Title of Invention	A PERSONAL CARE FORMULATION
Abstract	The application describes a range of personal care products than include a keratin protein fraction. The fraction may be intact or hydrolysed. It is preferably S-sulfonated. The content of the fraction may range from 0.001% to 50%. In most formulations is content will be less than 1% although in a certain products such as nail care products the content will be higher. A wide range of personal care products are described including shampoos body gels and lotions, conditioners, creams and cosmetics generally.

Title of Invention

A PERSONAL CARE FORMULATION

Abstract

The application describes a range of personal care products than include a keratin protein fraction. The fraction may be intact or hydrolysed. It is preferably S-sulfonated. The content of the fraction may range from 0.001% to 50%. In most formulations is content will be less than 1% although in a certain products such as nail care products the content will be higher. A wide range of personal care products are described including shampoos body gels and lotions, conditioners, creams and cosmetics generally.

Full Text	1 Field of the Invention 5 The invention relates to personal care formulations containing keratin and their use in cosmetics. Background of the invention Proteins and their derivatives are used in a wide range of personal care formulations, 10 including those intended for use on the hair, skin and nails. As a component of personal care formulations, proteins perform many functions, including conditioning, film forming, as a humectant and an emollient. Most commonly used proteins are hydrolysed in order to impart sufficient solubility to facilitate inclusion in a formulation. This is particularly the case with keratin proteins, which, are inherently insoluble due to 15 the crosslinks associated with the characteristically high degree of cysteine present in the protein. Numerous examples of the use of hydrolysed proteins, including keratins, in personal care formulations are known in the art. WO9851265 discloses the use of hydrolysed proteins and their derivatives, particularly 20 those with high, sulfur content, in formulations to protect hair from the insults of environmental and chemical damage. The inventors in WO9851265 use a combination of hydrolysed proteins and a polyamino cationic agent in order to prepare the desired formulations. 25 US4948876 describes an S-sulphocysteine keratin peptide produced by enzymatic hydrolysis for use as an auxiliary in the dyeing of wool and hair Enzymatic digestion is used by the authors to prepare low molecular weight peptides and achieve the desired solubility. WO 2004/047774 PCT/NZ2003/000263 2 US4S95722 discusses the use of a range of keratin decomposition products, including those obtained by chemical and enzymatic hydrolysis, for the preparation of cosmetic products. 5 Keratin fibres, such as human hair, wool and other animal fibres, consist of a complex mix of relaxed proteins that, are all part of the keratin family. These proteins can be grouped according to their structure and role within the fibre into the following groups: the intermediate filament proteins (IFP), which are fibrous proteins found mostly 10 in the fibre cortex; high sulfur proteins (HSP), which are globular proteins found in the matrix of the fibre cortex, as well as in the cuticle. 15 high glycine-tyrosine proteins (HGTP), found mostly in the fibre cortex. The ulrastrucrture of keratin fibres is well known in the art, and discussed in detail by R. C. Marshall, D. F. G. Orwin and J. M. Gillespie, Structure and Biochemistry of Mammalian Hard Keratin, Electron Microscopy Reviews, 4, 47,1991. In the prior art 20 described in which proteins are used as a cosmetic ingredient, the keratin utilized is hydrolysed as one material, with no attempt at fractionating the keratin source into its constituent components. As a result of protien hydrolysis, many of the desirable properties of the proteins are lost. Low molecular weight keratin peptides aggregate with a much lower degree of order to produce materials with much poorer physical 25 properties than the high molecular weight keratins from which they are derived. In addition, irreversible conversion of cysteine as may occur with chemical methods of keratin, decomposition, yields, a peptide product that has lost the core functionality than that distinguishes it from other protein materials. WO 2004/047774 PCT/NZ2003/000263 3 The need exists for personal care formulations which use intact keratins which maintain many of the desirable characteristics of the native keratins from which they are derived and possess a reactivity towards keratin substrates. 5 Object of the Invention It is an object of The invention to provide a personal care formulation which uses a keratin protein or to at least provide the public with a useful choice. Summary of the Invention 10 The invention provides a personal care formulation including a keratin protein fraction. The keratin protein fraction may be intact. The invention also provides a personal care formulation in which the karatin protein 15 fraction is hydrolysed. In particular, the invention provides a personal care formulation including a keratin protein fraction which is S-sulfonated. 20 The invention provides personal care formulations in which the keratin protein fraction is from the intermediate filament protein family. The invention also provides a personal care formulation in which the keratin protein fraction is from the high sulfur protein family. 25 The cysteine content of the keratin protein may be about 4%, The invention also provides a personal care formulation in which the keratin protein fraction is from the high glycine-tyrosine protein family. 30 WO 2004/047774 PCT/NZ2003/000263 4 Preferably the percentege of the intact S-sulfonated keratin protein fraction in the formulation is less than ten percent by weight. More preferably the ratio is between 0.001 and 1% inclusive by weight. However the 5 ratio may be from 0.001 % to 50% of keratin protein fraction. The invention also provides a personal care fomation containing about 0.001% to 50% of a keratin protein fraction. 10 The ratio is preferably 0.001 % to 10% and more preferably 0.001 % to 1 %. The invention also provides an additive for a personal care formation comprising a keratin protein fraction. 15 The personal care formulations may include the following: Coaditioning shampoo; Body/Facial cleanser/shampoo; Hair conditioner; Hair gel; 20 Hair mouse, setting lotion; Hairspray, Pre-perming solution; Post-pesrming solution; Moisturing cream; 25 Shower gel; Foaming bath gel; Mascara; Nail polish Liquid foundation. 30 Shaving cream; and Lipstick. WO 2004/047774 PCT/NZ2003/000263 5 However other personal care formulations are included within the invention. The invention also provides a personal care formulation including an intact sulfonated 5 keratin fraction wherein the ratio of keratin fraction is about 10% of the formulation. The formulation is adapted to be used as a nail polish or nail glosser. The personal care formulations comprise a suitable percentage by weight of a cosmetic carrier. 10 Additional elements such as vitamins and minerals may be added to enhance the protective efficacy of the formulations. Sunscreen factors with ultra-violet protection properties may also be added. 15 The invention also provides a method of using the personal cars fomulation or additives according to the invention. Detailed Description of the Drawings 20 The invention will now be described by way of example only in which: Figure 1 shows instron test results for permed hair fibres treated with 5% SIFP Figure 2 shows,instron test results for permed hair fibres treated with 2% SIFP Figure 3 shows instron test results for bleached hair fibres treated with 5% SIFP Figure 4 shows instron results for relaxed hair fibres treated with 2% SIFP 25 Figure-5 shows, substantivity of SIFP, SHSP and SPEP on undamaged and damaged hair at 50% relative humidity Figure 6 shows moisturisation with increasing relative humidity of undamaged and damaged hair treated with SIFP, SHSP and SPEP Figure 7 shows foaming results for common surfactants and SIFP, SHSP and SPEP in 30 the presence and absence of EDTA obtained from the waring blender test WO 2004/047774 PCT/NZ2003/000263 6 Figure 8 shows foaming results for shampoo formulations with and without SIFP, SHSP and SPEP Figure 9 is a summary of subjective assessment of a shampoo formulation in the presence and absence of SIFP 5 Detailed Description of the Invention The hard alpha keratin proteins such as those derived, from human hair, wool, animal fibres, horns, hooves or other mammalian sources, can be classified into particuolar components according to their biochemical properties, specifically their molecular 10 weight and amino acid composition. Table 1 illustrates the amino acid composition determined by conventional analytical methods of typical keratin protein fractions known in the art and also the subject of this invention. This involves acid hydrolysis of the analyte which converts all cystine and labile cysteine derivatives to cysteine, typically recorded as half-cysteine. 15 WO 2004/047774 PCT/NZ2003/000263 7 Table 1 illustrates an amino acid composition of keratin fractions: S-sulfonated karatin intermediate filament protein (SIFP), peptides derived from S-sulfonated keratin intermediate filament protein (SIFP-pep), S-sulfonated keratin high sulfur protein (SHSP), peptides derived from S-sulfonated keratin high sulfur protein (SHSP-pep), S- 5 sufonated keratin peptide (SPEP) as used in the invention. Intermediate filament protein (IFP), high, sulfur protein (HSP), high glycine-tyrosine protein (HGTP) and whole wool courtesy of Gillespie and Marshall, Variability in the proteins of wool and hair, Proc. Sixth Int. Wool Text. Res. Conf., Pretoria, 2, 67-77, 1980. All residues expressed as mol%. S-sulfocysteine, cystine and cysteine are measured as S- 10 carboxymethyl cysteine following reduction and alkylation, and reported as cys. Table 2 illustrates -the molecular weight determined by conventional analytical methods of typical keratin protein fractions known in the art and also the subject of this invention. Conventional analysis involves cleavage of cystine bonds within the keratin 15 using reduction so that the protein mass is determined in its native, uncrosslinked state, most similar to the unkeratinised state of the protein. Mass is determined using polyacrylamide gel electrophoresis. In the case of the peptide SPEP mass is determined using mass spectrometry. Using these methods the Keratin is made soluble without any hydrolysis of peptide bonds and an accurate measure of molecular weight is determined. 20 Table 2: Molecular weight of keratin fractions: S-sulfonated keratin intermediate filament protein (SIFP), peptides derived from S-sulfonated keratin intermediate Slament protein (SIFP-pep), S-sulfonated keratin high sulfur protein (SHSP), peptides WO 2004/047774 PCT/NZ2003/000263 8 derived from S-sulfonated keratin high sulfur protein (SHSP-pep), S-sulfonated keratin peptide (SPEP) as used in the invention. Intermediate filament protein (IFP), high sulfur protein (HSP) high glycine-tyrosine protein (HGTP) and whole wool courtesy of Gillespie and Marshall. Variability in the proteins of wool and hair, Proc. Sixth Int. 5 Wool Text. Res. Conf. Pretoria, 2, 67-77, 1980. Both amino acid composition and molecular weight varies across keratin types, between species and also within breeds of one species, for example between, wools from different breeds of sheep. The figures gives in tables 1 and 2 are indicative for the keratin source 10 stated. However, individual types of keratin proteins, or keratin protein, fractions, have distinctive characteristic, particularly molecular weight and amino acid content. The subject of the invention is formulations containing intact S-sulfonated keratin protein fractions. "Intact" refers tO proteins that have not been. significantly hydrolysed, 15 with hydrolysis being defined as the cleavage of bonds through the addition of water. Gillespie (Biochemistry and physiology of the skin, vol 1, Ed. Goldsmith Oxford University Press, London, 1983, pp475-510) considers "intact" to refer to proteins in the keratinized polymeric state and further refers to polypeptide subunits which complex to form intact keratins in wool and hair. For the purpose of this invention "intat" refers to 20 the polypeptide subunits described by Gillespie. These are equivalent to the keratin proteins in their native form without the disulfide crosslinks formed through the process of keratinisation. Keratin protein fracrtions are distinct groups from within the keratin protein family, such 25 as the intermediate filament, proteins, the high sulfur proteins or the high glycine- tyrosine proteins well known in the art. Intermediate filament proteins are described in detail by Orwin et al (Structure and Biochemistry of Manunalian Hard Keratin, Electron Microscopy Reviews, 4, 47,1991) and also referred to as low sulphur proteins by Gilliespie (Biochemistry and physiology of the skin, vol 1, Ed. Goldsmith Oxford 30 University Press. London, 1983, pp475-5lO). Key characteristics of this protein family are molecular weight in the range 40 — 60 kD and a cystene content (measured as half WO 2004/047774 PCT/NZ2003/000263 9 cystine of around 4%. The high sulfur protein family are also well described by Orwin and Gillispie in the same publications. This protein family has a large degree of heterogeity but can be characterised as having a molecular weight in the range 10 — 30 kD and a cysteine consent of greater than 10%. The subset of this family, the ultra high 5 sulfur proteins can have a cysteine content of up to 34%. The high glycine-tryosine protein family are also well described by Orwin and Gillespie in the same publications. This family is also referred to as the high tryrosine proteins and has characteristics of a molecular weight less than 10 KD, a tyrosine content typically greater than 10% and a glycine content typically greater than 20%. 10 For the purpose of this invention a "keratin protein fraction" is a purified form of keratin that contains predominantly, although not entirely, one distinct protein group as described above. In the content of this invention S-Sulfonated keratins, have cysteine/cystine present predominantly in the form S-sulfocysteine, commonly known 15 as the Bunte salt. This highly polar group imparts a degree of solubility to proteins Whilst being stable in solution, the S-sulfo group is a labile cysteine derivative, highly reactive towards thiols, such as cysteine, and other reducing agents. Reaction with reducing agents leads to conversion of the S-sulfo cysteine group back to cysteine. S- sulfo cysteine is chemically different to cysteic acid, although both groups contain the 20 SO3 group. Cysteic acid is produced irreversibly by the oxidation of cysteine or cystine and once formed cannot form disulfide crosslinks back to cysteine. S-sulfocystein is reactive towards cysteine and readily forms disulfide crosslinks. One aspect of the invention is personal care formulations containing S-sulfonated 25 keratin intermediate- filament protein (SIFP). These proteins are characterised as having a molecular weight in the range 40-60kD and a cysteine content determined through amino acid analysis of around 4%. This material may be prepared by a variety of methods, including those described in NZ/PCT02/00125. This material has excellent film forming properties, and can be reconstituted in a variety of ways, such as those 30 outlined in NZ/PCT02/00169. The characteristics of the material arise at least in part from the intact nature of the fibrous proteins. Intermediate filament proteins are known WO 2004/047774 PCT/NZ2003/000263 10 to associate on a molecular level, which is fundamental to the reformation of the proteins into materials. The ability of this material to act as a film former is a useful cosmetic property. In addition, the S-sulfo group is of use in personal care formulations as it is highly reactive towards thiols, forming a covalent disulfide bond. Thiols are 5 present in the form of cysteine, particularly in hair damaged through reductive processes such, as perming. In addition, as a highly polar group, the S-sulfo group is attracted to polar substrates, such as the surface of hair damaged through oxidation processes and bleaching. With this type of hair the SIFP can form, salt bridges and hydrogen bonds and consequently impart a durable conditioning effect. 10 A further aspect of the invention is cosmetic formulations containing S-sulfonated keratin high sulfur protein (SHSP). These proteins are characterised as having a molecular weight in the range 10-30kD and a cysteine content determined through amino acid analysis of greater than 10%. This material may be prepared by a variety of 15 methods, including those described in NZ/PCT02/O0125. As an intact globular protein derived from the matrix proteins of the keratin fibre cortex, and also the cuticle cells, this material has the potential to repair damaged hair, in particular where split ends will allow penetration of this intact protein into the fibre. In addition, with a higher proportion, of cysteine than commercially available keratin derivatives typically used in 20 personal care formulations, the potential to bind to damaged hair, or to bind to hair when, used as part of a permanent waving process, is significant. One aspect of the invention is keratin peptides derived from Keratin protein fractions. These peptides have a cysteine content similar to the fraction from which the peptide is 25 derived (approximately 4% for SIFP-pep and greater than 10% for SHSP-pep). Being of low molecular weight these materials can penetrate the surface of hair and skin and provide cosmetic function within the substrate. This material is differentiated from other hydrolysed keratins by virtue of being derived from a particular keratin protein fraction, as well as the cysteine being present as S-sulfo cysteine. A source of peptides with 30 variable amounts of cysteine is of particular value in the formulation of cosmetics. WO 2004/047774 PCT/NZ2003/000263 11 One aspect of the invention is personal care formulations containing S-sulfonated keratin peptides derived from bulk keratin. These peptides are characterised as having a molecular weight approximately lkD or less and a cysteine content determined through amino acid analysis of approximately 4%. This material may be prepared by a variety 5 of methods, including those described in NZ/PCT02/00125. This material is differentiated from other hydrolysed keratins by virtue of the cysteine being present in the form of S-sulfo groups. The low molecular weight of this material allows it to penetrate through the hair cuticle. This feature, combined with the S-sulfo groups present on the peptide and the reactivity of this group creates a useful ingredient for the 10 formulation of cosmetics, in particular hair cosmetics. Keratins are characterised by having a higher cysteine content than other proteins. In some protein fractions derived from wool cysteine contents as high as 30% have been reported Cysteine is a known reductant and keratin protein fractions that are the subject 15 of this invention are reductants and antioxidants that can be used as an active component in personal care formulations targeted at anti ageing, or reducing oxidative damage to hair and skin caused by free radicals, pollutants and environmental insults. Measurements of antioxidant properties of keratin protein fractions are detailed in Table 3. 20 Table 3: Antioxidanr activity of keratin fractions. Results expressed as the amount of Trolox equivalent antioxidant capacity per hundred gram, or milliliters, of sample (umol TEAC/1O0 g or mol TEAC/100mL), which represents the amount of Trolox (vitamin 25 E) that gives the same response as one hundred grams or mLs. of sample. Triplicate analyses (at different concentrations) were earned out on each extract. Equivalent WO 2004/047774 PCT/NZ2003/000263 12 activity calculated on the basis of protein concentration of sample used (SPEP and SHSP 15% solution SIFP 5% solution). Personal care formulation includes any substance or preparation intended for placement 5 in contact with any eternal part of the human body, including the mucous membranes of the oral cavity and the teeth, with a view to: — altering the odours of the body; — changing its appearance; — cleansing it; 10 — maintaining it in good condition; or — perfuming it, but does not inchlude any product that is required by law to regulated as a medicine, as a therapeutic substance or device, as a food or as a nurtritional or dietary supplement. 15 It also includes any personal care formulation intended to improve the appearance. Unless the contest clearly requires otherwise, throughout the description and the claims, the words "comprise", "comprising" and the like, are to be construed in an inclusive sense as opposed to an exclusive or exhaustive sense, that is to say, in the sense of 20 "including, but not limited to". The invention will now be described, by way of example only and with reference to the accompanying Examples which, are by way of exemplification only. 25 Examples In each formulation 'keratin fraction' is included at an indicative level. Keratin fraction refers to SIFP, SIFP-pep, SHSP, SHSP-pep, HGTP or S-sulfonated keratin peptides, all of which are described above. Unless otherwise stated, it is convenient to provide the keratin fraction in the form of a dilute aqueous solution and include the appropriate 30 amount of this solution in the formulation to achieve the keratin fraction level indicated. WO 2004/047774 PCT/NZ2003/000263 13 Typical concentrations of aqueous solutions for the keratin fraction types are SIFP 5%, SHSP 15% and S-sulfonated keratin peptides 15%. Therefore, in order to achieve the indicated level of 0.5% keratin fraction for SIFP, 10% of an SIFP solution would to be used in the formulation. Percentages are expressed as w/v. 5 Sample formulations Conditioning shampoo Sodium, lauryl sulphate 28% 2 5.0% 10 Sodium laureth-2-sulphate 70% 4.0 Cocamide DEA 70% 3.5 Cocamidopropyl betaine (30%) 3.0 Keratin fraction 0.5 Sodium chloride q.s 15 Citric acid q.s Fragrance q.s Preservative q.s Water q.s to 100 Procedure: A Combine 35.0 g water, sodium laureth sulphate and sodium lauryl 20 sulphate. Heat to 65º C until dissolved. Add cocamide DEA and allow to cool. B. Mix betaine -with water and add to phase A. Add keratin fractioin, adjust the pH to 6.5 with citric acid. Add preservative and fragrance as required, adjust to desired thickness with sodium chloride and add remaining water. 25 Hair gel Carbomer (Carbopol Ultrez 10) 0.5% Disodium EDTA 0.05 Glycerin 4.0 Triethanolamine (20%) 3.0 30 Keratin fraction 0.45 Preservative q.s WO 2004/047774 PCT/NZ2003/000263 14 Fragrance q.s Water q.s to 100 Procedure. A Heat 60.Og of water to 70ºC and add to carbopol, EDTA aud glycerol. Mix vigorously, Cool. Add triethanolamine to adjust pH to 6.3. Add keratin fraction. 5 Combine preservative and remaining water and add. Mix thoroughly ami add fragrance as desired. Clear Body/Facial Cleanser and Shampoo 10 Ammonium lauryl suphate 28% 25.0% Disodium laureth sulfosuccinate 20.0 Cocamidopropyl betaine 8.0 Keratin fraction 0.5 Sodiuim chloride qs 15 Fragrance (parfum) qs Preservative qs Water (aqua) qs to 100 Hair Conditioner 20 Cetrimonium Chloride 5.0% Stearyl alcohol 4.5 Keratin fraction 0.25 Fragrance qs Preservative qs 25 Water qs tol00 Hair Mousse Keratin fraction 0.25% Hydrogenated tallow trimonium chloride 0.20 30 Nonoxynol-10 0.35 Alcohol 10.0 WO 2004/047774 PCT/NZ2003/000263 15 Butane-48 10.0 Water qs to 100 Setting lotion 5 Carbomer (Carbopol Ultrez 10) 2.0% Mineral oil (light) 0.20 Keratin fraction 0.25 Alcohol 37.5 Fragrance qs 10 Water qs to lOO Hairspray VA/Crotonates/Vinyl Neodeconoate Copolymer 1.60% (Resyn 28-2930) 15 Aminomethyl propanol 0.15 PEG-75 lanolin 0.20 Keratin fraction 0.25 Alcohol 65.05 Butane 30 28.0 20 Pre-perming solution TEA- lauryl sulphate 30.0% Cocamidopropyl dimethylamine oxide 10.0 Cocamide DEA 7.5 25 Cocamidopropyl betaine 20.0 Cocamide MEA 3.0 Keratin fraction 0.5 Fragrance qs Preservative qs 30 Water qs WO 2004/047774 PCT/NZ2003/000263 16 Post-perming solution Keratin fraction 0.5% Cocamidopropyl dimethylamine oxide 10.0 PPG-5 -ceteth-10-phosphate 0.5 5 Glycerin 3.0 Hydroxypropyl methylcellulose 1.5 Fragrance qs Preservative qs Water qs to 100 10 Moisturising cream Cetearyl alcohol and ceteareth-20 5.0% Cetearyl Alcohol 2.0 Mineral oil (light) 5.0 15 Keratin fraction 0.5 Preservative 0.3 Fragrance q.s Water qs to 100 20 Hand and Body Lotion Polyglyceryl-3 methylglucose distearate 4.0% Stearyi/behenyl beesawaxate 3.0 Octyldodecanol 4.0 25 Avocado oil 6.0 Mineral oil 3.0 Jojoba oil 2.0 Keratin fraction 0.5 Ceramide III 0.2 30 Propylene glycol 3.0 Preservative q.s WO 2004/047774 PCT/NZ2003/000263 17 Fragrance (Parfum) q.s Water (aqua) q.s. to 100 Anti-Wrinkle Treatment Cream 5 Sodium behenoyl lactylate 2.0% Cetearyl alcohol 3.0 Glyceryl stearate 2.6 Isopropyl palmitate 6.0 Sunflower seed oil 6.0 10 Keratin fraction 0.5 Glycerine 3.0 Magnesium ascorbyl phosphate (and) lecithin 6.0 (Rovisome-C, R.L.T.A) Preservative q.s. 15 Water q.s. to 100 Facial Moisture Cream Myristyl lactate 3.0% Laneth-25 (and) ceteth-25 (and) oleth-25 (and) 1.0 20 Steareth-25 (Solulan 25, Amexchol) Mineral oil (70 visc.) 16.5 Petrolaium 3.0 Tocotrienol 1.0 Carbomer 934 0.75 25 Keratin fraction 0.5 Triethanolamine (10% aq) 7.5 Preservative q.s Fragrance q.s. Water q.s. to 100 30 Moisturising Body Lotion WO 2004/047774 PCT/NZ2003/000263 18 Methy] glucose dioleate 2.0% Methyl glucose sesquistearate 1.5 Methyl gluceth-20 distearate 1.5 Cetearyl alcohol (and) ceteareth-20 1.5 5 Isopropyl palmitate 3.0 Ceramide 3, hexyldecanol 2.0 Methyl gluceth-10 3.0 Keratin fraction 0.5 Carbomer l342 0.2 10 Triethanolamine 0.2 Fragrance q.s. Preservative q.s. Water q.s to 100 15 Cationic Emollient Lotion Isostearamidopropyl laurylacetodimonium 5.0% chloride Lactamide MEA 3.0 Isostearyl neopsntanoate 15.0 20 Myristyl myristate 1.0 Cetyl alcohol 4.0 Glycery7l isostearate 3.5 Keratin fraction 0.5 Preservative q.s. 25 Water q s to 100 Men's facial Conditioner Carbomer (Ultrez 10 Carbopol) 0.4% Propylene glycol 1.0 30 PPG-5-buteth 0.5 Beta glucan 2.0 WO 2004/047774 PCT/NZ2003/000263 19 PEG-60 hydragenated castor oil 0.5 Triethanolamine (99%) 0.4 Keratin fraction 0.5 SD-39 C alcohol (Quantum) 5.0 5 Fragrance q.s. Preservative q.s. Water q.s. to 100 Moisturising After Shave Treatment 10 Ceteareth-12 (and) ceteareth-20 (and) cetearyl 6.0% alcohol (and) cetyl palmitate (and) glyceryl stearate (Emulgade SE, Henkel) Cetearyl alcohol 1.0 15 Dicaprylyl ether 8.0 Octyldotiecanol 4.0 Glycerin 3.0 Carbomer (Ultrez 10 Carbopol) 0.3 Keratin fraction 0.5 20 Bisabolol 0.2 Ethyl alcohol 3.0 Water (and) sodium hyaluronate, (and) wheat 4.0 (triticum vulgare) germ extract (and) saccaromyces (and) cerevisiae extract (Eashave, Pentapharm) 25 Triethaolamine q.s. Fragrance q.s. Preservative q.S. Water q.s. to. 100 30 Antioxidant cream Glycerin (99.7%) 3.0% WO 2004/047774 PCT/NZ2003/000263 20 Xanthan gum 0.15 Disodium EDTA 0. 05 Hydrogenated polyisobutene 1.0 Isopropyl palmitate 5.0 5 Petrolanum 0.75 Dimethicone 0.75 Cyclopentasiloxane 3.0 Steareth-2 1.0 PEG-100 stearate 1.9 10 Cetyl alcohol 2.0 Ethylhexyl palmitate 3.0 Polyacrylamide (and) C13-14 isoparaffin (and) 2.0 laureth-7 (sepigel 305, Seppic) Keratin fraction 0.5 15 Glycerin (and) water (and) vitis vinitera (grape) 0.5 seed extract (Collaborative) Fragrance q.s. Preservative q.s. Water q.s.to 100 20 Liquid detergent Sodium laureth sulphate 50.0% Cocamide DEA 3.0 Keratin fraction 0.25 25 Sodium chloride qs Preservative qs Citric acid qs Water qs to 100 30 Shower Gel Sodium laureth sulphate 35.0% WO 2004/047774 PCT/NZ2003/000263 21 Sodium lauroyl sarcosinate 5.0 Cocoamidopropyl becaine 10.0 Cocoamidopropyl hydroxyl sultaine 5.0 Glycerine 2.0 5 Keratin fraction 0.15 Tetrasodium EDTA 0.25 Citric acid qs Fragrance qs Preservative qs 10 Water qs to lOO Foaming bath gel TEA lauryl sulphate 40.0% Lauroyl diethanolamide 10.0 15 Linoleic diethanolamide 7.0 PEG-75 lanolin oil 5.0 Keratin fraction 0.25 Tetrasodium EDTA 0.5 Fragrance qs 20 Preservative qs Dyes qs Water qs to 100 Nail Polish 25 For this example it is convenient to provide the keratin fraction as a dry powder, in the form of the S-sulfonic acid. First coat Keratin fraction (SIFP) 10.0% 30 Sodium hydroxide (4%) 10.0 Keratin fraction (SHSP or SPEP) qs WO 2004/047774 PCT/NZ2003/000263 22 Sodium lauryl sulphate qs Dye ar Pigment qs Water qs to l00 5 Nail Glosser keratin fraction (SIFP) 10.0% Keratin fraction (SHSP or sulfonated keratin peptide} qs Sodium hydroxide (40/0) 10.0 Sodium lauryl sulphate qs 10 Water qs to lOO Hardener Citric acid 21.0% Water 79.0 15 Mascara PEG-8 3.0% Xanthan gum 0.50 Tetrahydroxypropyl erhylanediamine 1.3 20 Carnauba wax 8.0 Beeswax 4.0 Isoeicosame 4.0 Polyisobutene 4.0 Stearic acid 5.0 25 Glyceryl stearate 1.0 Keratin fraction 0.25 Pigments 10.0 Polyurethane- 8.0 VP/VA Copolymer 2.0 30 Preservative qs Fragrance qs WO 2004/047774 PCT/NZ2003/000263 23 Water qs to l00 Liquid Foundation Polysorbate 80 0.1% 5 Potassium hydroxide 0.98 keratin fraction 0.25 Titanium dioxide/talc, 80% 0.1 Talc 3.76 Yellow iron oxide/talc, 80% 0.8 10 Red iron oxide/talc, 80% 0.38 Black iron oxide/talc, 80% 0.06 Propylene glycol 6.0 Magnesium aluminum silicate 1.0 Cellulose gum 0.12 15 di-PPG-3 myristyl ether adipate 12.0 Cetearyl alcohol (and) ceteth-20 phosphate (and) 3.0 dicetyl phosphate (Crodafos CS 20 Acid) Steareth-10 2.0 Cetyl alcohol 0.62 20 Steareth-2 0.5 Preservative qs Water qs to 100 Shaving Cream 25 Sodium cocosulfate 5.0% Keratin fraction 0.25 Glycerin 7.0 Disodium lauryl sulfosuccinate 50.0 Disodium EDTA qs 30 Sodium chloride qs Citric acid qs WO 2004/047774 PCT/NZ2003/000263 24 Fragrance qs Preservative qs Water qs to 100 5 Lipstick Octyldodecanol 22.0% Oieyl alcohol 8.0 Keratin fraction 0.16 C30-45 alkyl methicone 20.0 10 Lanolin oil 14.0 Petrolatum 5.0 Bentone 36 (Rheox) 0.6 Tenox 20 (Eastman) 0.1 Pigment/castor oil 10.0 15 Preservative qs Cyclomethicone qs to 100 Sulfite Hair Straightener 20 Carbomer (Carbopol 940) 1.5% Ammonium bisulphate 9.0 Diethylene urea 10.0 Cetearth 20 2.0 25 Keratin fraction 0.5 Fragrance qs Ammonium hydroxide 28% qs to pH 7.2 Water qs to 100 30 Post straightening nentralising solution WO 2004/047774 PCT/NZ2003/000263 25 Sodium bicarbonate 2.35% Sodium carbonate 2.94 EDTA 0.15 Cetearth 20 0.2 5 Keratin fraction 0.5 Fragrance qs Water qs to 100 Pre-relaxer Conditioner 10 Cationic polyamine 2.0% Imidazolidinyl urea 0.25 Keratin fraction 0.5 Fragrance qs 15 Preservative qs Water qs to 100 Alkali Metal Hydroxide Straightener (Lye) 20 Bemonite 1.0% Sodium Lauryl Sulphate 1.5 PEG-75 lanolin 1.5 Petrolatum 12.0 Cetearyl alcohol 12.0 25 Sodium hydroxide 3.1 Keratin fraction 0.5 Fragrance qs Water qs to 100 30 Post Relaxing Shampoo WO 2004/047774 PCT/NZ2003/000263 26 Sodium lauryl sulphate 10.0% Cocamide DEA 3.0 EDTA 0.2 Keratin fraction 0.5 5 Citric acid qs to pH 5.0 Fragrance qs Preservative qs Water qs to 100 10 Hair tonic/cuticle cover Glycerine 5.5% EDTA 0.07 Carbomer (Carbopol Ultrez 10) 0.33 15 Triethanolamine (20%) 1.0 Keratin fraction 0.5 Ethanol 10.0 Preservative qs Water qs to 100 20 Leave in hair conditioner Cetyl alcohol 5.0% Glyceryl stearate 3.0 25 Petrolatum 0.7 Isopropyl myristate 1.5 Polysorbate 60 1.0 Dimethiconol & cyciomethicone 4.0 Glycerine 7.0 30 EDTA 0.1 D-panthenol 0.2 WO 2004/047774 PCT/NZ2003/000263 27 Keratin fraction 0.5 Cyclomethicone 4.0 Fragrance qs Preservative qs 5 Water qs to 100 Post Hair-dyeing Conditoner 10 Quatemium-40 2.0% Keratin fraction 0.5 Amphoteric-2 4.0 Hydroxyethyl cellulose 2.0 Phosphoric acid qs to pH 4.5 15 Fragrance qs Water qs to 100 Temporary Hair Colouring Styling Gel 20 Dimethicone copolyol 1.5% PPG-10 methyl glucose ether 1.0 Polyvinypyrolidone 2.5 Trisopropanolamine 1. l Carbomer (Carbopol 940) 0.6 25 Laureth-23 1.0 Phenoxyethanol 0.2 Keratin fraction 0.5 EDTA 0.01 D&C orange 4 0.12 30 Ext D&C Violet 2 0.02 FD&C yellow 6 0.02 WO 2004/047774 PCT/NZ2003/000263 28 Ethanol 5.0 Fragrance qs Water qs to 100 5 Formulations containing keratin fractions may improve the cosmetic properties of hair. This is illustrated by the following examples. Example 1: Strengthening 10 Instron method Hair fibres placed in water prior to measurement with Instron tensile tester. Load cell 10N, Load range 10%, speed 30mm/min, gauge length 15mm. Energy required to extend individual hair fibres by 2% and 20% was recorded for 50 fibres and averaged. 15 Materials Perming solution 8% thioglycollic acid, pH adjusted to 8 with ammonia solution, 20 Perming Neutraliser 2.5% hydrogen peroxide Bleaching solution 9% hydrogen, peroxide, 1% ammonium persulfate, pH 8.3 25 Hair straightening (relaxing) solution 2.5% sodium hydroxide Relaxer Neutraliser 30 9.5% citric acid WO 2004/047774 PCT/NZ2003/000263 29 Perming protocol 1. Hair fibres [-4cm in length) from the same source (caucasian) were immersed in perming solution for 3 hours. 2. Placed in the neutralising solution for 30 min and air dried. 5 3. Placed in a solution containing the appropriate amount of keratin fraction for 30 min. 4. Treated fibres were rinsed, dried and equilibrated at 50% relative humidity, 23 °C overnight in the case of the "wash off" procedure. The rinsing step was omitted in the case off the "leave on" procedure. 10 5. Energy required to extend measured on Instron apparatus, Bleaching protocol 1. Hair fibres (~4cm in length) from the same source (Caucasian) were immersed in 15 bleaching solution for 3 hours. 2. Placed in a solution containing the appropriate amount of keratin fraction for 30 min. 3. Rinsed, dried and equilibrated at 50% relative humidity, 23 °C overnight. 4. Energy required to extend measured on Instron apparatus. 20 Relaxing protocol 1. Hair fibres (—4cm in length) from the same source (caucesian) were immersed in relaxing solution for 30 min. 2. Placed in the neutralising solution for 5 min, rinsed in RO water and air dried. 25 3. Placed in a solution containing the appropriate amount of keratin fraction for 30 min. 4. Rinsed, dried and equilibrated at 50% relative humidity, 23 °C overnight. 5. Energy required to extend measured on Instron apparatus. WO 2004/047774 PCT/NZ2003/000263 30 Test example 1: Perming protocol used with keratin fraction of 5% SIFF (supplied as a 5% aqueous solution) i.e. 0.25% active. Instron tensile tester method as described previously. Results are shown in Table 4 and Figure l. Table 4. Instron test results for permed, and undamaged hair fibres treated with. 5% SIFP. Results expressed, as average energy (millijoules) requited to extend hair fibres by 2 and 20% of the gauge length (15mm.). 10 This study indicates that hair fibres which have been weakened by a perming process regain strength following treatment with a solution containing a keratin fraction in both wash off and leave on protocols. The increase in energy needed to extend the permed/keratin treated fibres relative to the permed fibres was measured statistically using the student's t test and found to be significant in all cases. 15 Test example 2: Perming protocol used with keratin fraction of 2% SIFP (supplied as a 5% aqueous solution) i.e. 0.1% active. Instron tensile tester method as described previously. Results are shown in Table 5 and Figure 2. WO 2004/047774 PCT/NZ2003/000263 31 Table 5. Instron test results for permed and undamaged hair fibres treated with 2% SIFP. Results expressed as average energy (millijoules) required to extend hair fibres by 2 and 20% of the gauge length (15mm). 5 This study shows that permed hair fibres are strengthed after treatment with a 0.1% active solution of keratin fraction when it is used as part of a leave on protocol. The difference was analysed statistically using the Student's t test and found to be statistically significant (p 10 Test example 3. Bleaching protocol used with keratin fraction of 5% SIFP (supplied as a 5% aqueous solution) i.e. 0.25% active. Instron tensile tester method as described previously. Results are shown Table 6 and Figure 3. 15 Table 6. Instron test results for bleached and undamaged hair fibres treated with 5% SIFP. Results expressed as average energy (millijoules) required to extend hair fibres by 20% of the gauge length (15mm). This study indicates that hair fibres which have been subjected to bleaching have 20 increased strength following treatment with a solution containing 0.25% active keratin protein fraction as part of a leave on protocol. The difference was analysed statistically using the Student's t test and found to be statistically significant (p Test example 4. Relaxing protocol used with keratin fraction of 2% SIFP (supplied as a 25 5% aqueous solution) i.e. 0.1% active. Instron tensile tester method as described previously. Results are shown in Table 7 and Figure 4. WO 2004/047774 PCT/NZ2003/000263 32 Table 7. Instron test results for relaxed and undamaged hair fibres treated with 2% SIFP. Results expressed as average energy (millijoules) required to extend hair fibres by 20% of the gauge length (15mm). 5 This study indicates that hair fibres Which have been subjected to a hair straighteneing procedure have increased strength following treatment with a solution containing 0.1 % active keratin protein fraction as part of a wash off protocol. The difference was analysed statistically using the Student's t test and found to be statistically significant. 10 (p Test examples 1-4 demonstrate the keratin protein fractions impart a strengthening effect (as measured by an increase in the energy required to extend individual hair fibres) on hair which has been subjected to perming, bleaching and straightening which 15 are routinely used cosmetic treatments. Example 2: Substantivity 20 Keratin Shampoo Fomulation % by weight Ammonium lauryl sulphate (28 %) 25.0 Disodium laureth sulfosuccinate 20.0 Cocamidopropyl betaine 8.0 25 Preservative 0.3 Keratin fraction 0.5 WO 2004/047774 PCT/NZ2003/000263 33 Sodium chloride (20%) q.s Water q.s to 100 Experimental procedure 5 Hair swatches 2-3g were used. Experiments were performed in duplicate. Swatches were shampooed prior to use to remove residual conditioning agents. Swatches were either left undamaged, or were subjected to multiple perming procedures or bleaching procedures. 10 Swatches were equilibrated at 50% RH and weighed accurately. Keratin fractions were applied to the swatches either from an aqueous solution or as part of a shampoo formulation at a level of 3.0ml per swatch. The treatment solution was spread onto the swatch with fingertips, allowed to absorb for 1 min and rinsed under a stream of RO water. 15 The swatch was air-dried and equilibrated at 50% RH for 24 in prior to weighing. Results are summarized in Table 8 and Figure 5. WO 2004/047774 PCT/NZ2003/000263 34 Table 8: Percentage weight gain at 50% relative humidity for damaged and undamaged hair with and without treatment with a solution or shampoo formulation containing SIFP,SHSP and SPEP. 5 This study indicates that the SIFP keratin fraction is substantive to undamaged, permed and bleached hair from both an aqueous solution and shampoo formulation. The SHSP keratin fraction is also substantive from an aqueous solution and shampoo fomulation and seems to adsorb to a greater extent to bleached and permed hair and when applied as a solution rather than a shampoo. The keratin fraction which has molecular weight 10 less than 1kD, SPEP, is substantive to bleached and permed hair from an aqueous solution and shampoo however it was not associated with a weight increase on undamaged hair. A much greater weight increase was observed from an aqueous solution indicating that the surfactants present in the shampoo may be removing the keratin fraction. 15 These results indicate that the different keratin fractions have different surface activity on the hair fibre. The larger fractions have a greater ability to form adsorbing layers and convey a conditioning and smoothing (gloss) effect compared with the low molecular weight SPEP. 20 Example 3: Moisturisation Experimental procedure Hair swatches 2-3 g were used Each treatment within the experiment was performed in 25 duplicate. Swatches were shampooed with a high surfactant (non-conditioning) shampoo prior to use to remove residual conditioning agents. Swatches were either left undamaged, or were subjected to multiple perming or bleaching procedures. 30 Swatches were equilibrated at 50% RH for 24 hrs and weighed accurately. Swatches were equilibrated at 73% RH for 24 hrs and weighed accurately. WO 2004/047774 PCT/NZ2003/000263 35 The difference in weight as a result of increased humidity (in the absence of protein treatment) was calculated. Swatches were treated (in duplicate) with either an aqueous solution containing a keratin fraction or a shampoo containing a keratin fraction (as described earlier). 5 Swatches were equilibrated for 24 hrs and weighed at 50% RH. Swatches were equilibrated for 24 hr and weighed at 73% RH. The difference in weight as a result of increased humidity following treatment with a keratin solution or shampoo was calculated. 10 Results are summarised in Table 9 and Figure 6. Table 9. Percentage weight increase with increasing relative humidity for damaged and undamaged hair fibres treated with an aqueous solution or a shampoo containing SIFP, 15 SHSP or SPEP. This study idicates moisturisation cculd be increased or decreased depending on the keratin fraction apphlied. The SIFP keratin fraction decreased moisture uptake of WO 2004/047774 PCT/NZ2003/000263 36 permed, bleached and undamaged hair at high humidity when applied as an aqueous solution or in a shampoo. The SHSP fraction had less of an effect on moisture uptake at high humidity and there 5 was some indication that moisturisation decreased when applied from a shampoo in preference to an aqueous solution. SPEP increased moisture uptake particularly when applied from a shampoo. 10 Example 4: Foaming of formulations Experimental procedure Waring Blender Test Method: 15 1. Prepare 100 mL of a 5% solution of material to be tested. 2. Pour into blender. 3. Blend for 1 minute on high. 4. Pour all the liquid into 500 mL measuring cylinder, 5. Record the amount of foam (-100 ml,) immediately and record. 20 6. Record the amount of foam, in mLs after 5 minutes: (this will give "low foam" measurement) Test example 7. Comparison of foaming of keratin fraction with common surfactants 25 and effect of adding 0.5% metal ion sequesterant ethylenediammine tetracetic acid (EDTA). Waring bleeder test applied. 30 Results are summarized in Table 1.0 and Figure 7. WO 2004/047774 PCT/NZ2003/000263 37 Table 10. Foam quantity and stability in a waring blender test. Results are expressed as. foam volume immediately following blending and after 5 minutes. 5 This study indicates that the SIFP keratin fraction shows mild foaming and forms stable foams. The SHSP fraction displayed intermediate foaming ability and formed very stable foams. SPEP formed unstable foams. The addition of the ion sequestering agent EDTA increased the foaming capacity of all fractions. 10 Test example 8, Foaming properties of keratin fraction mixtures. Keratin fractions were combined and the waring blender test used to assess foaming. Results are summarised in Table 11. WO 2004/047774 PCT/NZ2003/000263 38 Table 11: Foam quantity and stability of keratin fraction mixtures in a waring blender test. Results are expressed as foam volume immediately following blending and after 5 minutes. 5 This study indicates that addition of the SHSP keratin fraction to the less foaming SIFP fraction increases the foam capacity. Test example 9. Foaming of shampoo formulations containing keratin fractions. Shampoo formulation described earlier, containing 0.5% active keratin fraction. 10 Waring blender test results summarized in Table 12 and Figure 8. Table 12. Foam quantity and stability of shampoo with and without SIFP, SHSP and SPEP in a waring blender test Results are expressed as foam volume immediately 15 following blending and after 5 minutes. It is known that proteins of ten have an adverse effect of foaming in formulations. This study indicates that addition of the SIFP keratin fraction to a shampoo formulation does not have a deleterious effect on foaming, moreover there is some evidence that 20 foam stability in increased. Furthermore addition of the SHSP fraction to a shampoo formulation increases the foaming capacity and results in a greater foam after i minutes compared to that in the absence of the keratin. The SPEP keratin fraction does suppress foam formation. 25 Example 5: Subjective assessment of keratiu fractions in shampoo formulation WO 2004/047774 PCT/NZ2003/000263 39 Method Human volunteers were given two unlabelled shampoo formulations (described earlier), one of which contained 0.5% active of the SIFP keratin fraction. Volunteers were asked to wash their hair with one sample as many times as usual over 5 the period of one week and then repeat with the other sample. Volunteers were then given a questionnaire to fill out ranking each sample in terms of foaming ability, gloss impartment, hair feel, combablility, and appearance. The lower number was associated with an undesirable effect eg in the case of combability 1= extremely difficult to comb and 6 = excellent combability. 10 Test example 10 Questionnaires were collected and the scores recorded and averaged. Results are summarized in Table 13 and Figure 9. 15 Table 13. Subjective assessment of a shampoo formulation with and without SIFP. Results are an average of scores recorded by human volunteers. This study indicates that volunteers did net observe a major change in foaming of the 20 shampoo formulation as a result of addition of the keratin fraction. Moreover the presence of the keratin fraction was observed to impart superior gloss, feel, combability and improved appearance to the formalation indicating that it was acting as a conditioning agent. WO 2004/047774 PCT/NZ2003/000263 40 Whilst the invention has been described with reference to the above Examples, it will be appreciated that numerous improvements and modifacations may be made without departing from the scope of the invention as set out in this specification. 5 Industrial Applicability The compositions described in the application will be useful in a wide range of personal care products such as shampoos, gels, conditioners, creams and detergents and including cosmetics such as moisturiziers, lotions, creams and gels. PCT/NZ20O3/000263 Received 13 October 2004 41 Claims 1. A personal care formulation containing an s -sulfonated keratin protein fraction. 5 2. A personal care formulation as claimed in claim 1 wherein the keratin protein fraction is intact. 3. A personal care formulation as claimed in claim 1 wherein the keratin protein fraction is hydrolysed. 10 4. A personal care formulation as claimed in any one of claims 1 to 3 wherein the keratin protein fraction is from the intermediate filament protein family. 5. A personal care formulation as claimed in any one of claims 1 to 3 wherein the 15 keretin protein fraction is from the high sulfur protein family. 6. A personal care formulation according to claim 4 wherein the cysteine content of the keratin protein is around 4%. 20 7. A personal care formulation according to claim 5 wherein the cysteine content of the keratin protein is greater than 10%. 8. A personal care formulation as claimed in any one of claims 1 to 3 wherein the keratin protein fraction is from the high glycine-tyrosine protein family. 25 9. A personal care formulation containing from about 0.001% to 50% of an s- sulfonated keratin protein fraction. 10. A personal care formulation according to claim 9 containing from 0.001% to 10% 30 of an s-sulfonated keratin protein fraction. AMENDED SHEET IPEA/AU PCT/NZ2O03/000263 Received 22 December 2004 42 11. A personal care formulation according to, claim 10 containing from 0.001 % to 1 % of an s-sulfonated keratin protein fraction. 12. A personal care formulation, according to any one of claims 9-11 wherein the 5 keratin protein fraction is intact 13. A personal care formulation acconding to any one of claims 9-11 wherein the karatein protein fraction is hydrolysed. 10 14. A personal care formulation according to any one of claims 12 to 13 wherein, the keratin protein fraction is from-the intemediate filament protein family. 15. A personal care fonnulaticn according to any one of claims 12 to 13 wherein the keratin protein fraotion is from the high sulfer protein family. 15 16. A personal care fomulation according to claim 14 wherein the cysteine content of the keratin protein is around 4%. 17. A personal care formulation according to claim 15 wherein the cysteine content of 20 the keratin protein is greater than 10%. 18. A personal care formulation according to any one of claims 12 to 13 wherein the keratin protein fraction is from the high glycine-tyrosine protein family. 25 19. An additive comprising an S-sulfonated keratin protein fraction, when used in a personal care formulation. 20. An additive according to claim 19 wherin the protein fraction is intact. 30 21. An additive according to claim 19 wherein the protein fraction is hydrolysed. Amended Sheet IPEA/AU PCT/NZ20O3/000263 Received 13 October 2004 43 22. An additive according to any one of claims 19 to 21 wherein the protein fraction is from the intermediate filament protein family. 23. An additive according to any one of claims 19 to 21 wheretin the protein fraction is 5 from the high sulfur protein family. 24. An additive according to claim 22 wherein the cysteine content of the protein is around 4%. 10 25. An additive according to claim 23 whererin the cysteine content of the protein is greater than 10%. 26. An additive according to any one of claims 19 to 21 wherein the protein fraction is from the high glycine-tyrosins protein family. 15 27. An additive for a personal care formulation that contains from 0.001% to 50% of an s-sulfonated keratin of protein fraction. 28. An additive according to claim 27 containing from 0.001% to 10% of an s- 20 sulfonated keratin protein fraction. 29. An additive according to claim 29 containing from 0.001% to 1% of an s- sulfonated keratin protein fraction. 25 30. An additive according to any one of claims 29-29 wherein the keratin protein fraction is intact. 31. An additive according to any one of claims 27-29 wherein the keratin protein fraction is hydrolysed. 30 AMENDED SHEET IPEA/AIJ PCT/NZ2O03/O00263 Received 13 October 2004 44 32. An additive according to any one of claims 30 to 31 wherein the keratin protein fraction is from the intermediate filament protein family. 33. An additive according to any one of claims 30 to 31 wherein the keratin protein 5 fraction is from the high sulphur protein family. 34. An additive according to claim 32 wherein the cysteine content of the keratin protein is around 4%. 10 35. An additive according to claim 33 wherein the cysteine content of the keratin protein is greater than 10%. 36. An additive as claimed in any one of claims 27-31 wherein the keratin protein fraction is from the high glycine-tyrosine protein family 15 37. A method of using a personal carr formulation as claimed in any one of claims 1- 18. 38. A method of treating hair comprising the use of a formulation or additive 20 according to any one of claims 1 -36. AMENDED SHEET IPEA/AU The application describes a range of personal care products than include a keratin protein fraction. The fraction may be intact or hydrolysed. It is preferably S-sulfonated. The content of the fraction may range from 0.001% to 50%. In most formulations is content will be less than 1% although in a certain products such as nail care products the content will be higher. A wide range of personal care products are described including shampoos body gels and lotions, conditioners, creams and cosmetics generally.

Full Text

1

Field of the Invention
5 The invention relates to personal care formulations containing keratin and their use in
cosmetics.
Background of the invention
Proteins and their derivatives are used in a wide range of personal care formulations,
10 including those intended for use on the hair, skin and nails. As a component of personal
care formulations, proteins perform many functions, including conditioning, film
forming, as a humectant and an emollient. Most commonly used proteins are
hydrolysed in order to impart sufficient solubility to facilitate inclusion in a formulation.
This is particularly the case with keratin proteins, which, are inherently insoluble due to
15 the crosslinks associated with the characteristically high degree of cysteine present in
the protein. Numerous examples of the use of hydrolysed proteins, including keratins,
in personal care formulations are known in the art.
WO9851265 discloses the use of hydrolysed proteins and their derivatives, particularly
20 those with high, sulfur content, in formulations to protect hair from the insults of
environmental and chemical damage. The inventors in WO9851265 use a combination
of hydrolysed proteins and a polyamino cationic agent in order to prepare the desired
formulations.
25 US4948876 describes an S-sulphocysteine keratin peptide produced by enzymatic
hydrolysis for use as an auxiliary in the dyeing of wool and hair Enzymatic digestion is
used by the authors to prepare low molecular weight peptides and achieve the desired
solubility.

WO 2004/047774 PCT/NZ2003/000263
2
US4S95722 discusses the use of a range of keratin decomposition products, including
those obtained by chemical and enzymatic hydrolysis, for the preparation of cosmetic
products.
5 Keratin fibres, such as human hair, wool and other animal fibres, consist of a complex
mix of relaxed proteins that, are all part of the keratin family. These proteins can be
grouped according to their structure and role within the fibre into the following groups:
the intermediate filament proteins (IFP), which are fibrous proteins found mostly
10 in the fibre cortex;
high sulfur proteins (HSP), which are globular proteins found in the matrix of
the fibre cortex, as well as in the cuticle.
15 high glycine-tyrosine proteins (HGTP), found mostly in the fibre cortex.
The ulrastrucrture of keratin fibres is well known in the art, and discussed in detail by R.
C. Marshall, D. F. G. Orwin and J. M. Gillespie, Structure and Biochemistry of
Mammalian Hard Keratin, Electron Microscopy Reviews, 4, 47,1991. In the prior art
20 described in which proteins are used as a cosmetic ingredient, the keratin utilized is
hydrolysed as one material, with no attempt at fractionating the keratin source into its
constituent components. As a result of protien hydrolysis, many of the desirable
properties of the proteins are lost. Low molecular weight keratin peptides aggregate
with a much lower degree of order to produce materials with much poorer physical
25 properties than the high molecular weight keratins from which they are derived. In
addition, irreversible conversion of cysteine as may occur with chemical methods of
keratin, decomposition, yields, a peptide product that has lost the core functionality than
that distinguishes it from other protein materials.

WO 2004/047774 PCT/NZ2003/000263
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The need exists for personal care formulations which use intact keratins which maintain
many of the desirable characteristics of the native keratins from which they are derived
and possess a reactivity towards keratin substrates.
5 Object of the Invention
It is an object of The invention to provide a personal care formulation which uses a
keratin protein or to at least provide the public with a useful choice.
Summary of the Invention
10 The invention provides a personal care formulation including a keratin protein fraction.
The keratin protein fraction may be intact.
The invention also provides a personal care formulation in which the karatin protein
15 fraction is hydrolysed.
In particular, the invention provides a personal care formulation including a keratin
protein fraction which is S-sulfonated.
20 The invention provides personal care formulations in which the keratin protein fraction
is from the intermediate filament protein family.
The invention also provides a personal care formulation in which the keratin protein
fraction is from the high sulfur protein family.
25
The cysteine content of the keratin protein may be about 4%,
The invention also provides a personal care formulation in which the keratin protein
fraction is from the high glycine-tyrosine protein family.
30

WO 2004/047774 PCT/NZ2003/000263
4
Preferably the percentege of the intact S-sulfonated keratin protein fraction in the
formulation is less than ten percent by weight.
More preferably the ratio is between 0.001 and 1% inclusive by weight. However the
5 ratio may be from 0.001 % to 50% of keratin protein fraction.
The invention also provides a personal care fomation containing about 0.001% to 50%
of a keratin protein fraction.
10 The ratio is preferably 0.001 % to 10% and more preferably 0.001 % to 1 %.
The invention also provides an additive for a personal care formation comprising a
keratin protein fraction.
15 The personal care formulations may include the following:
Coaditioning shampoo;
Body/Facial cleanser/shampoo;
Hair conditioner;
Hair gel;
20 Hair mouse, setting lotion;
Hairspray,
Pre-perming solution;
Post-pesrming solution;
Moisturing cream;
25 Shower gel;
Foaming bath gel;
Mascara;
Nail polish
Liquid foundation.
30 Shaving cream; and
Lipstick.

WO 2004/047774 PCT/NZ2003/000263
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However other personal care formulations are included within the invention.
The invention also provides a personal care formulation including an intact sulfonated
5 keratin fraction wherein the ratio of keratin fraction is about 10% of the formulation.
The formulation is adapted to be used as a nail polish or nail glosser.
The personal care formulations comprise a suitable percentage by weight of a cosmetic
carrier.
10
Additional elements such as vitamins and minerals may be added to enhance the
protective efficacy of the formulations.
Sunscreen factors with ultra-violet protection properties may also be added.
15
The invention also provides a method of using the personal cars fomulation or
additives according to the invention.
Detailed Description of the Drawings
20 The invention will now be described by way of example only in which:
Figure 1 shows instron test results for permed hair fibres treated with 5% SIFP
Figure 2 shows,instron test results for permed hair fibres treated with 2% SIFP
Figure 3 shows instron test results for bleached hair fibres treated with 5% SIFP
Figure 4 shows instron results for relaxed hair fibres treated with 2% SIFP
25 Figure-5 shows, substantivity of SIFP, SHSP and SPEP on undamaged and damaged hair
at 50% relative humidity
Figure 6 shows moisturisation with increasing relative humidity of undamaged and
damaged hair treated with SIFP, SHSP and SPEP
Figure 7 shows foaming results for common surfactants and SIFP, SHSP and SPEP in
30 the presence and absence of EDTA obtained from the waring blender test

WO 2004/047774 PCT/NZ2003/000263
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Figure 8 shows foaming results for shampoo formulations with and without SIFP, SHSP
and SPEP
Figure 9 is a summary of subjective assessment of a shampoo formulation in the
presence and absence of SIFP
5
Detailed Description of the Invention
The hard alpha keratin proteins such as those derived, from human hair, wool, animal
fibres, horns, hooves or other mammalian sources, can be classified into particuolar
components according to their biochemical properties, specifically their molecular
10 weight and amino acid composition. Table 1 illustrates the amino acid composition
determined by conventional analytical methods of typical keratin protein fractions
known in the art and also the subject of this invention. This involves acid hydrolysis of
the analyte which converts all cystine and labile cysteine derivatives to cysteine,
typically recorded as half-cysteine.
15

WO 2004/047774 PCT/NZ2003/000263
7
Table 1 illustrates an amino acid composition of keratin fractions: S-sulfonated karatin
intermediate filament protein (SIFP), peptides derived from S-sulfonated keratin
intermediate filament protein (SIFP-pep), S-sulfonated keratin high sulfur protein
(SHSP), peptides derived from S-sulfonated keratin high sulfur protein (SHSP-pep), S-
5 sufonated keratin peptide (SPEP) as used in the invention. Intermediate filament
protein (IFP), high, sulfur protein (HSP), high glycine-tyrosine protein (HGTP) and
whole wool courtesy of Gillespie and Marshall, Variability in the proteins of wool and
hair, Proc. Sixth Int. Wool Text. Res. Conf., Pretoria, 2, 67-77, 1980. All residues
expressed as mol%. S-sulfocysteine, cystine and cysteine are measured as S-
10 carboxymethyl cysteine following reduction and alkylation, and reported as cys.
Table 2 illustrates -the molecular weight determined by conventional analytical methods
of typical keratin protein fractions known in the art and also the subject of this
invention. Conventional analysis involves cleavage of cystine bonds within the keratin
15 using reduction so that the protein mass is determined in its native, uncrosslinked state,
most similar to the unkeratinised state of the protein. Mass is determined using
polyacrylamide gel electrophoresis. In the case of the peptide SPEP mass is determined
using mass spectrometry. Using these methods the Keratin is made soluble without any
hydrolysis of peptide bonds and an accurate measure of molecular weight is determined.
20

Table 2: Molecular weight of keratin fractions: S-sulfonated keratin intermediate
filament protein (SIFP), peptides derived from S-sulfonated keratin intermediate
Slament protein (SIFP-pep), S-sulfonated keratin high sulfur protein (SHSP), peptides

WO 2004/047774 PCT/NZ2003/000263
8
derived from S-sulfonated keratin high sulfur protein (SHSP-pep), S-sulfonated keratin
peptide (SPEP) as used in the invention. Intermediate filament protein (IFP), high
sulfur protein (HSP) high glycine-tyrosine protein (HGTP) and whole wool courtesy of
Gillespie and Marshall. Variability in the proteins of wool and hair, Proc. Sixth Int.
5 Wool Text. Res. Conf. Pretoria, 2, 67-77, 1980.
Both amino acid composition and molecular weight varies across keratin types, between
species and also within breeds of one species, for example between, wools from different
breeds of sheep. The figures gives in tables 1 and 2 are indicative for the keratin source
10 stated. However, individual types of keratin proteins, or keratin protein, fractions, have
distinctive characteristic, particularly molecular weight and amino acid content.
The subject of the invention is formulations containing intact S-sulfonated keratin
protein fractions. "Intact" refers tO proteins that have not been. significantly hydrolysed,
15 with hydrolysis being defined as the cleavage of bonds through the addition of water.
Gillespie (Biochemistry and physiology of the skin, vol 1, Ed. Goldsmith Oxford
University Press, London, 1983, pp475-510) considers "intact" to refer to proteins in the
keratinized polymeric state and further refers to polypeptide subunits which complex to
form intact keratins in wool and hair. For the purpose of this invention "intat" refers to
20 the polypeptide subunits described by Gillespie. These are equivalent to the keratin
proteins in their native form without the disulfide crosslinks formed through the process
of keratinisation.
Keratin protein fracrtions are distinct groups from within the keratin protein family, such
25 as the intermediate filament, proteins, the high sulfur proteins or the high glycine-
tyrosine proteins well known in the art. Intermediate filament proteins are described in
detail by Orwin et al (Structure and Biochemistry of Manunalian Hard Keratin,
Electron Microscopy Reviews, 4, 47,1991) and also referred to as low sulphur proteins
by Gilliespie (Biochemistry and physiology of the skin, vol 1, Ed. Goldsmith Oxford
30 University Press. London, 1983, pp475-5lO). Key characteristics of this protein family
are molecular weight in the range 40 — 60 kD and a cystene content (measured as half

WO 2004/047774 PCT/NZ2003/000263
9
cystine of around 4%. The high sulfur protein family are also well described by Orwin
and Gillispie in the same publications. This protein family has a large degree of
heterogeity but can be characterised as having a molecular weight in the range 10 — 30
kD and a cysteine consent of greater than 10%. The subset of this family, the ultra high
5 sulfur proteins can have a cysteine content of up to 34%. The high glycine-tryosine
protein family are also well described by Orwin and Gillespie in the same publications.
This family is also referred to as the high tryrosine proteins and has characteristics of a
molecular weight less than 10 KD, a tyrosine content typically greater than 10% and a
glycine content typically greater than 20%.
10
For the purpose of this invention a "keratin protein fraction" is a purified form of
keratin that contains predominantly, although not entirely, one distinct protein group as
described above. In the content of this invention S-Sulfonated keratins, have
cysteine/cystine present predominantly in the form S-sulfocysteine, commonly known
15 as the Bunte salt. This highly polar group imparts a degree of solubility to proteins
Whilst being stable in solution, the S-sulfo group is a labile cysteine derivative, highly
reactive towards thiols, such as cysteine, and other reducing agents. Reaction with
reducing agents leads to conversion of the S-sulfo cysteine group back to cysteine. S-
sulfo cysteine is chemically different to cysteic acid, although both groups contain the
20 SO3 group. Cysteic acid is produced irreversibly by the oxidation of cysteine or cystine
and once formed cannot form disulfide crosslinks back to cysteine. S-sulfocystein is
reactive towards cysteine and readily forms disulfide crosslinks.
One aspect of the invention is personal care formulations containing S-sulfonated
25 keratin intermediate- filament protein (SIFP). These proteins are characterised as having
a molecular weight in the range 40-60kD and a cysteine content determined through
amino acid analysis of around 4%. This material may be prepared by a variety of
methods, including those described in NZ/PCT02/00125. This material has excellent
film forming properties, and can be reconstituted in a variety of ways, such as those
30 outlined in NZ/PCT02/00169. The characteristics of the material arise at least in part
from the intact nature of the fibrous proteins. Intermediate filament proteins are known

WO 2004/047774 PCT/NZ2003/000263
10
to associate on a molecular level, which is fundamental to the reformation of the
proteins into materials. The ability of this material to act as a film former is a useful
cosmetic property. In addition, the S-sulfo group is of use in personal care formulations
as it is highly reactive towards thiols, forming a covalent disulfide bond. Thiols are
5 present in the form of cysteine, particularly in hair damaged through reductive processes
such, as perming. In addition, as a highly polar group, the S-sulfo group is attracted to
polar substrates, such as the surface of hair damaged through oxidation processes and
bleaching. With this type of hair the SIFP can form, salt bridges and hydrogen bonds
and consequently impart a durable conditioning effect.
10
A further aspect of the invention is cosmetic formulations containing S-sulfonated
keratin high sulfur protein (SHSP). These proteins are characterised as having a
molecular weight in the range 10-30kD and a cysteine content determined through
amino acid analysis of greater than 10%. This material may be prepared by a variety of
15 methods, including those described in NZ/PCT02/O0125. As an intact globular protein
derived from the matrix proteins of the keratin fibre cortex, and also the cuticle cells,
this material has the potential to repair damaged hair, in particular where split ends will
allow penetration of this intact protein into the fibre. In addition, with a higher
proportion, of cysteine than commercially available keratin derivatives typically used in
20 personal care formulations, the potential to bind to damaged hair, or to bind to hair
when, used as part of a permanent waving process, is significant.
One aspect of the invention is keratin peptides derived from Keratin protein fractions.
These peptides have a cysteine content similar to the fraction from which the peptide is
25 derived (approximately 4% for SIFP-pep and greater than 10% for SHSP-pep). Being of
low molecular weight these materials can penetrate the surface of hair and skin and
provide cosmetic function within the substrate. This material is differentiated from other
hydrolysed keratins by virtue of being derived from a particular keratin protein fraction,
as well as the cysteine being present as S-sulfo cysteine. A source of peptides with
30 variable amounts of cysteine is of particular value in the formulation of cosmetics.

WO 2004/047774 PCT/NZ2003/000263
11
One aspect of the invention is personal care formulations containing S-sulfonated
keratin peptides derived from bulk keratin. These peptides are characterised as having a
molecular weight approximately lkD or less and a cysteine content determined through
amino acid analysis of approximately 4%. This material may be prepared by a variety
5 of methods, including those described in NZ/PCT02/00125. This material is
differentiated from other hydrolysed keratins by virtue of the cysteine being present in
the form of S-sulfo groups. The low molecular weight of this material allows it to
penetrate through the hair cuticle. This feature, combined with the S-sulfo groups
present on the peptide and the reactivity of this group creates a useful ingredient for the
10 formulation of cosmetics, in particular hair cosmetics.
Keratins are characterised by having a higher cysteine content than other proteins. In
some protein fractions derived from wool cysteine contents as high as 30% have been
reported Cysteine is a known reductant and keratin protein fractions that are the subject
15 of this invention are reductants and antioxidants that can be used as an active
component in personal care formulations targeted at anti ageing, or reducing oxidative
damage to hair and skin caused by free radicals, pollutants and environmental insults.
Measurements of antioxidant properties of keratin protein fractions are detailed in Table
3.
20
Table 3: Antioxidanr activity of keratin fractions. Results expressed as the amount of
Trolox equivalent antioxidant capacity per hundred gram, or milliliters, of sample (umol
TEAC/1O0 g or mol TEAC/100mL), which represents the amount of Trolox (vitamin
25 E) that gives the same response as one hundred grams or mLs. of sample. Triplicate
analyses (at different concentrations) were earned out on each extract. Equivalent

WO 2004/047774 PCT/NZ2003/000263
12
activity calculated on the basis of protein concentration of sample used (SPEP and
SHSP 15% solution SIFP 5% solution).
Personal care formulation includes any substance or preparation intended for placement
5 in contact with any eternal part of the human body, including the mucous membranes
of the oral cavity and the teeth, with a view to:
— altering the odours of the body;
— changing its appearance;
— cleansing it;
10 — maintaining it in good condition; or
— perfuming it,
but does not inchlude any product that is required by law to regulated as a medicine,
as a therapeutic substance or device, as a food or as a nurtritional or dietary supplement.
15 It also includes any personal care formulation intended to improve the appearance.
Unless the contest clearly requires otherwise, throughout the description and the claims,
the words "comprise", "comprising" and the like, are to be construed in an inclusive
sense as opposed to an exclusive or exhaustive sense, that is to say, in the sense of
20 "including, but not limited to".
The invention will now be described, by way of example only and with reference to the
accompanying Examples which, are by way of exemplification only.
25 Examples
In each formulation 'keratin fraction' is included at an indicative level. Keratin fraction
refers to SIFP, SIFP-pep, SHSP, SHSP-pep, HGTP or S-sulfonated keratin peptides, all
of which are described above. Unless otherwise stated, it is convenient to provide the
keratin fraction in the form of a dilute aqueous solution and include the appropriate
30 amount of this solution in the formulation to achieve the keratin fraction level indicated.

WO 2004/047774 PCT/NZ2003/000263
13
Typical concentrations of aqueous solutions for the keratin fraction types are SIFP 5%,
SHSP 15% and S-sulfonated keratin peptides 15%. Therefore, in order to achieve the
indicated level of 0.5% keratin fraction for SIFP, 10% of an SIFP solution would to be
used in the formulation. Percentages are expressed as w/v.
5
Sample formulations
Conditioning shampoo
Sodium, lauryl sulphate 28% 2 5.0%
10 Sodium laureth-2-sulphate 70% 4.0
Cocamide DEA 70% 3.5
Cocamidopropyl betaine (30%) 3.0
Keratin fraction 0.5
Sodium chloride q.s
15 Citric acid q.s
Fragrance q.s
Preservative q.s
Water q.s to 100
Procedure: A Combine 35.0 g water, sodium laureth sulphate and sodium lauryl
20 sulphate. Heat to 65º C until dissolved. Add cocamide DEA and allow to cool. B. Mix
betaine -with water and add to phase A. Add keratin fractioin, adjust the pH to 6.5 with
citric acid. Add preservative and fragrance as required, adjust to desired thickness with
sodium chloride and add remaining water.
25 Hair gel
Carbomer (Carbopol Ultrez 10) 0.5%
Disodium EDTA 0.05
Glycerin 4.0
Triethanolamine (20%) 3.0
30 Keratin fraction 0.45
Preservative q.s

WO 2004/047774 PCT/NZ2003/000263
14
Fragrance q.s
Water q.s to 100
Procedure. A Heat 60.Og of water to 70ºC and add to carbopol, EDTA aud glycerol.
Mix vigorously, Cool. Add triethanolamine to adjust pH to 6.3. Add keratin fraction.
5 Combine preservative and remaining water and add. Mix thoroughly ami add fragrance
as desired.
Clear Body/Facial Cleanser and Shampoo
10 Ammonium lauryl suphate 28% 25.0%
Disodium laureth sulfosuccinate 20.0
Cocamidopropyl betaine 8.0
Keratin fraction 0.5
Sodiuim chloride qs
15 Fragrance (parfum) qs
Preservative qs
Water (aqua) qs to 100
Hair Conditioner
20 Cetrimonium Chloride 5.0%
Stearyl alcohol 4.5
Keratin fraction 0.25
Fragrance qs
Preservative qs
25 Water qs tol00
Hair Mousse
Keratin fraction 0.25%
Hydrogenated tallow trimonium chloride 0.20
30 Nonoxynol-10 0.35
Alcohol 10.0

WO 2004/047774 PCT/NZ2003/000263
15
Butane-48 10.0
Water qs to 100
Setting lotion
5 Carbomer (Carbopol Ultrez 10) 2.0%
Mineral oil (light) 0.20
Keratin fraction 0.25
Alcohol 37.5
Fragrance qs
10 Water qs to lOO
Hairspray
VA/Crotonates/Vinyl Neodeconoate Copolymer 1.60%
(Resyn 28-2930)
15 Aminomethyl propanol 0.15
PEG-75 lanolin 0.20
Keratin fraction 0.25
Alcohol 65.05
Butane 30 28.0
20
Pre-perming solution
TEA- lauryl sulphate 30.0%
Cocamidopropyl dimethylamine oxide 10.0
Cocamide DEA 7.5
25 Cocamidopropyl betaine 20.0
Cocamide MEA 3.0
Keratin fraction 0.5
Fragrance qs
Preservative qs
30 Water qs

WO 2004/047774 PCT/NZ2003/000263
16
Post-perming solution
Keratin fraction 0.5%
Cocamidopropyl dimethylamine oxide 10.0
PPG-5 -ceteth-10-phosphate 0.5
5 Glycerin 3.0
Hydroxypropyl methylcellulose 1.5
Fragrance qs
Preservative qs
Water qs to 100
10
Moisturising cream
Cetearyl alcohol and ceteareth-20 5.0%
Cetearyl Alcohol 2.0
Mineral oil (light) 5.0
15 Keratin fraction 0.5
Preservative 0.3
Fragrance q.s
Water qs to 100
20 Hand and Body Lotion
Polyglyceryl-3 methylglucose distearate 4.0%
Stearyi/behenyl beesawaxate 3.0
Octyldodecanol 4.0
25 Avocado oil 6.0
Mineral oil 3.0
Jojoba oil 2.0
Keratin fraction 0.5
Ceramide III 0.2
30 Propylene glycol 3.0
Preservative q.s

WO 2004/047774 PCT/NZ2003/000263
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Fragrance (Parfum) q.s
Water (aqua) q.s. to 100
Anti-Wrinkle Treatment Cream
5 Sodium behenoyl lactylate 2.0%
Cetearyl alcohol 3.0
Glyceryl stearate 2.6
Isopropyl palmitate 6.0
Sunflower seed oil 6.0
10 Keratin fraction 0.5
Glycerine 3.0
Magnesium ascorbyl phosphate (and) lecithin 6.0
(Rovisome-C, R.L.T.A)
Preservative q.s.
15 Water q.s. to 100
Facial Moisture Cream
Myristyl lactate 3.0%
Laneth-25 (and) ceteth-25 (and) oleth-25 (and) 1.0
20 Steareth-25 (Solulan 25, Amexchol)
Mineral oil (70 visc.) 16.5
Petrolaium 3.0
Tocotrienol 1.0
Carbomer 934 0.75
25 Keratin fraction 0.5
Triethanolamine (10% aq) 7.5
Preservative q.s
Fragrance q.s.
Water q.s. to 100
30
Moisturising Body Lotion

WO 2004/047774 PCT/NZ2003/000263
18
Methy] glucose dioleate 2.0%
Methyl glucose sesquistearate 1.5
Methyl gluceth-20 distearate 1.5
Cetearyl alcohol (and) ceteareth-20 1.5
5 Isopropyl palmitate 3.0
Ceramide 3, hexyldecanol 2.0
Methyl gluceth-10 3.0
Keratin fraction 0.5
Carbomer l342 0.2
10 Triethanolamine 0.2
Fragrance q.s.
Preservative q.s.
Water q.s to 100
15 Cationic Emollient Lotion
Isostearamidopropyl laurylacetodimonium 5.0%
chloride
Lactamide MEA 3.0
Isostearyl neopsntanoate 15.0
20 Myristyl myristate 1.0
Cetyl alcohol 4.0
Glycery7l isostearate 3.5
Keratin fraction 0.5
Preservative q.s.
25 Water q s to 100
Men's facial Conditioner
Carbomer (Ultrez 10 Carbopol) 0.4%
Propylene glycol 1.0
30 PPG-5-buteth 0.5
Beta glucan 2.0

WO 2004/047774 PCT/NZ2003/000263
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PEG-60 hydragenated castor oil 0.5
Triethanolamine (99%) 0.4
Keratin fraction 0.5
SD-39 C alcohol (Quantum) 5.0
5 Fragrance q.s.
Preservative q.s.
Water q.s. to 100
Moisturising After Shave Treatment
10
Ceteareth-12 (and) ceteareth-20 (and) cetearyl 6.0%
alcohol (and) cetyl palmitate (and) glyceryl
stearate (Emulgade SE, Henkel)
Cetearyl alcohol 1.0
15 Dicaprylyl ether 8.0
Octyldotiecanol 4.0
Glycerin 3.0
Carbomer (Ultrez 10 Carbopol) 0.3
Keratin fraction 0.5
20 Bisabolol 0.2
Ethyl alcohol 3.0
Water (and) sodium hyaluronate, (and) wheat 4.0
(triticum vulgare) germ extract (and) saccaromyces
(and) cerevisiae extract (Eashave, Pentapharm)
25 Triethaolamine q.s.
Fragrance q.s.
Preservative q.S.
Water q.s. to. 100
30 Antioxidant cream
Glycerin (99.7%) 3.0%

WO 2004/047774 PCT/NZ2003/000263
20
Xanthan gum 0.15
Disodium EDTA 0. 05
Hydrogenated polyisobutene 1.0
Isopropyl palmitate 5.0
5 Petrolanum 0.75
Dimethicone 0.75
Cyclopentasiloxane 3.0
Steareth-2 1.0
PEG-100 stearate 1.9
10 Cetyl alcohol 2.0
Ethylhexyl palmitate 3.0
Polyacrylamide (and) C13-14 isoparaffin (and) 2.0
laureth-7 (sepigel 305, Seppic)
Keratin fraction 0.5
15 Glycerin (and) water (and) vitis vinitera (grape) 0.5
seed extract (Collaborative)
Fragrance q.s.
Preservative q.s.
Water q.s.to 100
20
Liquid detergent
Sodium laureth sulphate 50.0%
Cocamide DEA 3.0
Keratin fraction 0.25
25 Sodium chloride qs
Preservative qs
Citric acid qs
Water qs to 100
30 Shower Gel
Sodium laureth sulphate 35.0%

WO 2004/047774 PCT/NZ2003/000263
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Sodium lauroyl sarcosinate 5.0
Cocoamidopropyl becaine 10.0
Cocoamidopropyl hydroxyl sultaine 5.0
Glycerine 2.0
5 Keratin fraction 0.15
Tetrasodium EDTA 0.25
Citric acid qs
Fragrance qs
Preservative qs
10 Water qs to lOO
Foaming bath gel
TEA lauryl sulphate 40.0%
Lauroyl diethanolamide 10.0
15 Linoleic diethanolamide 7.0
PEG-75 lanolin oil 5.0
Keratin fraction 0.25
Tetrasodium EDTA 0.5
Fragrance qs
20 Preservative qs
Dyes qs
Water qs to 100
Nail Polish
25 For this example it is convenient to provide the keratin fraction as a dry powder, in the
form of the S-sulfonic acid.
First coat
Keratin fraction (SIFP) 10.0%
30 Sodium hydroxide (4%) 10.0
Keratin fraction (SHSP or SPEP) qs

WO 2004/047774 PCT/NZ2003/000263
22
Sodium lauryl sulphate qs
Dye ar Pigment qs
Water qs to l00
5 Nail Glosser
keratin fraction (SIFP) 10.0%
Keratin fraction (SHSP or sulfonated keratin peptide} qs
Sodium hydroxide (40/0) 10.0
Sodium lauryl sulphate qs
10 Water qs to lOO
Hardener
Citric acid 21.0%
Water 79.0
15
Mascara
PEG-8 3.0%
Xanthan gum 0.50
Tetrahydroxypropyl erhylanediamine 1.3
20 Carnauba wax 8.0
Beeswax 4.0
Isoeicosame 4.0
Polyisobutene 4.0
Stearic acid 5.0
25 Glyceryl stearate 1.0
Keratin fraction 0.25
Pigments 10.0
Polyurethane- 8.0
VP/VA Copolymer 2.0
30 Preservative qs
Fragrance qs

WO 2004/047774 PCT/NZ2003/000263
23
Water qs to l00
Liquid Foundation
Polysorbate 80 0.1%
5 Potassium hydroxide 0.98
keratin fraction 0.25
Titanium dioxide/talc, 80% 0.1
Talc 3.76
Yellow iron oxide/talc, 80% 0.8
10 Red iron oxide/talc, 80% 0.38
Black iron oxide/talc, 80% 0.06
Propylene glycol 6.0
Magnesium aluminum silicate 1.0
Cellulose gum 0.12
15 di-PPG-3 myristyl ether adipate 12.0
Cetearyl alcohol (and) ceteth-20 phosphate (and) 3.0
dicetyl phosphate (Crodafos CS 20 Acid)
Steareth-10 2.0
Cetyl alcohol 0.62
20 Steareth-2 0.5
Preservative qs
Water qs to 100
Shaving Cream
25 Sodium cocosulfate 5.0%
Keratin fraction 0.25
Glycerin 7.0
Disodium lauryl sulfosuccinate 50.0
Disodium EDTA qs
30 Sodium chloride qs
Citric acid qs

WO 2004/047774 PCT/NZ2003/000263
24
Fragrance qs
Preservative qs
Water qs to 100
5 Lipstick
Octyldodecanol 22.0%
Oieyl alcohol 8.0
Keratin fraction 0.16
C30-45 alkyl methicone 20.0
10 Lanolin oil 14.0
Petrolatum 5.0
Bentone 36 (Rheox) 0.6
Tenox 20 (Eastman) 0.1
Pigment/castor oil 10.0
15 Preservative qs
Cyclomethicone qs to 100
Sulfite Hair Straightener
20
Carbomer (Carbopol 940) 1.5%
Ammonium bisulphate 9.0
Diethylene urea 10.0
Cetearth 20 2.0
25 Keratin fraction 0.5
Fragrance qs
Ammonium hydroxide 28% qs to pH 7.2
Water qs to 100
30 Post straightening nentralising solution

WO 2004/047774 PCT/NZ2003/000263
25
Sodium bicarbonate 2.35%
Sodium carbonate 2.94
EDTA 0.15
Cetearth 20 0.2
5 Keratin fraction 0.5
Fragrance qs
Water qs to 100
Pre-relaxer Conditioner
10
Cationic polyamine 2.0%
Imidazolidinyl urea 0.25
Keratin fraction 0.5
Fragrance qs
15 Preservative qs
Water qs to 100
Alkali Metal Hydroxide Straightener (Lye)
20 Bemonite 1.0%
Sodium Lauryl Sulphate 1.5
PEG-75 lanolin 1.5
Petrolatum 12.0
Cetearyl alcohol 12.0
25 Sodium hydroxide 3.1
Keratin fraction 0.5
Fragrance qs
Water qs to 100
30 Post Relaxing Shampoo

WO 2004/047774 PCT/NZ2003/000263
26
Sodium lauryl sulphate 10.0%
Cocamide DEA 3.0
EDTA 0.2
Keratin fraction 0.5
5 Citric acid qs to pH 5.0
Fragrance qs
Preservative qs
Water qs to 100
10 Hair tonic/cuticle cover
Glycerine 5.5%
EDTA 0.07
Carbomer (Carbopol Ultrez 10) 0.33
15 Triethanolamine (20%) 1.0
Keratin fraction 0.5
Ethanol 10.0
Preservative qs
Water qs to 100
20
Leave in hair conditioner
Cetyl alcohol 5.0%
Glyceryl stearate 3.0
25 Petrolatum 0.7
Isopropyl myristate 1.5
Polysorbate 60 1.0
Dimethiconol & cyciomethicone 4.0
Glycerine 7.0
30 EDTA 0.1
D-panthenol 0.2

WO 2004/047774 PCT/NZ2003/000263
27
Keratin fraction 0.5
Cyclomethicone 4.0
Fragrance qs
Preservative qs
5 Water qs to 100
Post Hair-dyeing Conditoner
10 Quatemium-40 2.0%
Keratin fraction 0.5
Amphoteric-2 4.0
Hydroxyethyl cellulose 2.0
Phosphoric acid qs to pH 4.5
15 Fragrance qs
Water qs to 100
Temporary Hair Colouring Styling Gel
20 Dimethicone copolyol 1.5%
PPG-10 methyl glucose ether 1.0
Polyvinypyrolidone 2.5
Trisopropanolamine 1. l
Carbomer (Carbopol 940) 0.6
25 Laureth-23 1.0
Phenoxyethanol 0.2
Keratin fraction 0.5
EDTA 0.01
D&C orange 4 0.12
30 Ext D&C Violet 2 0.02
FD&C yellow 6 0.02

WO 2004/047774 PCT/NZ2003/000263
28
Ethanol 5.0
Fragrance qs
Water qs to 100
5 Formulations containing keratin fractions may improve the cosmetic properties of hair.
This is illustrated by the following examples.
Example 1: Strengthening
10 Instron method
Hair fibres placed in water prior to measurement with Instron tensile tester. Load cell
10N, Load range 10%, speed 30mm/min, gauge length 15mm.
Energy required to extend individual hair fibres by 2% and 20% was recorded for 50
fibres and averaged.
15
Materials
Perming solution
8% thioglycollic acid, pH adjusted to 8 with ammonia solution,
20 Perming Neutraliser
2.5% hydrogen peroxide
Bleaching solution
9% hydrogen, peroxide, 1% ammonium persulfate, pH 8.3
25
Hair straightening (relaxing) solution
2.5% sodium hydroxide
Relaxer Neutraliser
30 9.5% citric acid

WO 2004/047774 PCT/NZ2003/000263
29
Perming protocol
1. Hair fibres [-4cm in length) from the same source (caucasian) were immersed in
perming solution for 3 hours.
2. Placed in the neutralising solution for 30 min and air dried.
5 3. Placed in a solution containing the appropriate amount of keratin fraction for 30
min.
4. Treated fibres were rinsed, dried and equilibrated at 50% relative humidity, 23
°C overnight in the case of the "wash off" procedure. The rinsing step was omitted in
the case off the "leave on" procedure.
10 5. Energy required to extend measured on Instron apparatus,
Bleaching protocol
1. Hair fibres (~4cm in length) from the same source (Caucasian) were immersed in
15 bleaching solution for 3 hours.
2. Placed in a solution containing the appropriate amount of keratin fraction for 30
min.
3. Rinsed, dried and equilibrated at 50% relative humidity, 23 °C overnight.
4. Energy required to extend measured on Instron apparatus.
20
Relaxing protocol
1. Hair fibres (—4cm in length) from the same source (caucesian) were immersed in
relaxing solution for 30 min.
2. Placed in the neutralising solution for 5 min, rinsed in RO water and air dried.
25 3. Placed in a solution containing the appropriate amount of keratin fraction for 30
min.
4. Rinsed, dried and equilibrated at 50% relative humidity, 23 °C overnight.
5. Energy required to extend measured on Instron apparatus.

WO 2004/047774 PCT/NZ2003/000263
30
Test example 1: Perming protocol used with keratin fraction of 5% SIFF (supplied as a
5% aqueous solution) i.e. 0.25% active. Instron tensile tester method as described
previously. Results are shown in Table 4 and Figure l.

Table 4. Instron test results for permed, and undamaged hair fibres treated with. 5%
SIFP. Results expressed, as average energy (millijoules) requited to extend hair fibres by
2 and 20% of the gauge length (15mm.).
10 This study indicates that hair fibres which have been weakened by a perming process
regain strength following treatment with a solution containing a keratin fraction in both
wash off and leave on protocols. The increase in energy needed to extend the
permed/keratin treated fibres relative to the permed fibres was measured statistically
using the student's t test and found to be significant in all cases.
15
Test example 2: Perming protocol used with keratin fraction of 2% SIFP (supplied as a
5% aqueous solution) i.e. 0.1% active. Instron tensile tester method as described
previously. Results are shown in Table 5 and Figure 2.

WO 2004/047774 PCT/NZ2003/000263
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Table 5. Instron test results for permed and undamaged hair fibres treated with 2%
SIFP. Results expressed as average energy (millijoules) required to extend hair fibres by
2 and 20% of the gauge length (15mm).
5 This study shows that permed hair fibres are strengthed after treatment with a 0.1%
active solution of keratin fraction when it is used as part of a leave on protocol. The
difference was analysed statistically using the Student's t test and found to be
statistically significant (p 10 Test example 3. Bleaching protocol used with keratin fraction of 5% SIFP (supplied as a
5% aqueous solution) i.e. 0.25% active. Instron tensile tester method as described
previously. Results are shown Table 6 and Figure 3.

15 Table 6. Instron test results for bleached and undamaged hair fibres treated with 5%
SIFP. Results expressed as average energy (millijoules) required to extend hair fibres by
20% of the gauge length (15mm).
This study indicates that hair fibres which have been subjected to bleaching have
20 increased strength following treatment with a solution containing 0.25% active keratin
protein fraction as part of a leave on protocol. The difference was analysed statistically
using the Student's t test and found to be statistically significant (p Test example 4. Relaxing protocol used with keratin fraction of 2% SIFP (supplied as a
25 5% aqueous solution) i.e. 0.1% active. Instron tensile tester method as described
previously. Results are shown in Table 7 and Figure 4.

WO 2004/047774 PCT/NZ2003/000263
32

Table 7. Instron test results for relaxed and undamaged hair fibres treated with 2%
SIFP. Results expressed as average energy (millijoules) required to extend hair fibres by
20% of the gauge length (15mm).
5
This study indicates that hair fibres Which have been subjected to a hair straighteneing
procedure have increased strength following treatment with a solution containing 0.1 %
active keratin protein fraction as part of a wash off protocol. The difference was
analysed statistically using the Student's t test and found to be statistically significant.
10 (p Test examples 1-4 demonstrate the keratin protein fractions impart a strengthening
effect (as measured by an increase in the energy required to extend individual hair
fibres) on hair which has been subjected to perming, bleaching and straightening which
15 are routinely used cosmetic treatments.
Example 2: Substantivity
20 Keratin Shampoo Fomulation
% by weight
Ammonium lauryl sulphate (28 %) 25.0
Disodium laureth sulfosuccinate 20.0
Cocamidopropyl betaine 8.0
25 Preservative 0.3
Keratin fraction 0.5

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Sodium chloride (20%) q.s
Water q.s to 100
Experimental procedure
5
Hair swatches 2-3g were used. Experiments were performed in duplicate.
Swatches were shampooed prior to use to remove residual conditioning agents.
Swatches were either left undamaged, or were subjected to multiple perming procedures
or bleaching procedures.
10 Swatches were equilibrated at 50% RH and weighed accurately.
Keratin fractions were applied to the swatches either from an aqueous solution or as part
of a shampoo formulation at a level of 3.0ml per swatch.
The treatment solution was spread onto the swatch with fingertips, allowed to absorb for
1 min and rinsed under a stream of RO water.
15 The swatch was air-dried and equilibrated at 50% RH for 24 in prior to weighing.
Results are summarized in Table 8 and Figure 5.

WO 2004/047774 PCT/NZ2003/000263
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Table 8: Percentage weight gain at 50% relative humidity for damaged and undamaged
hair with and without treatment with a solution or shampoo formulation containing
SIFP,SHSP and SPEP.
5 This study indicates that the SIFP keratin fraction is substantive to undamaged, permed
and bleached hair from both an aqueous solution and shampoo formulation. The SHSP
keratin fraction is also substantive from an aqueous solution and shampoo fomulation
and seems to adsorb to a greater extent to bleached and permed hair and when applied
as a solution rather than a shampoo. The keratin fraction which has molecular weight
10 less than 1kD, SPEP, is substantive to bleached and permed hair from an aqueous
solution and shampoo however it was not associated with a weight increase on
undamaged hair. A much greater weight increase was observed from an aqueous
solution indicating that the surfactants present in the shampoo may be removing the
keratin fraction.
15
These results indicate that the different keratin fractions have different surface activity
on the hair fibre. The larger fractions have a greater ability to form adsorbing layers and
convey a conditioning and smoothing (gloss) effect compared with the low molecular
weight SPEP.
20
Example 3: Moisturisation
Experimental procedure
Hair swatches 2-3 g were used Each treatment within the experiment was performed in
25 duplicate.
Swatches were shampooed with a high surfactant (non-conditioning) shampoo prior to
use to remove residual conditioning agents.
Swatches were either left undamaged, or were subjected to multiple perming or
bleaching procedures.
30 Swatches were equilibrated at 50% RH for 24 hrs and weighed accurately.
Swatches were equilibrated at 73% RH for 24 hrs and weighed accurately.

WO 2004/047774 PCT/NZ2003/000263
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The difference in weight as a result of increased humidity (in the absence of protein
treatment) was calculated.
Swatches were treated (in duplicate) with either an aqueous solution containing a
keratin fraction or a shampoo containing a keratin fraction (as described earlier).
5 Swatches were equilibrated for 24 hrs and weighed at 50% RH.
Swatches were equilibrated for 24 hr and weighed at 73% RH.
The difference in weight as a result of increased humidity following treatment with a
keratin solution or shampoo was calculated.
10 Results are summarised in Table 9 and Figure 6.

Table 9. Percentage weight increase with increasing relative humidity for damaged and
undamaged hair fibres treated with an aqueous solution or a shampoo containing SIFP,
15 SHSP or SPEP.
This study idicates moisturisation cculd be increased or decreased depending on the
keratin fraction apphlied. The SIFP keratin fraction decreased moisture uptake of

WO 2004/047774 PCT/NZ2003/000263
36
permed, bleached and undamaged hair at high humidity when applied as an aqueous
solution or in a shampoo.
The SHSP fraction had less of an effect on moisture uptake at high humidity and there
5 was some indication that moisturisation decreased when applied from a shampoo in
preference to an aqueous solution.
SPEP increased moisture uptake particularly when applied from a shampoo.
10 Example 4: Foaming of formulations
Experimental procedure
Waring Blender Test
Method:
15 1. Prepare 100 mL of a 5% solution of material to be tested.
2. Pour into blender.
3. Blend for 1 minute on high.
4. Pour all the liquid into 500 mL measuring cylinder,
5. Record the amount of foam (-100 ml,) immediately and record.
20 6. Record the amount of foam, in mLs after 5 minutes: (this will give "low foam"
measurement)
Test example 7. Comparison of foaming of keratin fraction with common surfactants
25 and effect of adding 0.5% metal ion sequesterant ethylenediammine tetracetic acid
(EDTA).
Waring bleeder test applied.
30 Results are summarized in Table 1.0 and Figure 7.

WO 2004/047774 PCT/NZ2003/000263
37

Table 10. Foam quantity and stability in a waring blender test. Results are expressed as.
foam volume immediately following blending and after 5 minutes.
5 This study indicates that the SIFP keratin fraction shows mild foaming and forms stable
foams. The SHSP fraction displayed intermediate foaming ability and formed very
stable foams. SPEP formed unstable foams. The addition of the ion sequestering agent
EDTA increased the foaming capacity of all fractions.
10 Test example 8, Foaming properties of keratin fraction mixtures.
Keratin fractions were combined and the waring blender test used to assess foaming.
Results are summarised in Table 11.

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Table 11: Foam quantity and stability of keratin fraction mixtures in a waring blender
test. Results are expressed as foam volume immediately following blending and after 5
minutes.
5 This study indicates that addition of the SHSP keratin fraction to the less foaming SIFP
fraction increases the foam capacity.
Test example 9. Foaming of shampoo formulations containing keratin fractions.
Shampoo formulation described earlier, containing 0.5% active keratin fraction.
10 Waring blender test results summarized in Table 12 and Figure 8.

Table 12. Foam quantity and stability of shampoo with and without SIFP, SHSP and
SPEP in a waring blender test Results are expressed as foam volume immediately
15 following blending and after 5 minutes.
It is known that proteins of ten have an adverse effect of foaming in formulations.
This study indicates that addition of the SIFP keratin fraction to a shampoo formulation
does not have a deleterious effect on foaming, moreover there is some evidence that
20 foam stability in increased. Furthermore addition of the SHSP fraction to a shampoo
formulation increases the foaming capacity and results in a greater foam after i minutes
compared to that in the absence of the keratin. The SPEP keratin fraction does suppress
foam formation.
25 Example 5: Subjective assessment of keratiu fractions in shampoo formulation

WO 2004/047774 PCT/NZ2003/000263
39
Method
Human volunteers were given two unlabelled shampoo formulations (described earlier),
one of which contained 0.5% active of the SIFP keratin fraction.
Volunteers were asked to wash their hair with one sample as many times as usual over
5 the period of one week and then repeat with the other sample.
Volunteers were then given a questionnaire to fill out ranking each sample in terms of
foaming ability, gloss impartment, hair feel, combablility, and appearance.
The lower number was associated with an undesirable effect eg in the case of
combability 1= extremely difficult to comb and 6 = excellent combability.
10
Test example 10
Questionnaires were collected and the scores recorded and averaged.
Results are summarized in Table 13 and Figure 9.

15
Table 13. Subjective assessment of a shampoo formulation with and without SIFP.
Results are an average of scores recorded by human volunteers.
This study indicates that volunteers did net observe a major change in foaming of the
20 shampoo formulation as a result of addition of the keratin fraction. Moreover the
presence of the keratin fraction was observed to impart superior gloss, feel, combability
and improved appearance to the formalation indicating that it was acting as a
conditioning agent.

WO 2004/047774 PCT/NZ2003/000263
40
Whilst the invention has been described with reference to the above Examples, it will be
appreciated that numerous improvements and modifacations may be made without
departing from the scope of the invention as set out in this specification.
5 Industrial Applicability
The compositions described in the application will be useful in a wide range of personal
care products such as shampoos, gels, conditioners, creams and detergents and
including cosmetics such as moisturiziers, lotions, creams and gels.

PCT/NZ20O3/000263
Received 13 October 2004
41
Claims
1. A personal care formulation containing an s -sulfonated keratin protein fraction.
5 2. A personal care formulation as claimed in claim 1 wherein the keratin protein
fraction is intact.
3. A personal care formulation as claimed in claim 1 wherein the keratin protein
fraction is hydrolysed.
10
4. A personal care formulation as claimed in any one of claims 1 to 3 wherein the
keratin protein fraction is from the intermediate filament protein family.
5. A personal care formulation as claimed in any one of claims 1 to 3 wherein the
15 keretin protein fraction is from the high sulfur protein family.
6. A personal care formulation according to claim 4 wherein the cysteine content of
the keratin protein is around 4%.
20 7. A personal care formulation according to claim 5 wherein the cysteine content of
the keratin protein is greater than 10%.
8. A personal care formulation as claimed in any one of claims 1 to 3 wherein the
keratin protein fraction is from the high glycine-tyrosine protein family.
25
9. A personal care formulation containing from about 0.001% to 50% of an s-
sulfonated keratin protein fraction.
10. A personal care formulation according to claim 9 containing from 0.001% to 10%
30 of an s-sulfonated keratin protein fraction.
AMENDED SHEET
IPEA/AU

PCT/NZ2O03/000263
Received 22 December 2004
42
11. A personal care formulation according to, claim 10 containing from 0.001 % to 1 %
of an s-sulfonated keratin protein fraction.
12. A personal care formulation, according to any one of claims 9-11 wherein the
5 keratin protein fraction is intact
13. A personal care formulation acconding to any one of claims 9-11 wherein the
karatein protein fraction is hydrolysed.
10 14. A personal care formulation according to any one of claims 12 to 13 wherein, the
keratin protein fraction is from-the intemediate filament protein family.
15. A personal care fonnulaticn according to any one of claims 12 to 13 wherein the
keratin protein fraotion is from the high sulfer protein family.
15
16. A personal care fomulation according to claim 14 wherein the cysteine content of
the keratin protein is around 4%.
17. A personal care formulation according to claim 15 wherein the cysteine content of
20 the keratin protein is greater than 10%.
18. A personal care formulation according to any one of claims 12 to 13 wherein the
keratin protein fraction is from the high glycine-tyrosine protein family.
25 19. An additive comprising an S-sulfonated keratin protein fraction, when used in a
personal care formulation.
20. An additive according to claim 19 wherin the protein fraction is intact.
30 21. An additive according to claim 19 wherein the protein fraction is hydrolysed.
Amended Sheet
IPEA/AU

PCT/NZ20O3/000263
Received 13 October 2004
43
22. An additive according to any one of claims 19 to 21 wherein the protein fraction is
from the intermediate filament protein family.
23. An additive according to any one of claims 19 to 21 wheretin the protein fraction is
5 from the high sulfur protein family.
24. An additive according to claim 22 wherein the cysteine content of the protein is
around 4%.
10 25. An additive according to claim 23 whererin the cysteine content of the protein is
greater than 10%.
26. An additive according to any one of claims 19 to 21 wherein the protein fraction is
from the high glycine-tyrosins protein family.
15
27. An additive for a personal care formulation that contains from 0.001% to 50% of
an s-sulfonated keratin of protein fraction.
28. An additive according to claim 27 containing from 0.001% to 10% of an s-
20 sulfonated keratin protein fraction.
29. An additive according to claim 29 containing from 0.001% to 1% of an s-
sulfonated keratin protein fraction.
25 30. An additive according to any one of claims 29-29 wherein the keratin protein
fraction is intact.
31. An additive according to any one of claims 27-29 wherein the keratin protein
fraction is hydrolysed.
30
AMENDED SHEET
IPEA/AIJ

PCT/NZ2O03/O00263
Received 13 October 2004
44
32. An additive according to any one of claims 30 to 31 wherein the keratin protein
fraction is from the intermediate filament protein family.
33. An additive according to any one of claims 30 to 31 wherein the keratin protein
5 fraction is from the high sulphur protein family.
34. An additive according to claim 32 wherein the cysteine content of the keratin
protein is around 4%.
10 35. An additive according to claim 33 wherein the cysteine content of the keratin
protein is greater than 10%.
36. An additive as claimed in any one of claims 27-31 wherein the keratin protein
fraction is from the high glycine-tyrosine protein family
15
37. A method of using a personal carr formulation as claimed in any one of claims 1-
18.
38. A method of treating hair comprising the use of a formulation or additive
20 according to any one of claims 1 -36.
AMENDED SHEET
IPEA/AU

The application describes a range of personal care products than include a keratin protein fraction. The fraction
may be intact or hydrolysed. It is preferably S-sulfonated. The content of the fraction may range from 0.001% to 50%. In most
formulations is content will be less than 1% although in a certain products such as nail care products the content will be higher. A
wide range of personal care products are described including shampoos body gels and lotions, conditioners, creams and cosmetics
generally.

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Patent Number

217413

Indian Patent Application Number

00964/KOLNP/2005

PG Journal Number

13/2008

Publication Date

28-Mar-2008

Grant Date

26-Mar-2008

Date of Filing

24-May-2005

Name of Patentee

KERATEC LIMITED

Applicant Address

CNR SPRINGS AND ELLESMERE JUNCTIONS ROADS, LINCOLN, LCANTERBURY, NEW ZEALAND.

Inventors:

#	Inventor's Name	Inventor's Address
1	KELLY ROBERT JAMES	61 ST MARTINS ROAD. CHRISTCHURCH. NEW ZEALAND.
2	RODDICK-LANZILOTTA ALISA DAWN	13 BRANDON STREET, HORNBY, CHRISTCHURCH, NEW ZEALAND.

PCT International Classification Number

A61K 7/00

PCT International Application Number

PCT/NA2003/000263

PCT International Filing date

2003-11-28

PCT Conventions:

#	PCT Application Number	Date of Convention	Priority Country
1	522836	2002-11-28	New Zealand
2	524706	2003-03-12	New Zealand