, more particularly a detoxified lipid A, such as monophosphoryl or dlphosphoryl lipid A, or alum. In particular, age-related amyloidosis including neurological disorders such as Alzheimer's Disease (AD), including diseases or conditions characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI), Lewy body dementia, Down's syndrome, hereditary cerebral hemorrhage with amyloidosis (Dutch type); the Guam Parkinson-Dementia complex; as well as other diseases w^ich are based on oi^ associated with amyloid*-like-proteins such as progressive supranuclear palsy, multiple sclerosis; Creutzfeld Jacob disease, Parkinson's disease, HlV-related dementia, ALS (amyotropic lateral sclerosis). Adult Onset Diabetes; senile candiac amyloidosis; endocrine tunnors, and others, including macular degeneration, but particularly a disease or condition characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment {MCI), is treated by administering a supramolecular antigenic construct according to the present invention, but particularly a vaccine composition comprising such a supramolecular antigenic constmcts according to the invention to a an animal, particularly a mammal or a human, affected by such a disorder and thus in need of such a treatment but especially Alzheimer's Disease, the symptomatic manifestation of which Is evidenced by a mild forgetfulness up to a total loss of memory. The composition of the present invention comprising a supramolecular antigenic construct according to the invention and as described herein before may be prepared In the form of a liquid solution, or of an injectable suspension, or else in a solid fomi suitable for solubilization prior to Injection in the context of, for example, a kit for making use of the present composition, as described below. The composition of the present Invention comprising a supramolecular antigenic construct is administered to a human or animal suffering from an amyloid-associated In particular, the antigenic peptide composition according to the invention is administered by parenteral, particularly by intra-peritoneal, intraveneous, subcutaneous and jntra-muscular injection. The dosage of the composition will depend on the condition being treated, the particular composition used, and other clinical factors such as weight, size and condition of the patient, body surface area, the particular compound or composition to l^e administered, other drugs being administered concurently, and the route of administration. The therapeutic vaccine composition according to the invention may be administered in combination with other biologically active substances and procedures for the treatment of diseases. The other biologically active substances may be part of the same composition already comprising the therapeutic vaccine according to the invention, in form of a mixture, wherein the therapeutic vaccine and the other biologically active substance are intermixed in or with the same pharmaceutically acceptable solvent and/or carrier or may be provided separately as part of a separate compositions, which may be offered separately or together in form a kit of parts. The therapeutic vaccine composition accorcling to the invention may be administered concomitantly v^rith the other biologically active substance or substances, intermittently or sequentially. For example, the therapeutic vaccine composition according to the invention may be administered simultaneously with a first additional biologically active substance or sequentially after or before administration of the therapeutic vaccine. If an application scheme is chosen where more than one additional biologically active substance are administered together with the at least one therapeutic vaccine according to the invention, the compounds or substances may partially be administered simultaneously, partially sequentially in various combinations. It is another object of the present invention to provide for mixtures of a therapeutic vaccine according to the invention and, optionally, one or more further biologically active substances, as well as to methods of using a therapeutic vaccine according to the .. . invention, or mixtures thereof including compositions comprising said therapeutic vaccine or mixtures of therapeutic vaccines for the prevention and/or therapeutic treatment and/or alleviation of the effects of amyloidoses, a group of diseases and disorders associated with amyloid plaque fomiation including secondary amyloidoses and age-related amyloidoses such as diseases including, but not limited to, neurological disorders such as Alzheimer's Disease (AD), including diseases or conditions characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI), Lewy body dementia, Down's syndrome, hereditary cerebral hemorrhage with amyloidosis {Dutch type); the Guam Parkinson-Dementia complex; as well as other diseases which are based on or associated with amyloid-like proteins such as progressive supranuclear palsy, multiple sclerosis; Creutzfeld Jacob disease, Parkinson's disease, HIV-related dementia, ALS (amyotropic lateral sclerosis). Adult Onset Diabetes; senile cardiac amyloidosis; endocrine tumors, and others, including macular degeneration. The mixtures according to the invention may comprise, in addition to a therapeutic vaccine according to the invention, a biologically active substance such as, for example, known compounds used in the medication of amyloidoses, a group of diseases and disorders associated with amyloid or amyloid-like protein such as the Ap protein involved in Alzheimer's Disease including an antibody raised against an immunogenic peptide antigen, particularly an antibody raised against an immunogenic antigen presented in forni of a supramolecufar antigenic construct, more particularly an antibody according to the present invention and as disclosed herein. In another embodiment of the invention, the other biologically active substance or compound may also be a therapeutic agent that may be used in the treatment of diseases and disorders which are caused by or associated with amyloid or amyloid-like proteins including amyloidosis caused by amyloid p or may be used in the medication of other neurological disorders. The other biologically active substance or compound may exert Its biological effect by the same or a simiiar mechanism as the therapeutic vaccine according to the invention or by an unrelated meciranism of action or by a multiplicity of related and/or unrelated _^, _. mechanisms of action. Generally, the other biologically active compound may include neutron-transmission enhancers, psychotherapeutic drugs, acetylcholine esterase inhibitors, calcium-channel blockers, biogenic amines, benzodiazepine tranquillizers, acetylcholine synthesis, storage or release enhancers, acetylcholine postsynaptic receptor agonists, monoamine oxidase-A or -B inhibitors, N-methyl-D-aspartate glutamate receptor antagonists, nonsteroidal anti-inflammatory drugs, antioxidants, and serotonergic receptor antagonists. In particular, the mixture according to the invention may comprise at least one other biologically active compound selected from the group consisting of compounds against oxidative stress, anti-apoptotic compounds, metal chelators, inhibitors of DNA repair such as pirenzepin and metabolites, 3-amino-1-propanesulfonlc acid (SAPS), 1,3-propanedisulfonate (1,3PDS), secretase activators, P- and y -secretase inhibitors, tau proteins, neurotransmitter, p-sheet breakers, anti-inflammatory molecules, or cholinesterase inhibitors (ChEls) such as tacrine, rivastigmine, donepezil, and/or galantamine and other drugs and nutritive supplements, together Vi^ith an therapeutic vaccine according to the invention and, optionally, a pharmaceutically acceptable carrier and/or a diluent and/or an excipient. In a further embodiment, the mixtures according to the invention may comprise niacin or memantine together with a therapeutic vaccine according to the invention and, optionally, a pharmaceutically acceptable carrier and/or a diluent and/or an excipient. In still another embodiment of the invention mixtures are provided that comprise "atypical antipsychotics" such as, for example clozapine, ziprasidone, risperidone, aripiprazole or olanzapine for the treatment of positive and negative psychotic symptoms including hallucinations, delusions, thought disorders (manifested by marked incoherence, derailment, tangential*^), and bizarre or disorganized behavior, as well as anhedonia, flattened affect, apathy, and social withdrawal, together with an therapeutic vaccine according to the Invention and, optionally, a pharmaceutically acceptable carrier and/or a diluent and/or an excipient. In a specific embodiment of the invention, the compositions and mixtures according to the invention and as described herein before comprise the vaccine according to the invention and the biologically active substance, respectively, in a therapeutically or prophylactically effective amount. Other compounds that can be suitably used in mixtures in combination with the vaccine according to the invention are described, for example, in WO 2004/058258 (see especially pages 16 and 17) including therapeutic drug targets (page 36-39), alkanesulfonic acids and alkanolsulfuric acid (pages 39-51), cholinesterase inhibitors (pages 51-56), NMDA receptor antagonists (pages 56-58), estrogens (pages 58-59), non-steroidal anti-inflammatory drugs (pages 60-61), antioxidants (pages 61-62), peroxisome prol iterators-activated receptors (PPAR) agonists (pages 63-67), cholesterol-lowering agents (pages 68-75); amyloid inhibitors (pages 75-77), amyloid formation inhibitors (pages 77-78), metal chelators (pages 78-79), anti-psychotics and anti-depressants (pages 80-82), nutritional supplements (pages 83-89) and compounds increasing the availability of biologically active substances in the brain (see pages 89-93) and prodrugs (pages 93 and 94 ), which document is incorporated herein by reference, but especially the compounds mentioned on the pages indicated above. It is long known that vaccination of an animal or human host with a nomial host protein may lead to the development of auto-anflbodies directed against the host protein resulting in disorders collectively known as autoimmune disorders. A|5 and its APP precursor protein are such nornial proteins. Using these host proteins in a vaccination thus has the potential of creating undesired side-effects. There is some evidence in the literature that Ap may activate a neuroinflammatory response which may partly be caused by an overactivation of the complement system, which is already highly activated in patients suffering from Alzheimer's Disease or other neurodegenerative diseases. Human Ap in Its p-sheet conformation is a powerful activator of the human complement system. It strongly binds to the collagen tall of the human complement Clq. Overactivation of the complement System can result in the host's natural defense system turning around and leading to autodestructton of cells and tissues including neurons and their processes. For example, the membrane attack complex (MAC) which is part of the host's natural defense system and protects the host against invading bacteria and viruses by inserting itself into said bacteria and viruses, upon overactivation can insert itself into host cells and cause autodistmction. Overactivation may further lead to the stimulation of microglia to produce toxic compounds such as oxygen-free radicals and harmful proteases. It is thus a further object of the present invention to prevent potential side effects such as neurological complications caused by vaccinating an animal or a human suffering from an autoimmune disease with an autoantigen, which has the potential to further stimulate an already over-activated complement system. This can be achieved within the scope of the present Invention by administering an Ap peptide antigen, particularly a palmitoylated Ap peptide antigen, more particularly the palmitoylated APi.15 peptide antigen, but especially the palmitoylated Api-15 peptide antigen {ACI-24, Apvis) in combination with a complement inhibitor. It is thus another embodiment of the invention to provide a vaccine composition comprising in addition to an Ap peptide antigen, particularty the Ap peptide antigen according to the invention and described herein before; an inhibitor of the comptement system. The complement inhibitor may be a compound selected from the group consisting of soluble human complement Receptor 1, anti- human complement protein C5 such as, for example, a humanized anti C5 monoclonal antibody or a single-chain fragment of a humanized monoclonal antibody, Cl-esterase inhibitor-N and Natural human C1 Inhibitor. Recent emphasis on co / morbidity of Ap and cerebralvascular disease, the link between Ap and atherosclerosis, cognitive impairment associated with amyloid angiopathy, significant cerebral microvascular pathology, and deficient clearance of Ap across the Blood Brain Batter in Alzheimer's-Disease, aJI indicate thatvascuiar-disorder is an important feature of chronic neurodegeneration condition In Alzheimer's Disease. (ZIolcovic, B.: (2005) Trends in Neuroscrences 28, 202-208) Therefore, neurovascular dysfunction could have a major role in the pathogenesis of Alzheimer's Disease. There is ample evidence of a strong association between cognitive decline in Alzheimer's Disease and cerebrovascular disorder (Torre, de la, J. C; (2004) Neurol. Res. 26, 517-524, Gorelick, P. B.: (2004) Stroke 35, 2620-2622). Reduced microvascular density, increased numbers of fragmented vessels, marked changed of vessel diameters, etc. have been described in Alzheimer's Disease (Baliey, T. L. et al: (2004) Neurol. Res, 26, 573-578 Farkas, E., and Luiten, P. G.: (2001) Prof. Neurobiol. 64.575-611). Several studies, including the large population-based Rotterdam study (Greenberg, S. M et al: (2004) Stroke 35, 2616-2619) have shown that vascular risk factors might be responsible for cognitive decline in the elderly - leading to so-called "vascular dementia". Several risk factors for Alzheimer's Disease and vascular dementia overlap, including transient ischemia attacks, atherosclerosis, cardiac disease, high serum viscosity etc. Vascular dementia occurs as a result of damage to brain tissue following oxygen deprivation caused by narrowed or blocked blood vessels in the brain and it is the second most frequent form of dementia, Palients frequently suffer form both Alzheimer's Dis&ase and vascular dementia. It is estimated that 17 million people in ttie EU and 55.000 people in \\\& USA suffer from vascular dementia. A therapy restoring normal Oj - pressure in tfie brain, despite blood flow impairmerit has tfie potentra/ of srgnrfrt^nC/y rnfltiendng (he evofulron of Aizhermefs Orsease and reducing dramatically vascular dementia. It is thus still another embodiment of the invention to provide a vaccine composition v^ich comprises in addition to an A0 peptide antigen, particularly the A|3 peptide antigen according to the invention and as described herein before, a compound which triggers a decrease of the Oi/hemogiobin affinity such that oxygen is released subseiifaent/y to the organ tissues. In particular, the Oj/hemoglobin affinity modula^ng compound may be a compound selected from the group consisting of an antilipidemic drug such as, for example, clofibric acid or beiafibrate including the bezafibrate derivatives LR15 and L35, urea derivatives such as, for example, [2-[4[l(arylamino)carbonyl]^amino]phenoxy]-2-methylpropionic acid, an allosleric effector of haemoglobin such as, for example, 2,3-dipUosphoglycerate (DPG), inositol hexak/sphosphate (\HP), and pyrtdoxa* phosphate. More particularly, the O^/hemoglobln affinity modulating compound may be a compound comprising an anioriic ligand for an allosleric site of hemoglobin, wherein the anionic ligand comprises an internal pyrophosphate ring, optionally together with a nontoxic cation. Even more particu(arfy, the 0?/hemogEobin affinrty moduiating compound is a inositol hexapnosphats OHP) dehvstrve corr^hsing at ieast ore interna} pyropho^pl^ate ring, optionally together witti a nontoxic cation. In order to capture the beneficial effects offered by a complement inhibitor anci a 0?/hemoglobin affinity modulating compound in alleviating the potentially hamiful effects of an overactivated complement system and cerebrovascular disorders, respectively, the present invention provides a vaccine composition wherein an Ap peptide antigen, particulariy the A^ peptide antigen according to the Invention and described herein before, is comprised jn combination with an inhibitor of the complement system and an 0?/hemogiobin affinity modulating compound, particularly an allosteric effector of hemoglobin. The vaccine composition according to the inveritfon comprising an A|3 peptide antigen, particularly the A^ peptide antigen according to the indention and described hefein t>efore, may be* administered concomitantly, intemiittently or sequentially with a* complement inhibitor and/or an O^hemoglobin afTinity modulating compound to alleviate the potentially harmful effects of an overactlvated complement system and cerebrovascular disorders, respectively. ^°^ example, the vaccine composition according to the inventiori may be administered simultaneously with a complement .. inhibitor or sequentiaiiy after or before admirtistrathn of the vaccine. ?f an application scheme is chosen v^here a complement inhibitor and a O^/hemoglobin affinity mociutating compound, particularly an alfosteric effector of hemoglobin, are administered together with the at least one vaccine according to the invention, the compounds or substances may partially be administered simultaneousfy, partially sequentially in various combinations. It is another object of the present invention to provide for mixtures of a vaccine according to the invention and a complement inhibitor and/or a O^/hemogiobin affinity (T^oduiating compound, particuiariy an sliostsric effector of hemogtobin, as weii as for methods of using a vaccine according to the invention, or mi>ttures thereof including compositions comprising said vaccine OF mixtures of a vaccine according to the invention arid a complement inhibitor and/or a O^/hemoglobiri affinity modulating compound, particularly an aliosleric effector of hemoglobin, for the prevention and/or therapeutic treatment and/or alleviation of the effects of amyloidoses, a group of diseases and disorders associated with amyloid plaque fonnation including secondary amyJoJdDses and age-rented amyJoidoses such as diseases jndudinp, but not limited to, neurological disonJers such as Alzheimer's Disease (Alzheimer's Disease), Lewy body dementia, Down's syndrome, hereditary cerebra/ hemorrhage with amyloidosis (Dutch type); the Guam Parkin son-Dementia complex; as well as other diseases which are based on or associated with amytoid-iike proteins such as progressive supranuctear palsy, murtrpte sderosrs; CreutrfeW Jacob draease, Parkinson's cjrsease. H^V-related dementia, ALS (amyotropic lateral sclerosis), Adu}t Onset D/abetes; senile cardiac amyloidosis; er:docriPe tumors. anO offers, induding macu)ar d^generaiion. The modified amyloid 1-15 peptide may be synthesized following l^e method reported in Nicolau et. ai. (2002) Proc Natl. Acad. Sci USA 99, 2332-2337. Ttie approach reported in Nicoiau et a1 involves modifying the ar^tigenic peptide by an on-resin grafting of a lipophilic or hydrophobic moiety, to the terminal amino acid residues of a pre-fomned peptide. In particular, a protected amino acid, particularly a Fmoc-protected amino acid, is attached to a resin using known coupling chemistry. The protecting group is removed and a second protected airiino acid reaidud coupled. Standard automated peptide synthesis using knoWh protection chemistry,-particularly Fmoc/IBu chemistry, and standard side-chain protecting groups are then used to synthesis the A^ antigenic peptide, parttcufarly the Apvi5 antigenic peptide by coupling on amino acids 1 to 15 of amytaid pn3tern ABi-42-to produce the peptide fragment wrfh a sequence given in SEQ \D NO:1. in a final step two further protected amino acids are couplsd fo the growng peptide fragment. The Mrt groups can ihert be selectively cleaved and coupted to ;ialmjiic acid. After washing of the resin, the protecting group is removed and the re&ln Simultaneously cleaved, followed by side-chain deprotections using standard methodobgy. The final product can then be obtained In higfi purity and its identity confirmed by methods known in the art such as, for example, eiectrospray mass spectrometry. The lipophilic or hydrophobic moiety according to the present invention may be a fatty acid, a triglyceride or a phospholipid wherein the fatty acid carbon back bone has at least 10 carbon atoms. Particuiariy, the lipophilic or hydrophobic moiety is a fatty acid with a carbon backbone of at least approximately 14 carbon atoms and up to approximately 24 carbon atoms, with each individual number of carbon atom falling within this range afso being part of the present invention. More particularfy, the fipophific or hydnjphobic moiety has a carbon backbone of at /east 14 carbon atoms, but especia/y 76 carbon atorr^s. Examples of hydn:>pUobic moieties inc\ade, but are not JImlted to, pa*mitlc actd, stearic acid, myris\ic acid, lauric acid, oleic acid. Yindeic acid. and linolenic acid. In a specific embodiment of the present invention the lipophilic or hydrophobic moiety is palmitic acid. Liposoma) antigens according to the invention jinay then be pfGparad sts described in Nicolau et al., 2002. The modified amyioid Ap antigenic peptide, particularly the modified APi.is antigenic peptide may be reconslrtuled in a constnjct consis^ng of liposomes, partlculahy liposomes made of dimynstoyl phosphatidyl choline (DMPC), dimyrisloyi phosphatidyl ethanolamine (DMPEA), dimyristojfl phosphatidyl cjJycerol (DMPG) and cholesterol, optionally containing monophosphoryl lipid A,. In a spacrfic embodiment of the invention iiposomes with iipid A are u&ed as adjuvant to prepare the anti-amyloid vaccine. Dimyristoylphosphatidyl-choline, -glycerol and cholesterol are mixed;' particularly in a molar ratto of 0.9:10:0.7. A strong- . . immunmodulator such as, for example, monophosphoryl lipid A is then added at a suitable cortcentration, perticuiariy at a concentra^on of between 30 and 50 mg per mmol, more particularly at 40 mg per mmol of phospholipids. The modifiad antigenic Ap peptkle is then added at a moiar ratio peptide to phospholipids of between 1:30 and 1:200. particuiarfy at amofarralioof betv^en 1:50 and 1:120, more particiilarly of 1:100. Solvents are rernoved, for example through evaporation, and the resuming film hydrated with sterile buffer solution such as, for example PBS. Liposomes may aiso be prepared by the crossftow injection techniQue as described, for example, in Wagner et al (2002) Journal of Liposome Research Vol 12(3), pp 259 - 270. During the injection of lipid solutions into an aqueous buffer system, lipids tend to fonn "pFecipitates^ followed by self arrangement in vesicles. The obtained vesicle size depends on factors such as lipid concentratbn, sttrnnq rate, injection rate, and the choice of lipids. The preparation system may consist of a crossflow injection module, vessels for the polar phase (e.g. a PBS buffer solution), an ethanol/iipid solution vessel and a pressure device, but particularly a nitrogen pressure device. While the aqueous or po}ar solution is pumped through the crasaflow Injection module the ethanoi/itpid solution is injected into the polar phase with varying pressures applied. For determining Immuogenidty of the modified A(E antigenic construct a suitable animat selected from th€ group consisting of mice. rats, rabbits, pigs, birds, etc, but pamcuiariy mice, especially C57BU6 mice are immunized with ttie antigenic peptide. Immunogenlcity of the antigenic construct is detemitned by probing Sera samples in suitabie time inten/ai^ after immunization u^ing a trnmunoassay such as, for exampie, an ELISA assay: The modified antigenic constrvct, particuiariy ihe palmftoy)ated aniigenic construct ^nd. more particularly, the pa^miloylated Api,i5 construct is used for the immunization of an animal, particularly a mammal or a human, suffering from symptoms associated with amyk^osis. a group of diseases and disorders associated with amyJoid pJaqLPe fomiation including secondary amyiOLdosis and age-related amyic^idosis Including, but hot limited to, neurological disorders such as Alzheimer's Disease (AD), including diseases or conditions characterized by a loss of cognrtive memory capacity such as, for example, n^iid cognitive impairment (MCI), Lewy body dementia, Down's syndnsme, hereditary cerebral hemorrhage with amyloidosis (Dutch type); the Guam Parkinson-Dementia complex; as well as other diseases which are based on or associated with amyloid-like proteins such as progressive supranuclear palsy, multiple sclerosis; Creutzfeld Jacob disease, Parkinson's disease, HIV-related dementia, ALS (amyotropic lateral scierosrsX Adult Onset Diabetes; s&niie candiac amyloidosis; endocrine tumors, and others, Including macular degeneration, but particularly a disease or condition characterized by a loss of cognise memory capacity such as, for example, mild cognitive impairment (MCI) or any other amyloid-associated disease. Tt^e supramolecufar antigenic construct acconding to the present invention, but particularly a vaccine composition comprising such a supra molecular antigenic construct according to the invention Is administered to an animal, particularly a mammal or a human^ by any appropriate standard routes of administration, tn general, the composition may be aciministered by topical, oral, rectal, nasal or parenteral (for example, intravenous, subcutaneous, or intramuscular) routes. In addition, the composition may t>e incorporated into sustained release matrices such as biodegradabie polymers, the polymers being implanted in the vicinity of where delivery is desired, for example, at the site of a tumor. The method includes administration of a single dose, administration of repealed doses at predetsrmined time intervals, and sustained adminislratton for a predetermined period of time. !n a specific embodiment of the invention ttie antigenic construct according to the invention, particularly a vaccine composition comprising said antigenic constmct in a pharmaceutically acceptable form, is administered in repeated doses, in particular in 1 to 15 doses, more particUarly in 2 to 10 doses, more particularly in 3 to 7 doses and even more particularty in 4 to 6 doses, in time intervals of between 1 and 10 weeks, particularly tn time intervals of between 1 and 6 tveetca, more partrco/arfy in time intervals of between ^ and 4 weeks, and even more particularly in time intervals of between 2 and 3 weeks. The immune response is monitored by taking Sera samples at a suitable time after boosting, particularty 3 to 10 days after boosting, more particularty 4 to 8 days after bocrating"and more particularly 5 \o 6 days after boosting and ... determining the immunogenicity of the antigenic construct using known methodology, pa^icu^ariy one of the common}y UBsd immunoassays such as, for example, an ELl^A assay lmmuni2ation vk^th the antigenic construct according to the invention, but particuiariy with a vaccine composition comprising the antigenic construct according to the invention in a pharmaceuticafly acceptabfe fomi ieads to a significant and higtify specific immune response in the treaied animal or humaUr The supramoiecuiar antigenic construct compositions of the present invention are administered to a human or animal to induce immunity to antigenic agents such as infectious organisms or to antigenic aspects of other pathological conditions such as p-amybicf aggregation (Alzheimer's Disease) or hyper profiferalive disorders such as cancer The immunized human or animal devetopa circulating antibodies against the infectious organism, thereby reducing or inactivating Its ability to stimulate disease. Tt^e compositions of the present invention may also be used to produce antibodies directed against antigenic peptides. Resulting antibodies are administered to individuals to passively immunize them against a variety of diseases or disorders, including but not amlted to. diseases associated vfith amyloid protein. Thus, in a specific embodiment of the invention, the supra molecular antigenic construct compositions of the present invention are used to produce a panel of monoclonal or polyclonal antibodies that are specific for various disorders, incyding for ewartple, Alzheimer's Disease. Antibodies are made by methods well Known to those of ordinary sklLl in the art. The compositions of the present invention are administered to a human or animal by any appropriate means, preferably by injection. For example, a modified antigenic pepttde reconstituted in liposomes is administared by subcutaneous injection. Whether internally produced or provided from external sources, the circuiating antibodies bind to antigen and reduce or inactivate its ability to stimulate d^&ease. In certain embodiments, the supramolecular antigenic constructs comprise a peptide having the amino acid sequence of P-amyloid. The peptides may also compri&e or correspond to whoie amyloid beta peptide and active fragments thereof. Additionallyn pepti6&& usefu} for the present Invention funher comprise Ap Further provided is a method for producing an antibody including any functionally equivalent antibody or functional parts thereof according to the present Invention, particularly a method for producing a monocbnal antibody including any functionally equivalent antibody or functional parts thereof according to the invention, which method comprises raising antibodies btjt particularly monoclonal antibodies against a supramoiecuJar antigenic construct comprising an antigenic peptide coEresponding to the amino acid sequence of the Ap peptide antigen according to the invention and as described herein before, but particularly an A[31-16(A15) peptide antigen, more partrcularVan A6f-16(i14) orApi-fQ(if3) papt/de antigen, even more parfictvlar^ an Api-14 peptide antigen, but especially the (3-amyloid peptide ApM^, modified with hydrophobic moieties such as, for example,,palmitic acid or a hydrophiiic moiety such as, for example, polyethylene glycol (PEG) or a comt>lnatlon of both, wherein said hydrophobic and hydrophiiic moiety, respectively, is covalentiy bound to each temiinus of the antigenic peptide throjgh at least one, particularly through 1 or 2 amino acids coupled to the terminai amino acid residue at each end of the antigenic peptide, such as. for example, lysine or any other suitable amho add or amino acia anaK^gue cupduit? ui serving as a connecting device fof coupling the hydrophobic and hydrophi/ic moiety to tfj© peptide frsgrnent such as, fof exaropJe, glutamic sad snd oyste^D. The antibody, particularty the monoclonal antibody, obtainable by said method is capable, upon administration to an animal, particularly a mammal or a human, suffering from memory impaimnent, of retaining or increasing the cognitive memory capacity in ibe treated arjimaJ, marrtmal of human. » is a further aspect of the invention io provide an antibody including any functionally equivalent antibody or functional parta thereof, or, more particularly* a monoclonal antibody including any functionally equivalent antibody or functional parts thereof, which has been raised against a supramolecular antigenic construct comprising an antigenic peptide corresponding to the amino acid sequence of the Ap peptide antigen according to the invention and as described herein before, but particularly an Api-16(A15) peptide antigen, more particularly an A|31-16{A14) orApl-16(A13) peptide antigen* even more particulariy an Api-14 peptide antigen, but especially the p-amybid peptide Apiis, modified with a hydrophobic moiety such as, tor example, paimitic acid or a hydrophiffc moiety such as, for exampfe* pofyethytene glycol (PEG) or a combination of both, wherein said hydniiphobic and hydrophiiic moiety, respectrvely, Is covalently bound to each of the termini of the antigenic peptide through an amino acid such as, for example, lysine or any other suitable amino acid or amino acid analogue capable of sen/ing as a linker molecule. When a PEG is used as the hydrophiiic moiety, the free PEG termini are covalently bound to phosphafjdylethanolamine Of any other ^impound suitable to function as the anchoring element for embedding the antigenic construct in the bilayer of a liposome. EXAMPLES EXAMPLE 1: 5)'nthe5» Of tetra{paimitoyi fys'iFieyAp^.is peptide antigen 1.1 Synthesis ProtocoJ V. The palmiloylated amyloid 1-15 peptide was synthesized following an improved previously reported method {Nicolau et. al. 2002). This new approach involved on-resin grafting of palmitic acid to the terminal Lys residues of the pre-formed peptide rather than stepwise sof^d-phase synthesis incorporat^tng the modified ^mino acid F:rtoc- Lys(Pal)-OH. This new approach improtfes coupling efficiency ancf gives a product of consj6erab\y higher purify. Thus, the orihogonalfy protected amino acid Fm(K-Lys(Mn}-OH was attached to a Wang resin using HBTU coupling chemistry. The Fmoc group was removed using 20% piperidine in DMF and a second residue of Fmc^c-Lys(^Att)-OH was coupled. Standard automated peptide synthesis using Fmoc/tBu chemistry and standanJ side-chain protecting groups was then used to coupfe on the neirt 15 amino adds. Fina^y, the Jasl two amino acids coupted were Fmoc-Lys(Mtt>-OH, The Mtt groups were then selectively deaved using 1% TFA in dichloromethane and then coupled to Palmitic acid using HBTU. After resin wash, the Fmoc group was removed with 20% piperidine in N, N-DimethyIfomiamide (DMF) and finally simultaneous resin cleavage and sfde-cha^n deprcifecCions were earned otit ustng TFA under standard condition&. Trituration from cold diethyl ether gave the product as a white solid. Eiectrospray' mass spectrametry confirmed- the identity of the product {m^z expected: 1097,9 ([MISH-); found: 1096.B ([M-3H]3+), with no other tri-, di- or mono-palmrtoylated peptides detected. EXAMPLE 2: Synthasis of N- and C- torminal Upid-PEG ^-amyloid peptide antigen PalmTtoylation, while providing an anchor *or the peptide in the liposome biiayer, due to the relative reduced length of the Cie.o fa^y acid moiety ieads to the peptide practically laying on the Jjposome surface. Therefore. Ihe ceils processing the ar^tigen wiJ) have to take up the entire liposome v^th the peptide, v^ich could result in a slower Innmune response in relative terms. To enhance the immune response, another anchor/spacer has been applied to reconatrtiite tfie peptide in the liposome, e.g. polyethyiene glycol (PEG). PEG was covalently attached to the lysine residue bound at both termini of the peptide. At the other end of the chain (PBCn=7D) phosphatidyl ettiano^ amine (PEA) wae coval&ntiy bound to function as the anchoring element in the liposome bilayer Thus, the liposome still functions as an adjuvant and the peptide being sufticiently far away from the bilayer can be processed alone and thus increases its Immunogenicity as compared to the palmiloyJated anirpen. Methodologies for the mono-psgylation of peptides at the N-a-posltlon are l^nown and wtdefy used. Site-specific mono-pegyiation at internal, N- or C-terminaf amino-acid residues of medium sized peptides has also been described foHowing either solid-phass or peptide-grafting approaches. In orcJer fo avoid prab^ems w/th steric hindrance, the reactran was carried out /n Che solution-phase. This successful approach involved the synthesis of the peptide sequences using standard Fmoc/Su amino acid s^de-chain protections. For those peptide sequences containing internal Lys or His residues (1-16, 1-15), an orthogonally protected LysdvDde} was added to each termini An addition^ Giy was added to ihe C-terminal to facilitate synthesis. The Fmoc group was removed with 20% pipehdine in DMF and N-acetyiated using acetic anhydride. Selective cleavage of the ivDde groups was achieved with 3% hydrazine hydrate in DMF for 1 hrs. The 2-chlorotrityl resin was favored over the more widely used Wang resin since the former proved to be much more resistant to hydrazinolysia. Furthermore, the 2-ch(orafhtyf resin is extremely acid sensitive and thus, un}}ke th& Wang resin, enabies the }&oiation of protected peptides. Indeed, it was necessary to perform the coupling reaction in the solution phase as coupling of the resin-bound peptide to the pre-act*vated pegylaled lipid reagent DSPE-PEG-SPA did not give rise to any coupling product. Thus selective cleavage from the resin under mild conditions (acetic acid/trifluaroethanol/diohloromethane, 1:1:8, 1 hrs. rt} gave the internal^ protected peptides. products before final side-chain deprotections can be achieved by using cation-exchange chromatography. Subsequent peptide side-chain deprotections and separation of the excess quenched DSPE-PEG-SPA leads to the isolation of the desired conjugates with an acceptabte purrfy. Pegylated and Palmitoylated antigens EXAMPLE 3: Structur and Conformation analysis 3.1 Analysis ofoanformation of the reconstittited antcgen To anchor the antigen AB 1-15 on ttie iiposomal surface a palmjtoyialed lysine tandem was used at each end of the peptide as previously described {Nicolau»C.etal, 2002). The fatty acid of the palmitic acid contains 16 carbon atoms which have been shown to have the appropriate length for stable insertion into the liposomal bftayer. In this construct the pept/de is pract/caWy laytng on the surface of the //posome due to the length of the CI 6 fatty acid moiety. In an attempt to have the antigenic peptide associated with liposome-lipid A in a different conformation, another anchor/spacer has been used to reconstitute the peptide Api-16 (ACI-01) in liposomes, namely polyethylene glycol (PEC with 77 repetitive units).The influence of the spacer between the liposomal anchor and the AB peptide on the secondary conformation of the amyloid sequence reconstituted m Itposontes was measured by Circuiar Oichroism (Figure la). The PEGyj3ted Api-16 appears to be in a random coiJ or unstructured protein confomnation (negath/e signal at 210nm and slowly approaching the zero aJcis up to 200nm) v/hereas the palmitoylated peptidfc Ap1-15 contains a significant pn^portion of P-she©t conformation (positive signal up to 210 nm, crossing zero axis then and approaching it again up to 260 nm). It appears therefore that the closer proximity of the paimitoyiated peptide to the {fpasomal surface can impose a defined secondary conformation, This is potentially due to etectrasEatrc interactions of ttie peptide with the liposome surface, which is apparently r^ot possib\e with the PEG)^ted peptide. Z2 gtructure Analysis of paLmitQvlatedP-Amvloid1-1_S reconst^tutod in Liposomes To analyze the influence of drfferenl linker molecules on the conformation of the p-Amyloid 1-15 peptide reconstituted in liposomes a NMR analysis was earned out (Figures lb and 1c). Here palmitoylic acid and polyehtylene glycol (PEG with n=77). respectively, were used as the linker molecule or anchor to the liposome. For NMR studies samples encompassing the palmitoylated amyloid ^-^5 (ACl-24) and pegylated Api_i6 antigen (ACI-01) peptides reconstituted in liposomes were homogenized by vorlexing and the concentration of the solution was increased by centrifugation (3000 rpm for 3*90 minutes at 4"C). and the r&sufting wet peifefs transfen'ed /nto MAS n^tors, Addffiona? samples were prepared by suspending the ACl-01 arvj ACJ-24 peptide pr&par^tions at a cortcentration of ImM in PBS buffer at pH 7.2, as wejj a& a 4 mW soJutJon in the same buffer of ttie peptide sequence without JJrtKer. 10% of DjO were added to each sample. ^H HR-MAS NMR spectra were recorded on a Bruker Avance 500 spectrometer operating at a frequency of 500.13 MHz (11 AT) equipped with a 4mm triple resonance CHI^^CI^H) HR-MAS probe. Each sample was introduced into 4mm ZrOj rotors fitted with SOpL cylindrical inserts. For all NMR experiments samples were spun at a frequency equal to the spectral width (6250Rz) which eliminates spinning sidebands from the spectnjm. The one dimensional proton NMR spectra were acquired with both presaturation and the Watergate sequence (Piotlo.Met af (T992);.Piot(o,M., et af (2005)) and by accuirru^frng 1000-1500 scans. The temperature of the bearing air flowing into the probe was sat to 295K to Insure 29SK in the smnpie. Figures 1 b and 1 c demonstrates the differences in the one dimensional NMR spectra of palmitoylated and pegylated 0-Amyloid peptide. Two significant differences at 9.00 and 8.25 ppm coukJ be obsen/ed. Due to the fact that both peptides have the exactly same amino acid sequence, with the exception of the 16"" Lysine, these differences at 8.00 and 8,25ppm indicate differences in secondary structure because Lysine shouldn't give a positive signal in this spectra area of aromatic annino acid residues. It could be denrionsirated by one-dimensional proton NMR spectra in the area of aromatit amino acid residues ttiat the specific design of the supramoiecular construct according to the pre&ent invention results in a amyloid antigenic peptide with a unique, tiighly specific and significant seconcfary structure when reconstituted in /(posomes, which (Offers with diifersnt ^ker motecutes. This could m&an that the linker / anchor forces and fixes the peptide into a certain or defined secondary structure which is dependent on the used linker molecule, in case of using these molecules as a vaccine for active immunization it is likely thai antibodies raised against these structurally different antigens will be antigen- and confomiation-specific. Previous data obtained by ELISA and ORT (object recognrtion task a cognitive memory test) after/mmunization of APP x PS-t mfce of palmitoy/ated Api.i5 and pegy/ated A|3i-ts antigens (see Example beiow> show that oniy the pa^mitf>yiated antigen restore memory impairment in this Alzheimer's Disea&e disease model although both demonstrated the same immunogentcity. The potential mechanism by which two antigens presenting the same peptide causing in vivo two different functional antibodies, is most likely linked to the different secondary structure of the presented peptide caused by the linker technology. EXAMPLE 4: Quantification of externa)- and Interna J-oriented reconstituted peptide The amount of reconstituted peptide in ACI-01 and ACI-24 was established by a fluorescamine (FLA)-based assay which reacts specifically with primary amines to form high^ fluorescent covalent adducts (Udenfriend, S, et at, 1972). Reaction of FLA with the N-terminuaof thePal1-15 peptide in ACI'24 and with Lys-16 in ACI-01 is anticipated. in order to separate free peptides from those in »ie liposomes, samples were subjected to ultracer^tflfugation and the resuWng supen:atants analyzed for peptkie content using the FLA assay. No free peptktes were delectable in either ACi-01 or ACJ-24 supematanl. Labe/ffig of the pelleted fract'tans with FLA showed very high s&iectivity for reaction whh the peptide in the frposomes both for ACl-24 and ACK01. In order to determine the tofa/ peptide present on the riposome surfaces, fhe essays were repeated in the presence of Triton X-100 (2% in PBS) to disrupt the lipid bifayers. This resulted in a significant increase in labeling; revealing that approxlmaieiy 63 % of peptide is exposed on ttie outer membrane surface. On the other hand, labeling of ACI-01 with FLA only reaches a plateau at 1.2 mM FLA at which concentration the emission is ider^tical when the assay \s performed either in the absence or presence of Triton X-100. This demonstrates that all of the peptide is exposed on the surface of the P&Gyiated v/accir^e ACL-01. EXAMPLE 5: Comparison of ImmunDoenici^ of Pagylated and Palmttoylated Anngem in WiJdtypB C57BU6 mice (ELtSA) Uposoma} antigens were prepared as described (Nico^u et aJ., 2002). The antjgens pegy/ated AB^.I^JAMJ, A04-n arrd palmltoylated Api-ts were reconstituted in a construct consisting of /rposomes made of drmyrrstoy/ ptiosphal/dy/ choline (DMPC), dlmyrtstoyl phosphatidyt ethanofamine (DMPEA), dimyristoyi phosphatidyl gfycerof (DIWPGJ and cholesterol (0.9: 0.1: 0.1: 0.7 molar ratios) containing monophosphoryl lipid A (Sigma-Aldfich, St Louis, MO^ USA) at 40mg/mM phospholipids. The pegylated APMS(4I4). AP ^v and palmrtoylated AP1.15 (ACl-24) antigens were used for the immunization ir C57BU6 mice in 2 week intervals. 10-12 animals were immunized with each antigen. Sera were taken 5 days after the boostings and ELISA were conducted with several dilutions of the sera. Comparative results showing the immunogenicity of the different antigens ar& presented. The ELISA data showed that Hposoma* PEG-Apf^-recdTjj ^ siQnificanDy more immunogenic than pafmlicylafed A^i-is Add/twa/ ALUM d^d not enhance the immunogenicity of P£G-Apvi6CAi4j ^^ the mice. The antibody response induced by P^G-A6A-I \ was slower in comparison to PEG-Ag^i^fiii), Due 10 The quesfian of translation of the faster immune response into a higher memory capacity the pegylaied antigen was compar«] with the palrnitoylated antigen in double transgenrc Al£heinier's Dlseaae mice model. Analtamatl^ method can be iisBd as de&cribad In USS843942 and EP1337322. EXAMPLE 8: Camparison of Immunogftr^lclty of Pagy)ated versus Palmitoylated Antigens in Alzhvimar's Oi3e«BG Mice Model fELlSA) "Young (3-4 morith) female mice were used of a doijbte transgenic mouse strain flxpresaing both mutant human Amyloid Precursor Protein (APP-W171) and mutant human presenilin-l (PSl-A24eE) both under the control of the mouse thyl gene promoter and in F1 (FVB :ejedr All mice iwei"e genot/peO Iwjce durinp their life-span by a second PCR perfonned at the onset of the study, ancj before bhrxj randomization into diff&rent experimental groups. Mice had tree access to water and standard mouse thow (Muracon-G, Trouw Nutrition, Gent. Belgium). Mice were housed under a reversed day-night rhythm in standard metal cages, in accordance with local legcslation on animal wellare. 5 d before the onset of the behavior test, mice were caged in macrolon Type 2 cages and Iransported to the behavior laboratory to acctimatize ana habituate to the Jest-iator&lory environment. Briefly, a three month immunization schedule was installed of six bi-weekly inoculations with ACI-01 and ACI-24. One group of mice received empty liposomes as control, the Mice were habituated for 1 hr to a Plexiglas open-field box (52 x 52 x 40 cm) with black vertical walls and a translucent floor dimly illuminated by a lamp placed underneath the box. The next day the animals were placed in the same box and submitted to a 10 min acquisition trial. During this trial mice were placed individually in the open field in the presence of object A (marble or dice), and the time spent exploring object A (when the animal's snout was directed toward the object at a distance The retention or cognitive memory capacity of APR x PS-1 mice could be significantly increased by immunization with palmitoylated Api-i5 antigen (ACI-24) compared to control treated APP x PS-1 mice (76.1 ± 3,9% versus 49.1 ± 4.5% for control; Table 3). This proves that ACI-24 immunized mice recognized and remembered the original object for at least 3 hours, thereby eliciting that their motivation and their exploration capacity were intact like a healthy age-, gender-, and strain-matched mice, when compared to healthy non-treated and non-transgenic wiidtype mice (61.8 ± 5,1%). Although ACI-01 peptide is only one C-terminal amino acid longer (the 16'^ Lysine) than ACI-24 peptide and only the linker technology is different between these vaccines, immunization with pegylated Api.ie antigen (ACI-01) doesn't demonstrate any memory restoration (45.6 ± 6.2%) comparable to ACI-24. Data are e)cpressed in mean (Ap ng/g brain homogenate ± SEM) The immunization with ACI-24 led to a significant decrease of insoluble, plaque-related-Ap1-40 and Ap1-42. The soluble Ap1-42 levels were also significantly reduced, whereas the levels of soluble Ap't-40 showed only a trend to decrease. Deposit: The following hybridoma cell lines were deposited with the "Deutsche Sammlung von Mikroorganismen und Zellkulturen GmbH (DSMZ)" in Braunschweig, Mascheroder Weg 1 B, 38124 Braunschweig, under the provisions of the Budapest Treaty: A method of producing a therapeutic vaccine composition comprising using an Aβ antigenic peptide fragment consisting of a single or repetitive stretch of between 13 and 15 contiguous amino acid residues from the N-termina) part of the A(3 peptide for the treatment of an amyloid-associated disease or condition. A method according to claim 1, wherein the contiguous stretch of 13 to 15 amino acid residues is obtained from the N-terminal fragment 1-16 or 1-17 of the Ap peptide. A method according to claims 1 or 2, wherein the therapeutic vaccine composition comprises all Ap peptide fragment consisting of a single or repetitive stretch of-between 13 and 15 contiguous amino acid residues from the N-termina( part of the Ap peptide selected from the group consisting of residues 1-15, 1-14, and 1-13. A method according to claim 3, wherein the therapeutic vaccine composition comprises a single or repetitive Ap peptide fragment selected from the group consisting of AΒMS peptide antigen as given in SEQ ID NO: 1 and AΒI.I6(AI4) as given in SEA ID NO: 3. A method of any one of claims 1 to 4, wherein the Ap peptide antigen is modified such that it is capable of maintaining and stabilizing a defined conformation characterized by a balanced proportion of a-helical and/or p-sheet and/or random coil portions. A method according to any one of claims 1 to 5, wherein the Ap peptide antigen is presented reconstituted in a carrier such as, for example, a vesicle, a particulate body or molecule. A method according to claim 6, wherein the Ap peptide antigen is presented reconstituted in a liposome. A method according to claim 7, wherein the Ap peptide antigen is modified by a lipophilic or hydrophobic moiety that facilitates insertion into the lipid bilayer of the liposome carrier/adjuvant. A method according to claim 8, wherein the dimension of the lipophilic or hydrophobic moiety in combination with the overall net charge of the antigenic peptide and of the carrier/adjuvant to which the peptide becomes attached to, incorporated or reconstituted in is such that the antigenic peptide is exposed, stabilized and presented in a highly biologically active conformation, which allowrs the immune system of the target organism to freely interact with the antigenic detemiinants contained in the antigenic construct in its exposed, stabilized and highly biologically active conformation, which leads to a strong immune response. A method according to any one of claims 8 to 9, wherein the lipophilic or hydrophobic moiety is a fatty acid, a triglycerides or a phospholipid, A method according to claim 10, wherein the lipophilic or hydrophobic moiety is a fatty acid, particularly a fatty acid with a carbon back bone of at least 10 carbon atoms. A method according to claim 11, wherein the hydrophobic moiety is palmitic acid. A method according to any one of claims 7 to 12, wherein the liposome preparation contains an adjuvant. , A method according to claim 13, wherein the adjuvant is lipid A, particularly detoxified lipid A, such as monophosphory! or diphosphory! lipid A or alum. . A method of producing a therapeutic vaccine composition comprising using an immunogenic antigenic peptide for the treatment of an amyloid-associated disease or condition, wherein the (3-amyloid peptide antigen is a palmitoylated AβMs peptide antigen modified by covalently attached palmitoylated amino acid residues, particularly between 2 and 4, more particularly 4 residues, reconstituted in a liposome, A method according to claim 13. wherein the AβMs peptide antigen is modified by 2 palmltoylated amino acid residues covalently attached to the N- and C-termrnus of the peptide, respectively. A method according to claim 16, wherein the Api.ts peptide antigen is modified by 4 palmitoylated amino acid residues, two of which are covalently attached to the N-and C-terminus of the peptide, respectively. . A method according to claim 15, wherein 2 or more palmitoylated Aβ1.15 peptide antigen molecules modified by covalently attached palmltoyi residues, particularly one or two residues, at each end of the peptide are reconstituted in a single liposome. . A method according to any one of claims 1 to 18, wherein the amyloid associated disease or condition is one selected from the group consisting of diseases including, but not limited to, neurological disorders such as Alzheimer's Disease (AD), including diseases or conditions characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI), Lewy body dementia, Down's syndrome, hereditary cerebral hemorrhage with amyloidosis (Dutch type); the Guam Parkinson-Dementia complex; as well as other diseases which are based on or associated with amyloid-iike proteins such as progressive supranuclear palsy, multiple sclerosis; Creutzfeld Jacob disease, Parkinson's disease, HIV-related dementia, ALS (amyotropic lateral sclerosis). Adult Onset Diabetes; senile cardiac amyloidosis; endocrine tumors, and others, including macular degeneration. ", A method according to claim 19, wherein the amyloid associated disease or condition is Alzheimer's Disease, A method according to claim 19, wherein the amyloid-associated condition is characterized by a loss of cognitive memory capacity in an animal, particularly a mammal or a human. A method according to claim 21, wherein treatment of an animal, particularly a mammal or a human, suffering from an amyloid-associated condition characterized by a loss of cognitive memory capacity leads to an increase in the retention of cognitive memory capacity, A method according to claim 22, wherein treatment of an animal, particulariy a mammal or a human, suffering from an amyloid-associated condition characterized by a bss of cognitive memory capacity leads to a complete restoration of cognitive memory capacity. An antigenic construct comprising an Aβ antigenic peptide fragment consisting of a single or repetitive stretch of between 13 and 15 contiguous amino acid residues from the N-terminal part of the Aβ peptide for the treatment of an amyloid-associated disease or condition. An antigenic construct according to claim 24, wherein the contiguous stretch of 13 to 15 amino acid residues is obtained from the N-terminal fragment 1-16 or 1-17 of the Ap peptide. An antigenic construct according to claim 24, wherein the therapeutic vaccine composition comprises an Ap peptide fragment consisting of a single or repetitive stretch of between 13 and 15 contiguous amino acid residues from the N-terminal part of the Ap peptide selected from the group consisting of residues 1-15, 1-14, and 1-13, An antigenic construct according to any one of claims 24 to 26, wherein the therapeutic vaccine composition comprises a single or repetitive Ap peptide fragment selected from the group consisting of Api-15 peptide antigen as given in SEQ ID NO: 1 and Aβi.i6 An antigenic construct of any one of claims 24 to 27, wherein the Aβ peptide antigen is modifted such that it is capable of maintaining and stabilizing a defined confomnation characterized by a balanced proportion of a-helical and/or p-sheet and/or random coil portions. An antigenic construct according to any one of claims 24 to 28. wherein the Ap peptide antigen is presented attached to or reconstituted In a carrier/adjuvant such as, for example, a vesicle, a particulate body or molecule. An antigenic construct according to claim 29, wherein the Ap peptide antigen is presented reconstituted in a liposome. An antigenic construct according to claim 30, wherein the Ap peptide antigen Is modified by a lipophilic or hydrophobic moiety that facilitates insertion into the lipid bitayer of the liposome carrier. An antigenic construct according to claim 30, wherein the dimension of the lipophilic or hydrophobic moiety in combination with the overall net charge of the antigenic peptide and of the carrier to which the peptide becomes attached incorporated or reconstituted in is such that the antigenic peptide is exposed to the solvent and presented in a conformation that is biologically active in that it allows the immune system of the target organism to freely interact with the antigenic determinants contained in the antigenic construct, which leads to a strong immunogenic response and, accordingly, a high antibody titer in the target organism. An antigenic construct according to any one of claims 30 to 32, wherein the lipophilic or hydrophobic moiety is a fatty acid, a triglycerides or a phospholipid. An antigenic construct according to claim 33, wherein the lipophilic or hydrophobic moiety is a fatty acid, particularly a fatty acid with a cartoon back bone of at least 10 carbon atoms. An antigenic construct according to claim 34, wherein the hydrophobic moiety is palmitic acid. An antigenic construct according to any one of claims 30 to 35, wherein the liposome preparation contains an adjuvant or an immunmoduiator. , An antigenic construct according to claim 36, wherein the immunmoduiator is lipid A, particularly detoxified lipid A such as monophosphoryl or diphosphoryl lipid A or afum. . A vaccine composition comprising an Aβi-15 peptide antigen for the treatment of an amyloid-associated disease or condition. . A vaccine composition according to claim 38, wherein the Aβi-15 peptide antigen is modified such that it is capable of maintaining and stabilizing a defined conformation characterized by a balanced proportion of random coil, a-helical and p-sheet portions. A vaccine composition according to any one of claims 38 or 39, wherein the Apvis peptide antigen is presented attached to a carrier such as, for example, a vesicle, a particulate body or molecule. A vaccine composition according to claim 40, wherein the Aβi.15 peptide antigen is presented reconstituted in a liposome. A vaccine composition according to claim 41, wherein the Aβi-15 peptide antigen rs modified by a lipophilic or hydrophobic moiety that facilitates insertion into the hydrophobic lipid bilayer of the liposome carrier/adjuvant. A vaccine composition according to claim 42, wherein the dimension of the lipophilic or hydrophobic moiety providing an anchor for the peptide in the liposome bilayer in combination with the overall net charge of the antigenic peptide and of the carrier to which the peptide becomes attached, incorporated or reconstituted in is such that the antigenic peptide is exposed to the solvent and presented in a conformation that is biotogicalty active in that it allows the immune system of the target organism to freely interact with the antigenic determinants contained in the antigenic construct, which leads to a strong immunogenic response and, accordingly, a high antibody titer in the target organism. A vaccine composition according to claim 43, wherein the lipophilic or hydrophobic moiety is a fatty acid, triglycerides or phospholipids. A vaccine composition according to claim 44, wherein the fatty acid carbon back bone has at least 10 carbon atoms. A vaccine composition according to claim 45, wherein the hydrophobic moiety is palmitic acid. A vaccine composition according to any one of claims 41 to 46, wherein the liposome preparation contains an adjuvant and/or an immunmodulator, A vaccine composition according to claim 47, wherein the immunmodulator is detoxified lipid A, such as monophosphoryl or diphosphoryl lipid A. A vaccine composition comprising an immunogenic antigenic peptide for the treatment of an amyloid-associated disease or condition, wherein the p-amyloid peptide antigen is a palmitoylated Aβi-15 peptide antigen modified by covalently attached palmitoyi residues, particularly between 2 and 4, more particularly 4 residues, at each end of the peptide reconstituted in a liposome. A vaccine composition according to claim 49, wherein 2 or more palmitoylated Aβi. 15 peptide antigen molecules modified by covalently attached palmitoyi residues at each end of the peptide are reconstituted in a single liposome. A vaccine composition according to any of the preceding claims, which, upon administration to an animal, particularly a mammal, but especially a human, results mainly in the generation of antibodies of non-inflammatory subtypes. A vaccine composition according to claim 51, wherein said antibodies are of the non-inflammatory Th2 subtype, particularly of isotypeHgd and lgG2b. A vaccine composition according to any of the preceding claims, which, upon administration to an animal, partitulariy a mammal, but especially a humafi, results mainly in the generation of antibodies of the T-cel) independent JgG subclass. A vaccine composition according to claim 53, wherein said antibodies are of the lgG3 isotype. A vaccine composition according to any of the preceding claims, which, upon administration to an animal, particularly a mammal, but especially a human does not lead to a significant increase in inflammation markers in the the brain. . A vaccine composition according to claim 53, wherein said markers are selected from the group consisting of lL-1 p, IL-6, IFN-y and TNF a. . A vaccine composition according to any of the precedirig claims which, upon administration to an animal, particularly a mammal, but especially a human leads to a significant decrease of insoluble, plaque-related- Api-40 and Ap1-42 in the brain. A vaccine composition according to any of the preceding claims which, upon administration to an animal, particularly a mammal, but especially a human leads to a significant reduction in the level of soluble Ap 1-42 in the brain. , A vaccine composition according to any of the preceding claims for the treatment of an amyloid-associated disease or condition in an animal, particularly a mammal or a human, suffering from such a condition. A vaccine composition according to claim 59, wherein the amyloid associated disease or condition is one selected from the group consisting of diseases including, but not limited to, neurological disorders such as Alzheimer's Disease (AD), including diseases or conditions characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI), Lewy body dementia, Down's syndrome, hereditary cerebral hemorrhage with amyloidosis (Dutch type); the Guam Parkinson-Dementia complex; as well as other diseases which are based on or associated with amyloid-like proteins such as progressive supranuclear palsy, multiple sclerosis; Creutzfeld Jacob disease, Parkinson's disease, HlV-related dementia, ALS (amyotropic lateral sclerosis), Adult Onset Diabetes; senile cardiac amyloidosis; endocrine tumors, and others, including macular degeneration. A vaccine composition according to claim 60, wherein the amyloid associated disease or condition is Alzheimer's Disease. A vaccine composition according to any of the preceding claims which, upon administration to an animal, particularly a mammal or a human, suffering from an amyloid-associated condition characterized by a loss of cognitive memory capacity leads to an increase in the retention of cognitive memory capacity. A vaccine composition according to any of the preceding claims which, upon administration to an animal, particularly a mammal, but especially to a human, suffering from an amyloid-associated condition characterized by a loss of cognitive memory capacity leads to a complete restoration of cognitive memory capacity. A vaccine composition comprising an Ap peptide antigen for the treatment of an amyloid-associated disease or condition together with an inhibitor of the complement system. . A vaccine composition according to claim 64, wherein the Ap peptide antigen is a Api-is peptide antigen. A vaccine composition according to claim 65 comprising an immunogenic antigenic peptide for the treatment of an amyloid-associated disease or condition, wherein the ^-amyloid peptide antigen is a palmitoylated Β;M5 peptide antigen modified by covalently attached palmitoyi residues, particularly between 2 and 4, more particularly 4 residues, at each end of the peptide reconstituted in a liposome together with an inhibitor of the complement system. . A vaccine composition comprising an A(3 peptide antigen for the treatment of an amyloid-associated disease or condition together with a compound, particularly an allosteric effector of hemoglobin, which triggers an enhanced, regulated oxygen release to the tissues. A vaccine composition according to claim 67, wherein the Ap peptide antigen is a A3i-i5 peptide antigen. A vaccine composition according to claim 68 comprising an immunogenic antigenic peptide for the treatment of an amyloid-associated disease or condition, wherein the p-amyloid peptide antigen is a palmitoylated Api.15 peptide antigen modified by covalently attached palmitoyi residues, particularly between 2 and 4, more particularly 4 residues, at each end of the peptide reconstituted in a liposome together with a compound, particularly an allosteric effector of hemoglobin, which triggers an enhanced, regulated oxygen release to the tissues. . A vaccine composition comprising an Ap peptide antigen for the treatment of an amyloid-associated disease or condition together with an Inhibitor of the complement system and a compound particularly an allosteric effector of hemoglobin, which triggers an enhanced, regulated oxygen release to the tissues. . A vaccine composition according to claim 70, wherein the Ap peptide antigen is a Aβ-is peptide antigen. 'V vaccine composition according to claim 71 comprising an immunogenic antigenic peptide for the treatment of an amyloid-associated disease or condition, wherein the β-amyloid peptide antigen is a palmitoylated AΒMS peptide antigen modified by covatently attached palmitoyi residues, particularly between 2 and 4, more particularly 4 residues, at each end of the peptide reconstituted In a liposome, together with an inhibitor of the complement system and a 02/hemoglobin affinity modulating compound, particularly an altosteric effector of hemoglobin, which triggers an enhanced, regulated oxygen release to the tissues. A vaccine composition according to any one of claims 54 to 66 and 70 to 72, wherein the complement inhibitor is a compound selected from the group consisting of soluble human complement Receptor 1, anti- human complement protein C5 such as, for example, a humanized anti C5 monoclonal antibody or a single-chain fragment of a humanized monoclonal antibody, Cl-esterase inhibitor-N and Natural human CI Inhibitor. A vaccine composition according to any one of claims 67 to 69 and 70 to 72, wherein the 02/hemoglobin affinity modulating compound is a compound selected from the group consisting of an antilipidemic drug such as, for example, clofibric acid or bezafibrate including the bezaftbrate derivatives LR16 and L35, urea derivatives such as, for example, [2-[4[[(afylamrno)carbonyl]-am(no]phenoxy]-2-mettiylpropionic acid, an allosteric effector of haemoglobin such as, for example, 2,3-diphosphoglycerate (DPG), inositol hexakisphosphate (IHP). and pyridoxal phosphate. A vaccine composition according to any one of claims 67 to 69 and 70 to 72, wherein the Oz/hemoglobin affinity modulating compound is a compound comprising an anionic ligand for an allosteric site of hemoglobin, wherein the anionic ligand comprises an internal pyrophosphate ring, optionally together with a nontoxic cation. A vaccine composition according to claim 75, wherein the 02/hemoglobin affinity modulating compound is a inositol hexaphosphate (IHP) derivative comprising at least one Internal pyrophosphate ring, optionally together with a nontoxic cation. . A vaccine composition according to any one of claims 64 to 75, wherein the P-amyloid peptide antigen comprises an antigenic construct according to any one of claims 24 to 37. . Use of an Aβ antigenic peptide fragment consisting of a single or repetitive stretch of between 13 and 15 contiguous amino acid residues from the N-terminal part of the Aβ peptide for the preparation of a pharmaceutical composition for the treatment of an amyloid-associated disease or condition. Use of a Aβ peptide antigen as described in claims 2 to 23 or an antigenic construct according to any one of claims 24 to 37 for the treatment of an amyloid-associated disease or condition. Use of a Aβ peptide antigen according to claim 79, wherein the amyloid associated disease or condition is one selected from the group consisting of diseases including, but not limited to, neurological disorders such as Alzheimer's Disease (AD), including diseases or conditions characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI), Lewy body dementia, Down's syndrome, hereditary cerebral hemorrhage with amyloidosis (Dutch type); the Guam Parkinson-Dementia complex; as well as other diseases which are based on or associated with amyloid-like proteins such as progressive supranuclear palsy, multiple sclerosis; Creutzfeld Jacob disease, Parkinson's disease, HIV-related dementia, ALS (amyotropic lateral sclerosis). Adult Onset Diabetes; senile cardiac amyloidosis; endocrine tumors, and others, including macular degeneration. Use of a Ap peptide antigen according to claim 80, wherein the amyloid associated disease or condition is Alzheimer's Disease. Use of an Aβ peptide antigen according to claim 80, wherein the amyloid-associated condition is characterized by a loss of cognitive memory capacity such as, for example, in mild cognitive impainnent (MCI) in an animal, particularly a mammal or a human. Use of a Aβ peptide antigen according to claim SO, wherein treatment of an animal, particularly a mammal or a human, suffering from an amyioid-associated condition characterized by a loss of cognitive memory capacity leads to an increase in the retention of cognitive memory capacity. Use of a Aβ peptide antigen according to claim 80, wherein treatment of an animal, particularly a mammal or a human, sufferirig from an amyloid-associated condition characterized by a loss of cognitive memory capacity leads to a complete restoration of cognitive memory capacity. A method for the treatment of an amyloid-associated disease or condition comprising administering to an animal, particularly to a mammal, but especially to human, suffering from such a disease or condition a therapeutic vaccine composition as claimed in any one of claims 38 to 77. A method according to claim 85, wherein the vaccine composition comprises an Aβi-i5 peptide antigen, particularly a palmitoylated Aβi.15 peptide antigen. A method according to claim 85, wherein administration of said vaccine composition results mainly in the generation of antibodies of non-inflammatory subtypes. A method according to claim 87, wherein said antibodies are of the non-Inflammatory Th2 subtype, particularly of isotype lgG1 and lgG2b. , A method according to claim 85, wherein administration of said vaccine composition results mainly in the generation of antibodies of the T-cell independent IgG subclass. A method according to claim 89, wherein said antibodies are of the lgG3 isotype. A method according to claim 85, does not lead to a significant increase in inflammation markers in the brain, A method according to claim 91, wherein said markers are selected from the group consisting of IL-1 p. IL-6, IFN-y and TNF a. A method according to claim 85, wherein administration of said vaccine composition leads to a significant decrease of insoluble, plaque-related- Api-40 and Api-42 in the brain. A method according to claim 85, wherein administration of said vaccine composition leads to a significant reduction in the level oi soluble Aβ1-42 in the brain. , A method according to any one of claims 85 to 94, wherein the amyloid associated disease or condition is one selected from the group consisting of diseases including, but not limited to, neurological disorders such as Alzheimer's Disease (AD), including diseases or conditions characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impaimient (MCI), Lewy body dementia, Down's syndrome, hereditary cerebral hemorrhage with amyloidosis (Dutch type); the Guam Parkinson-Dementia complex; as well as other diseases which are based on or associated with amyloid-like proteins such as progressive supranuclear palsy, multiple sclerosis; Creutzfeld Jacob disease, Parkinson's disease, HIV-related dementia, ALS (amyotropic lateral sclerosis). Adult Onset Diabetes; senile cardiac amyloidosis; endocrine tumors, and others, including macular degeneration. A method according to claim 95, wherein the amyloid associated disease or condition is Alzheimer's Disease. A method according to any one of claims 85 to 94, wherein administration of said vaccine composition to an animal, particularly a mammal or a human, suffering from an amyloid-associated condition characterized by a loss of cognitive memory capacity leads to an increase in the retention of cognitive memory capacity. A method according to any one of claims 85 to 94, wherein administration of said vaccine composition to an animal, particularly a mammal or a human, suffering from an amyloid-associated condition characterized by a Joss of cognitive memory capacity leads to a complete restoration of cognitive memory capacity. A method for significantly increasing the retention or cognitive memory capacity of a mammal, by immunization with a therapeutic vaccine composition as claimed in any one of claims 38 to 77 A method according to claim 99, wherein the vaccine composition comprises an Aβi.-i5 peptide antigen, particularly a palmltoylated AΒMS peptide antigen. I. A method for inducing an immune response in an animal, particularly a mammal or a human, suffering from an amyloid-associated condition characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impairment (MCI) by administering to said animal or human a therapeutic vaccine composition as claimed in any one of claims 38 to 77 such that the retention or cognitive memory capacity of the treated animal or human is increased. ;. A method for inducing an immune response in an animal, particulariy a mammal or a human, suffering from an amyloid-associated condition characterized by a loss of cognitive memory capacity such as, for example, mild cognitive impaimient (MCI) by administering to said animal or human a therapeutic vaccine composition comprising a Aβi.15 peptide antigen, particularly a palmltoylated Aβi.15 peptide antigen such that the cognitive memory capacity of the treated animal or human is completely restored. J. A method according to claim 85, wherein a vaccine composition according to any one of claims 64 - 77 is administered such that the complement inhibitor and the antigenic constmct are administered concomitantly, intenmittently or sequentially. k A method according to claim 103, wherein the complement inhibitor is administered prior to the vaccination with the antigenic construct, particularly within a time window starting up to 20 hours before the vaccination and ending immediately before the vaccination. ), A method according to claim 103, wherein the complement inhibitor is administered subsequent to the vaccination with the antigenic construct within a time window starting immediately after the vaccination and ending 1 day after vaccine application. 5. A method according to any one of claims 103 to 105, wherein the vaccine composition comprises an Aβvis peptide antigen, particularly a palmitoylated Aβ 15 peptide antigen, J. A method the preparation of a medicament for the treatment of an amyloid-associated disease or condition comprising using a vaccine composition as claimed in any one of claims 38 to 77. B. A method of producing a medicament for the treatment of an amyloid-associated disease or condition comprising using a immunogenic antigenic peptide, wherein the p-amyloid peptide antigen is a palmitoylated ApMs peptide antigen modified by covalently attached palmitoylated amino acid residues, particularly between 2 and 4, more pailicularly 4 residues, reconstituted in a liposome. 9. An antibody or an antibody mixture obtainable from an animal immunized with a vaccine composition according to any one of claims 31 to 43. 0. An antibody according to claim 50 characterized in that it is a monoclonal antibody or a derivative thereof,

Documents:

2923 CHENP 2008 PETITION POR.pdf

2923-CHENP-2008 CORRESPONDENCE OTHERS 01-10-2013.pdf

2923-CHENP-2008 CORRESPONDENCE OTHERS 06-11-2013.pdf

2923-CHENP-2008 CORRESPONDENCE OTHERS 08-11-2013.pdf

2923-CHENP-2008 AMENDED CLAIMS 06-06-2014.pdf

2923-CHENP-2008 AMENDED PAGES OF SPECIFICATION 06-06-2014.pdf

2923-CHENP-2008 CORRESPONDENCE OTHERS 01-09-2014.pdf

2923-CHENP-2008 EXAMINATION REPORT REPLY RECEIVED 06-06-2014.pdf

2923-CHENP-2008 FORM-18 30-11-2009.pdf

2923-CHENP-2008 OTHER PATENT DOCUMENT 06-06-2014.pdf

2923-CHENP-2008 POWER OF ATTORNEY 06-06-2014.pdf

2923-CHENP-2008 SEQUENCE LISTING 06-06-2014.pdf

2923-chenp-2008 abstract.pdf

2923-chenp-2008 claims.pdf

2923-chenp-2008 correspondence-others.pdf

2923-chenp-2008 description (complete).pdf

2923-chenp-2008 drawings.pdf

2923-CHENP-2008 FORM-1 01-09-2014.pdf

2923-chenp-2008 form-1.pdf

2923-chenp-2008 form-3.pdf

2923-chenp-2008 form-5.pdf

2923-chenp-2008 pct.pdf

Form 3.pdf

Petition for Annexure.pdf

Petition for sequence listing.pdf