CN116917308A

CN116917308A - Compositions for hair straightening and styling and methods of use

Info

Publication number: CN116917308A
Application number: CN202180085591.5A
Authority: CN
Inventors: 贾斯汀·帕洛尼
Original assignee: Olaprax Co ltd
Current assignee: Olaprax Co ltd
Priority date: 2020-12-19
Filing date: 2021-12-18
Publication date: 2023-10-20
Also published as: WO2022133333A3; WO2022133333A2

Abstract

Provided herein are peptides, wherein the peptides bear one or more amino acid sequence differences relative to SEQ ID No. 1, and the amino acid sequence differences comprise at least one cysteine substitution.

Description

Compositions for hair straightening and styling and methods of use

The present application claims priority from co-pending provisional application serial No. 63/205,666, which is converted from non-provisional application 17/128,036 filed on 12/19/2020 to provisional application 8/4/2021, the entire disclosure of which is incorporated herein by reference.

Background

Keratin refers to a filiform protein exhibiting specific physicochemical properties, which can be extracted from the keratinized layer of the epidermis. Keratin is the major protein in the skin and constitutes the top layer of hair, nails, and skin. Harmful chemicals and environmental influences such as UV and thermal radiation lead to permanent damage to the skin, hair and nails.

Keratin is defined by a primary structure based on amino acid chains. These chains vary in the number and sequence of amino acids, polarity, charge and size. Minor modifications in the amino acid sequence of keratin lead to significant property changes, as these sequences determine the overall molecular structure and bond properties. The sulfur-containing amino acids, methionine and cysteine establish intramolecular disulfide bonds or intermolecular disulfide bonds. The role of disulfide bonds is important for the structural integrity of keratin. Disulfide bonds can be broken by chemical treatment of hair and cause serious long-term damage to keratin over time.

Disulfide bonds within keratin chains result in characteristic waves, curls, and the overall or appearance of individual hair. These characteristics of hair may be desirable or undesirable, resulting in individuals seeking to perform hair treatments to alter the natural entity or shape of their hair. In order to limit or minimize the application of irritating chemicals for straightening hair or styling hair to a desired configuration, there is a need to develop safer and more effective alternative biobased compositions.

It is an object of the present disclosure to provide peptides for use in consumer products, cosmetic compositions, hair treatments and/or hair colors.

SUMMARY

The present disclosure provides information about compounds that can be used to treat keratin fibers, such as to strengthen and/or reduce or prevent breakage. This object is achieved by providing cysteine-reactive peptides.

In a first aspect, the peptide has a substitution of at least one amino acid of SEQ ID NO. 1 with cysteine, wherein the peptide comprises at least 50% sequence homology with respect to SEQ ID NO. 1. The peptide has at least one cysteine substitution at any one or more of a glutamine amino acid position, a valine amino acid position, an alanine amino acid position, and a serine amino acid position. The peptide forms an alpha helix and at least one of the cysteine substitutions is located in an outer region of the alpha helix.

In one embodiment, the cysteine substitutions are located in a region of SEQ ID NO. 1 that is identical to SEQ ID NO. 2. The cysteine substitution within SEQ ID NO. 2 may be, for example, a V17C substitution relative to SEQ ID NO. 1.

In another embodiment, the peptide has a substitution of the amino acid of SEQ ID NO. 1 with cysteine at H6C or Q13C, and optionally, an additional cysteine substitution at least one additional amino acid at another position. The additional cysteine substitutions relative to SEQ ID NO. 1 may be from.gtoreq.1 to.ltoreq.11 amino acids.

In another aspect, the peptide has at least 3 amino acid substitutions of SEQ ID NO. 1, and optionally, these cysteine substitutions are at amino acids other than the Q13C or H6C positions. In this connection, the cysteine substitutions relative to SEQ ID NO. 1 are.gtoreq.3 and.ltoreq.11 amino acids.

In one embodiment, the cysteine is added at the C-terminus, N-terminus, or both the N-and C-termini of the peptide relative to SEQ ID NO. 1.

In a second aspect, the peptide is any one of SEQ ID NOS 3-109 or a variant having at least 70% sequence homology thereto.

In one embodiment, a composition comprising the same concentration of the plurality of peptides disclosed herein increases hair strength relative to a composition comprising a concentration of the plurality of peptides of SEQ ID NO. 1. This can be demonstrated by the following: the peptides disclosed herein have a greater retention in hair after repeated washes than the retention of the same peptide in one wash, relative to the same test under the same conditions for the retention of SEQ ID No. 1. Various peptides may be used in the liquid composition to improve one or more characteristics, such as the strength, visual properties, tactile properties, or a combination thereof, of hair. The keratin-binding peptide is more resistant to washing than the keratin-binding peptide consisting of SEQ ID NO. 1, especially after being damaged, for example after one or more hair bleaching. The liquid composition may be a shampoo, a conditioner, an oil or a mask. The concentration of the peptide may be found to be from about 0.01% to about 0.1% by weight of the liquid composition.

In one embodiment, the hair is treated by applying a liquid composition comprising the peptide after the hair curling, hair straightening, hair coloring or hair bleaching preparation is applied to the hair, resulting in at least about a 5%, 10%, 20%, 30%, 40% or 50% reduction in hair breakage compared to when the hair is not treated with the composition after the hair curling, hair straightening, hair coloring or hair bleaching preparation is applied to the hair. As noted, the composition may be part of a kit.

Definition of the definition

The terms used in the present specification generally have their ordinary meanings in the art in the context of the present invention and in the specific context where each term is used. Certain terms are discussed below or elsewhere in the specification to provide additional guidance to the practitioner in describing the compounds, compositions and methods and how to make and use them. Furthermore, it will be appreciated that the same thing may be expressed in more than one way. Thus, alternative languages and synonyms may be used for any one or more of the terms discussed herein, nor does it assign any special meaning to whether a term is elaborated or discussed herein. The use of examples anywhere in this specification (including examples of any terms discussed herein) is illustrative only, and in no way limits the scope and meaning of any example term. Also, the examples provided are considered non-limiting.

As used herein, "one embodiment," "an aspect" means that the particular feature, structure, or characteristic is included. Not all of the possible features, structures, or characteristics are included. Moreover, such phrases are not necessarily referring to the same aspect or embodiment. Furthermore, when a particular feature, structure, or characteristic is described in connection with an aspect or an embodiment, it is submitted that it is within the knowledge of one skilled in the art to effect such feature, structure, or characteristic in connection with other aspects or embodiments whether or not explicitly described. Furthermore, it should be understood that an item contained in the list in the form of "at least one of A, B and C" may represent (a); (B); (C); (A and B); (A and C); (B and C); or (A, B and C). Similarly, an item listed in the form of "at least one of A, B or C" can represent (a); (B); (C); (A and B); (A and C); (B and C); or (A, B and C).

As used herein, "about" or "approximately" shall generally mean within 20%, preferably within 10%, more preferably within 5% of a given value or range. Except in the operating examples, or where otherwise indicated, all numbers expressing quantities of ingredients and/or reaction conditions are to be understood as being modified in all instances by the term "about".

Recitation of numerical ranges of endpoints includes all numbers subsumed within that range. By way of non-limiting example, the range "1 to 5" also includes the values 1, 1.5, 2, 2.75, 3, 3.8, 4, 5.

As used in this specification and the appended claims, the singular forms "a," "an," and "the" include plural referents unless the context clearly dictates otherwise.

As used in this specification and the appended claims, the term "or" is generally employed in its sense including "and/or" unless the context clearly dictates otherwise.

As used herein, "hair keratin disulfide" refers to thiol residues naturally occurring in hair keratin that form disulfide bonds. The formation of new disulfide bonds between thiol residues and peptides can result in straightened hair, styling hair, or hair with desirable flow and entity.

As used herein, "binding efficiency" refers to the ability to form chemical bonds, for example, between sulfur atoms in two cysteine residues.

As used herein, "substitution" refers to the replacement of one amino acid in a protein sequence with another amino acid.

As used herein, "adding" refers to inserting an amino acid between two other amino acids in a protein sequence.

As used herein, "residue" refers to an amino acid.

As used herein, a "biological binding site" refers to a chemically reactive moiety that allows for attachment to another molecule.

As used herein, "vector" refers to a DNA molecule that allows transcription of encoded genetic information.

Drawings

Fig. 1: the results of example 1, left to right hair was treated with: (1) untreated, (2) SEQ ID NO.3, (3) SEQ ID NO.4, (4) SEQ ID NO.5, (5) SEQ ID NO.6, (6) SEQ ID NO.7, (7) SEQ ID NO. 8.

Fig. 2: example 2 as a result, left to right hair was treated with: (1) untreated, (2) SEQ ID NO.3, (3) SEQ ID NO.4, (4) SEQ ID NO.5, (5) SEQ ID NO.6, (6) SEQ ID NO.7, (7) SEQ ID NO. 8.

Fig. 3: the results of example 3 were either untreated on the hair (left) or treated using the complete procedure described in example 3 (right).

Fig. 4: the results of example 4 were either untreated on the hair (left) or treated using the complete procedure described in example 4 (right).

Fig. 5: the results of example 5 were either untreated on the hair (left) or treated using the complete procedure described in example 5 (right).

Fig. 6 (a): the results of example 6, left to right hair was treated with: (1) untreated, (2) not fully treated with SEQ ID NO:8, (3) fully treated with SEQ ID NO:8.

Fig. 6 (b): the results of example 6, hair samples (2) and (3) from fig. 6a were compared for breaking force.

Fig. 7 (a): the results of example 7, which demonstrate the effect of varying peptide concentration.

Fig. 7 (b): the results of example 7, which demonstrate the effect of altering peptide binding time.

Fig. 7 (c): the results of example 7, which demonstrate the effect of varying the number of peptide applications.

Fig. 7 (d): the results of example 7, which demonstrate the effect of varying the amount of shampoo at the end of the treatment.

Fig. 8 (a): the results of example 8, which demonstrate a comparison of the breaking force of raw hair treated with different peptides and untreated hair. The dashed bars represent the results after 1 shampoo was applied, and the bar graph with diagonal lines represents the results after 10 shampoos were applied.

Fig. 8 (b): the results of example 8, which demonstrate the comparison of the breaking force of raw hair bleached with different peptides and untreated hair. The dashed bars represent the results after 1 shampoo was applied, and the bar graph with diagonal lines represents the results after 10 shampoos were applied.

Fig. 9 (a): results of applying the fluorescent peptide and shampooing the original hair 1 to 10 times as described in example 9. The dashed bars represent the results after 1 shampoo and the bar graph with horizontal lines represents the results after 10 shampoos.

Fig. 9 (b): results of hair bleaching after application of the fluorescent peptide and shampooing 1 to 10 times as described in example 9. The dashed bars represent the results after 1 shampoo and the bar graph with horizontal lines represents the results after 10 shampoos.

Fig. 9 (c): comparison of percent decrease in fluorescence intensity between 1 and 10 shampoos for peptides with and without Q13C substitution, as described in example 9. The dashed bars represent results with Q13C substitution and the diagonal bars represent results without Q13C substitution.

Fig. 10 (a): the results of example 10, which show that for peptides containing cysteine substitutions at specific amino acid positions (bars with horizontal lines) and peptides without cysteine substitutions at that position (bars with diagonal lines), the percentage of fluorescence intensity decreases between 1 and 10 shampoos. Error bars represent 95% confidence intervals.

Fig. 10 (b): the results of example 10, which show a decrease in the percentage of fluorescence intensity between 1 and 10 shampoo shampoos for peptides containing Q13C substitutions and having a total number of cysteine substitutions greater than 1 (horizontal line) and peptides containing no Q13C substitutions or having 1 substitution (diagonal bar). Error bars represent 95% confidence intervals.

Fig. 10 (c): the results of example 10, which show a decrease in the percentage of fluorescence intensity between 1 and 10 shampoo shampoos for peptides containing H6C substitutions and having a total number of cysteine substitutions greater than 1 (horizontal line) and peptides containing no H6C substitutions or having 1 substitution (diagonal bar). Error bars represent 95% confidence intervals.

Fig. 10 (d): the results of example 10, which show a decrease in the percentage of fluorescence intensity between 1 and 10 shampoos for peptides without Q13C or H6C substitution and with a total number of cysteine substitutions greater than the indicated number of substitutions (bars with horizontal lines) and all other peptides from example 10 (bars with diagonal lines). Error bars represent 95% confidence intervals.

Fig. 11 (a) - (d): the sequences tested and described in figures 1-10.

Detailed Description

While the concepts of the present disclosure are susceptible to various modifications and alternative forms, specific aspects and embodiments thereof have been shown by way of example in the drawings and will herein be described in detail. It should be understood, however, that there is no intention to limit the concepts of the present disclosure to the specific forms disclosed, but on the contrary, the intention is to cover all modifications, equivalents, and alternatives falling within the spirit and scope of the disclosure and the appended claims. It will be apparent to those skilled in the art that various changes or equivalents may be employed without departing from the scope herein.

Provided herein are peptides and combinations of such peptides. Such peptides and compositions containing peptides can typically bind to one or more thiol residues naturally occurring in hair keratin, allowing the formation of new disulfide bonds between hair keratin and the designed keratin-binding peptide. For example, provided herein is a method of providing durable styling, flow and body to hair by: 1. mechanically structuring hair keratin into a desired shape (i.e., permanent waves) or straightened configuration; 2. breaking natural disulfide bonds of hair keratin; and 3. Applying the peptide to the hair keratin, thereby forming a new disulfide bond between the hair keratin and the peptide. In some other cases, the method of treating hair comprises applying a peptide to the hair before and/or after the hair coloring or hair bleaching treatment, wherein keratin in the treated hair forms new disulfide bonds between the keratin of the hair and the applied peptide. In some cases, the method of treating hair may include applying a peptide to the hair, e.g., for strengthening and/or repairing the hair, wherein the peptide may form part of a cosmetic composition, e.g., in the form of a shampoo, conditioner, oil, or mask, etc. Application of a peptide to hair, which may be part of a cosmetic composition and is believed to repair and/or improve one or more properties of the hair, such as, but not limited to, increased hair strength, breakage resistance, feel (i.e., softness), visual properties (i.e., shine) as compared to hair prior to treatment with the peptide, may create new disulfide bonds between the hair keratin and the peptide.

Hair can be damaged by environmental factors such as aging, washing, dyeing and styling. Repeated washing results in swelling of the stratum corneum, while thermal damage from drying and chemical damage from hair coloring, hair bleaching, straightening or curling typically results in dehydration, breakage, damage and curling of the hair. Hair curls, whether naturally occurring in the hair of a subject or as a result of environmental damage, generally refer to hair in which all strands of hair are not uniformly aligned. The degree of hair curl (or curl) is defined by the arrangement of each hair strand relative to the surrounding hair strands. The present disclosure is also useful for styling and straightening curly hair strands to a desired absolute directionality, defined as the straightness or waviness of a population of individual (or large) hair strands. The present disclosure is also useful for styling and straightening curly hair strands to a desired absolute directionality, defined as the straightness or waviness of a population of individual (or large) hair strands.

The peptide sequence differs from SEQ ID NO. 1 by at least one amino acid and is generally capable of binding keratin. Amino acid sequence KKVELFPK (SEQ ID NO: 2.) is believed to be responsible for the binding of SEQ ID NO:1 to hair keratin. In the disclosed peptides, SEQ ID NO 1 and SEQ ID NO:2 may be substituted or substituted with cysteine.

In some embodiments, the total cysteine content of the disclosed peptides is less than 50% of SEQ ID NO. 1, less than 45% of SEQ ID NO. 1, less than 40% of SEQ ID NO. 1, less than 35% of SEQ ID NO. 1, less than 30% of SEQ ID NO. 1, less than 25% of SEQ ID NO. 1, less than 20% of SEQ ID NO. 1, less than 15% of SEQ ID NO. 1, less than 10% of SEQ ID NO. 1, less than 9% of SEQ ID NO. 1, less than 8% of SEQ ID NO. 1, less than 7% of SEQ ID NO. 1, less than 6% of SEQ ID NO. 1, or less than 5% of SEQ ID NO. 1.

Peptides are provided which may be used alone or in combination in hair compositions, such as those disclosed herein, those known in the art, or those designed by one of skill in the art, having the amino acid sequence of any one of the following: SEQ ID NOS:3-SEQ ID NOS:17, SEQ ID NOS:18-SEQ ID NOS:109, and fragments and variants of any one of SEQ ID NOS:1 and 3-SEQ ID NOS:17, SEQ ID NOS:18-SEQ ID NOS: 109. The fragments and variants may, for example, have at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90% or 95% sequence homology to any one or more of SEQ ID NO:1 and SEQ ID NOS:3-SEQ ID NOS:17, SEQ ID NOS:18-SEQ ID NOS: 109. The variant may include one or more amino acid substitutions, additions, deletions, or combinations thereof relative to a control peptide. The peptide typically comprises at least 1, preferably 2, 3 or more cysteines.

In some embodiments, the peptide has a length of 10-50 amino acids, or any subrange therebetween, or any specific integer therebetween, including but not limited to 10-45, 10-40, 10-35, 10-30, 10-29, 10-28, 10-27, 10-26, 10-25, 10-24, 10-23, 10-22, 10-21, 10-20, 10-19, 10-18, 10-17, 10-16, 10-15, 15-20, 15-21, 15-22, 15-23, 15-24, 15-25, 15-26, 15-27, 15-28, 15-29, 15-30, 18-27, 19-26, 20-25 or 21-24 amino acids, or 10, 11, 12, 13, 14, 16, 17, 21, 22, 24, 25, 29, 25, 28, or 28.

Typically, the peptide may bind to hair and/or keratin thereof. Preferably, the peptide exhibits improved binding and/or retention to hair relative to a control peptide, e.g., SEQ ID NO: 1. The binding and/or retention of hair can be expressed by measuring the resistance to water. The retention of the one or more peptides may be measured, for example, by: fluorescent labelling of the one or more peptides and their application to hair or keratin thereof and allowing them to bind to hair and/or keratin thereof, followed by subjecting the hair to repeated washing (i.e. shampoo). Comparison and statistical analysis of fluorescence imaging of the labeled peptides on the hair before and after at least 1, 5, 10, 15, 20, 25 or 30 washes allows determining the extent of retention of the one or more peptides to the hair. In some embodiments, the hair is damaged hair. For example, in some embodiments, hair is damaged prior to testing for binding and/or retention of hair, e.g., hair is subjected to repeated hair bleaching treatments, as described in examples 8 and 9.

In some cases, binding and/or retention to hair is demonstrated by fluorescent labeling of the peptide and application of the labeled peptide to the hair. Next, hair is washed one or more times and the retention of the wash by the labeled peptide is measured, for example by fluorescence imaging, and compared at one wash and ten washes, optionally 15 washes, 20 washes or more. In some cases, there was no significant difference in retention after 1 wash (less than 5% decrease in fluorescence) compared to retention after 10 washes (amount of peptide retained in hair). In other cases, the percent retention drop is less than about 10%; less than about 20%; less than about 30%; less than about 40%; or less than about 50%; when the fluorescence detected after one wash is compared with the fluorescence detected after ten washes. The same wash test can be performed on any of the peptides described herein to determine the extent of retention of the peptides in the hair and their retention capacity. In some embodiments, the hair is damaged prior to testing for binding and/or retention of hair, e.g., the hair is subjected to repeated hair bleaching treatments, as described in examples 8 and 9.

In some embodiments, the peptide may be used at a reduced concentration compared to a control such as SEQ ID NO. 1 to achieve the same or improved results. For example, in some embodiments, the concentration of one or more peptides is about less than 95 wt%, about less than 90 wt%, about less than 85 wt%, about less than 80 wt%, about less than 75 wt%, about less than 70 wt%, about less than 65 wt%, about less than 60 wt%, about less than 55 wt%, about less than 50 wt%, about less than 45 wt%, about less than 40 wt%, about less than 35 wt%, about less than 30 wt%, about less than 25 wt%, about less than 20 wt%, about less than 15 wt%, about less than 10 wt%, about less than 5 wt%, about 0.01 to about 0.1 wt%, of the effective concentration of the peptide corresponding to SEQ ID NO 1 for hair straightening or styling, or for other common hair care, and/or in combination with keratin or hair, and/or improving the strength, appearance or feel of hair.

In some embodiments, in the peptide, it corresponds to SSEQ ID NO:2 or SEQ ID NO:1 by cysteine amino acid residues. To derive the peptide, one or more glutamine (Q) amino acid residues of SEQ ID No. 1 are replaced or substituted with cysteine in any combination, one or more valine (V) amino acid residues of SEQ ID No. 1 are replaced or substituted with cysteine in any combination, one or more alanine (a) amino acid residues of SEQ ID No. 1 are replaced or substituted with cysteine in any combination; and/or one or more serine (S) amino acid residues of SEQ ID No. 1 are substituted or substituted with cysteine in any combination. In some embodiments, one or more of the glutamine, valine, alanine, and serine amino acid residues of SEQ ID NO. 1 are each replaced or substituted with cysteine in any combination.

In some embodiments, the peptide comprises adding a cysteine residue to one or both of the N-terminus or C-terminus of any one of SEQ ID NOS:1 or 3-109. In some embodiments, ten cysteine amino acid residues are added to the N-terminus of any of SEQ ID NOS 1 or 3-17 and 18-109 or variants thereof; nine cysteine amino acid residues are added to the N-terminus of any of SEQ ID NOS:1 or 3-17 and 18-109 or variants thereof; eight cysteine amino acid residues are added to the N-terminus of any of SEQ ID NOS:1 or 3-17 and 18-109 or variants thereof; seven cysteine amino acid residues are added to the N-terminus of any of SEQ ID NOS:1 or 3-17 and 18-109 or variants thereof; six cysteine amino acid residues are added to the N-terminus of any of SEQ ID NOS:1 or 3-17 and 18-109 or variants thereof; five cysteine amino acid residues are added to the N-terminus of any of SEQ ID NOS:1 or 3-17 and 18-109 or variants thereof; four cysteine amino acid residues are added to the N-terminus of any of SEQ ID NOS 1 or 3-17 and 18-109 or variants thereof; three cysteine amino acid residues are added to the N-terminus of any of SEQ ID NOS 1 or 3-17 or variants thereof; two cysteine amino acid residues are added to the N-terminus of any of SEQ ID NOS 1 or 3-17 and 18-109 or variants thereof; alternatively, one cysteine amino acid residue is added to the N-terminus of any of SEQ ID NOS:1 or 3-17 and 18-109 or variants thereof. In some embodiments, ten cysteine amino acid residues are added to the C-terminus of any of SEQ ID NOS 1 or 3-17 and 18-109 or variants thereof; nine cysteine amino acid residues are added to the C-terminus of any of SEQ ID NOS:1 or 3-17 and 18-109 or variants thereof; eight cysteine amino acid residues are added to the C-terminus of any of SEQ ID NOS:1 or 3-17 and 18-109 or variants thereof; seven cysteine amino acid residues are added to the C-terminus of any of SEQ ID NOS:1 or 3-17 and 18-109 or variants thereof; six cysteine amino acid residues are added to the C-terminus of any of SEQ ID NOS 1 or 3-17 and 18-109 or variants thereof; five cysteine amino acid residues are added to the C-terminus of any of SEQ ID NOS 1 or 3-17 and 18-109 or variants thereof; four cysteine amino acid residues are added to the C-terminus of any of SEQ ID NOS 1 or 3-17 and 18-109 or variants thereof; three cysteine amino acid residues are added to the C-terminus of any of SEQ ID NOS 1 or 3-17 and 18-109 or variants thereof; two cysteine amino acid residues are added to the C-terminus of any of SEQ ID NOS 1 or 3-17 and 18-109 or variants thereof; alternatively, one cysteine amino acid residue is added to the C-terminus of any of SEQ ID NOS:1 or 3-17 and 18-109 or variants thereof. Any ten or less cysteine amino acid residues added to the C-terminus of SEQ ID NOS 1 may be combined with any ten or less cysteine amino acid residues added to the N-terminus of SEQ ID NOS 1.

The peptides of SEQ ID NO. 3 to SEQ ID NO. 17 and 18-109 or variants thereof are modified by substitution with a cysteine at different positions relative to SEQ ID NO. 1. Peptides with Q13C or H6C and at least one additional cysteine substitution exhibited increased retention after 10 shampoos compared to peptides without at least one Q13C or H6C substitution. The positions of amino acid cysteine substitutions on the outer regions of the peptide alpha helices in positions similar to the Q13C and H6C positions may play a role in increasing retention of hair after multiple shampoos.

The disclosed peptides may be combined with one or more cosmetically acceptable carriers (i.e., water or aqueous solutions) and/or cosmetically acceptable excipients that are considered safe and effective with respect to human hair and/or human scalp and that may be applied to the hair of an individual without causing adverse biological side effects such as burning, itching and/or redness, or similar adverse reactions. The composition may further comprise excipients that impart a neutral pH or a pH of about 5 to about 8 to the formulation. The composition may be any suitable form of hair composition. Non-limiting examples may be in the form of low to medium viscosity liquids, lotions, emulsions, oils, masks, mousses, sprays, gels, creams, shampoos, conditioners, and the like. Suitable excipients, such as those listed below, may be included in the hair care composition or not, depending on the form of use of the composition (e.g., hair gel, cream, conditioner or shampoo).

The disclosed peptides may be combined with one or more cosmetically acceptable ingredients. Suitable proportions and combinations of ingredients will be determined by those skilled in the art, including, but not limited to, surfactants, preservatives, chelating agents (e.g., ethylenediamine tetraacetic acid; trisodium ethylenediamine disuccinate), vitamins (e.g., vitamin E or C), proteins, film formers, detergents, resins, hair styling agents, opacifiers, volatile agents, propellants, acidulants (e.g., ascorbic acid, citric acid), alkalizing agents (e.g., sodium hydroxide, sodium carbonate), pH adjusting agents (e.g., citric acid, sodium hydroxide, phosphoric acid, etc.), neutralizing agents, hydrolyzing agents, liquid vehicles, carriers, anti-frizziness agents, absorbents, emulsifiers, softeners, solubilizing agents, humectants, wetting agents, hydrolyzed proteins, reconstituting agents, acidulants, acidity regulators, detangling agents, polymers, polishing agents, lubricants, sequestering agents, sunscreens, thermal protectants, conditioning agents, buffers, stabilizers, thickening agents, salts, antioxidants, alcohols, polysorbates, PEG, polyquaternary polymers such as, polyammonium salt-7, polyammonium salt-11, quaternary dye-113, quaternary ammonium salt-113, quaternary active oils, quaternary silicone additives, quaternary fatty acids, quaternary active oils, and biological carriers. In some cases, the peptides are present in a composition comprising water, one or more hair conditioning agents, one or more pH adjusting agents and/or buffers, one or more chelating agents, one or more preservatives, one or more surfactants, one or more moisturizers or lubricants, and an emollient. The cosmetically acceptable excipients that may be present may generally be present in an amount of from about 10% to about 99.99%, from about 40% to about 99%, or from about 80% to about 99% by weight of the composition.

In some embodiments, the composition comprises an effective amount of one or more peptides to improve one or more aspects of hair strength, visual appearance (i.e., gloss), or tactile properties (i.e., feel), or to alter the shape or entity thereof, as compared to, for example, untreated hair or hair treated with an equivalent amount of a control peptide as set forth in SEQ ID NO. 1.

Hair breakage is a significant problem encountered during hair coloring, hair bleaching and other hair treatments. In some cases, the compositions described herein can improve hair quality by reducing hair breakage when the hair is subjected to treatments such as dyeing, hair bleaching, straightening, or permanent waving. In some cases, hair breakage can be reduced by at least about 5, 10, 15, 20, 25, 30, 35, 40, 45, or 50% or more using one or more of the disclosed peptides and compositions thereof after treatment with the peptides as compared to untreated hair from the same individual. Standard methods of measuring hair breakage are known, including recording the number of broken hair fibers using repeated hair combing experiments-as a function of repeated combing/brushing. See, for example, t.a. evans & k.park, A statistical analysis of hair breakage (statistical analysis of hair breakage), ii.repeated grooming experiments (repeated combing experiments), j.cosnet.sci., 61,439-455,2010.

One or more peptides disclosed herein can comprise a lipid conjugated to a site for biological conjugation. For example, the site for biological conjugation may be the amino acid sequence AKT, wherein the lipid is conjugated to a lysine of the amino acid sequence AKT. Any suitable lipid may be conjugated to the peptides disclosed herein. Examples include, but are not limited to, myristoleic acid/alcohol/amine, palmitoleic acid/alcohol/amine, oleic acid/alcohol/amine, elaidic acid/alcohol/amine, octadecenoic acid/alcohol/amine, linoleic acid/alcohol/amine, elaidic acid/alcohol/amine, alpha linolenic acid/alcohol/amine, arachidonic acid/alcohol/amine, eicosapentaenoic acid/alcohol/amine, erucic acid/alcohol/amine, caprylic acid (capric acid)/alcohol/amine), lauric acid/alcohol/amine, myristic acid/alcohol/amine, palmitic acid/alcohol/amine, lignoceric acid/alcohol/amine, arachidic acid/alcohol/amine, stearic acid/alcohol/amine, sphingolipids including ceramides, sphingomyelins, alpha cerebrosides, gangliosides, sulfatides, and phytosphingosines. The peptide compositions disclosed herein are useful as a daily or frequent use product, including but not limited to shampoos, conditioners, gels, mousses, pomades, anti-frizziness agents, sprays or hair coloring products, which can be applied to the hair as part of a conventional hair care program including washing, conditioning, coloring, drying and styling. These compositions are useful in salons. In some embodiments, the peptide composition may be suitable for home use.

The peptide composition may be a liquid, solid or gel, and may be filled and stored in any suitable container, including bottles, cartons, tubes and cans. The peptide composition may also be provided or used as part of a kit. In some embodiments, the kit is a hair straightening kit, a hair dyeing kit, a hair bleaching kit, or a hair styling kit. The kit may also include a developer (aqueous hydrogen peroxide), bottle, glove, shampoo, conditioner, and/or deodorant. Instructions for use of the kit are also generally provided. Instructions for use of the kit are also generally provided. In the case of coloring or hair bleaching kits, the kit typically includes more than one container (or more than one compartment in a given container) to ensure that the whitening agent (e.g., peroxide, bleach) or coloring agent is stored separately from the peptide-containing composition. The kit may optionally contain a shampoo and a conditioner.

The peptides disclosed herein can be prepared by expression in a cell. The peptide may be produced in a cell such as a bacterial or yeast cell. Examples include, but are not limited to, E.coli and Saccharomyces cerevisiae. Standard methods of cell production are well known to those skilled in the art. The method comprises the following steps:

1. Cloning the coding sequence of the peptide into an expression plasmid;

2. introducing a recombinant expression plasmid into a cell;

3. expressing the peptide in the cell; and

4. isolating the peptide from the cell.

Alternatively, peptides may be synthesized using chemical synthesis according to standard synthetic protocols.

The peptides disclosed herein can be used as part of a hair composition for straightening or shaping hair of a subject. The peptides disclosed herein can be applied by hand, in a drug vial, in a brush, in a dropper, in a spray bottle, or in any other suitable method and/or applicator.

The subject may be any mammal, preferably a human.

Typical hair straightening or styling treatments generally include two or three main steps, in combination with manually securing the hair to a desired final shape (e.g., using "curlers" or the like, as well as other shape forming tools known in the art):

1. hair keratin relaxes, in which disulfide bonds present in the hair are broken;

2. application, wherein the peptide of the invention or a hair composition thereof is applied to the hair; and

3. immobilization, in which new disulfide bonds are reformed.

In some cases, step 2 and step 3 may be combined into one step, or step 2 and step 3 may be performed simultaneously. In some other cases, the immobilization may be performed after the relaxation (step 1) (step 3), followed by administration of the peptide (step 2). Each step may involve applying the solution to the hair for about 5, 10, 15, 20, 25 or 30 minutes, although this time may range from about 5 minutes to 1 hour. In some cases, the hair relaxer composition is applied to the hair for a treatment time ranging from about 10 to 15 minutes, 35 to 45 minutes, 45 to 60 minutes, or 25 to 35 minutes. In some cases, shorter treatment times, such as about 10 to 15 minutes, may be used, depending on the existing damage to the hair, for example if it was previously bleached by the hair. In some cases, the peptide or hair composition thereof (step 2) is applied to the hair for a treatment time of about 5 minutes. Any of the steps may also optionally be repeated a number of times. The hair may optionally be washed and dried before or after any step.

The hair keratin relaxing composition (of step 1) or the peptide (of step 2) or the hair composition thereof may be applied using a brush and/or comb. Optionally, all hair fibers that are straightened or shaped are wetted with the composition used to ensure that the hair fibers are saturated. Optionally, after steps 1, 2 and 3, a leave-on treatment, such as a leave-on conditioner, may be applied to the hair for a treatment time of at least about 5 minutes, followed by optional drying of the hair.

The relaxation (step 1) and the fixation (step 3) may be performed using a number of different methods. In step 1, any of the following may be used to break the disulfide bond: (1) heating; (2) Applying an alkaline relaxer (e.g., sodium hydroxide solution at pH 12-14); (3) Applying an alkali-free relaxant (e.g., calcium hydroxide or guanidine carbonate at pH 9-11); (4) Application of a "thio" relaxant (e.g., sodium thioglycolate, ammonium thioglycolate, dithiothreitol, thioglycolate, thiolactic acid, dihydrolipoic acid esters, thioglycerol, mercaptopropionic acid, polyethylene glycol thiols); (5) Applying a natural, thiol-containing compound (e.g., glutathione, cysteine, cysteinyl-glycine), optionally together with ascorbic acid or a derivative thereof, preferably in a weakly alkaline solution (e.g., pH 9-10); or (6) administering an enzyme known to play a role in reducing disulfide bonds of keratin and its requisite substrate (e.g., glutathione reductase, cysteine dioxygenase, alkyl hydroperoxide reductase, thioredoxin reductase, dihydrolipoyl dehydrogenase, peptide methionine sulfoxide reductase, adenosine phosphate reductase, ribonucleoside diphosphate reductase). Non-thio relaxants are also known and may be used in place of "thio" relaxants, including but not limited to alkaline hydroxides (i.e., sodium hydroxide, potassium hydroxide), sodium bisulphite, ammonium bisulfide, zinc formaldehyde sulfoxylate, sodium metabisulfite, potassium borohydride, and hydroquinone.

For the immobilization performed in step 3, any of the following methods may be used to form or reform disulfide bonds: (1) applying sufficient heat; (2) applying an acid or an acidic solution; (3) applying hydrogen peroxide; (4) Applying any oxidase (e.g., glucose oxidase, etc.) that generates hydrogen peroxide with its requisite substrate(s); and/or (5) not washing hair at least 24 hours after step 2, optionally also adding conditioning agents to the hair. In some cases, applying sufficient heat to the hair during the fixing process may include drying and/or ironing the hair using a suitable number of passes, such as about 5 to 8 passes, over a temperature range of about 375°f to about 410°f or about 350°f to about 375°f. In some cases, lower heating temperatures may be used, depending on the existing damage to the hair, for example, if it was previously bleached by the hair.

Personal care and hair compositions typically contain conventional cosmetically acceptable excipients that can be used, for example, to alter various properties of the composition and improve aesthetics. Such cosmetically acceptable excipients are as described above. Common natural and synthetic excipients are described in, for example, international Cosmetic Ingredient Dictionary and Handbook (International cosmetic composition dictionary and handbook), twelfth edition 2008, ISBN-10:1882621433 (hereinafter referred to as "cosmetic handbook") and CTFA component information (http:// www.ctfa-online.org/pls/CTFA online.home), the contents of which are hereby incorporated by reference in their entirety.

Emulsifiers are typically used to aid in mixing ingredients that would otherwise be immiscible. The emulsifier may be synthetic or natural. Natural emulsifiers may include, but are not limited to, olive oil/wheat protein, olive oil/oat protein, sucrose esters, rice bran emulsifiers, and/or various other food and pharmaceutical grade emulsifiers, which may be used alone or in combination.

Synthetic emulsifiers may include, but are not limited to: silicone emulsifiers, such as dimethicone copolyols; sulfonates and sulfonic acid derivatives; a phosphorus organic derivative; a sugar ester; fatty esters, such as sorbitan monolaurate, sorbitan stearate, sorbitan laurate, sorbitan palmitate, sorbitan oleate; polyester/PEG (polyethylene glycol) derivatives such as polysorbate 20 (polysorbate-20) (polyethylene glycol 20 sorbitan monolaurate); fatty acid esters of fatty alcohols, such as glyceryl stearate, isopropyl stearate, hexyl laurate; fatty acid amides; acyl lactylates; alkoxylated compounds, such as alkoxylated block polymers, alcohols, alkylphenols, amines, amides, fatty esters, fatty acids, oils, sugar esters and polyesters, fatty acid esters of fatty alcohols and ethers of fatty alcohols; carboxylated alcohol ethoxylates and alkylphenol ethoxylates; carboxylic acid/fatty acid and mixtures thereof. Other suitable emulsifiers may include, but are not limited to, copolymers of unsaturated esters with styrene sulfonate monomers, dicetyl phosphate, stearyl alcohol, glycerol esters, polyoxyethylene glycol ethers of cetostearyl alcohol, stearic acid, polysorbate-20, cetostearyl alcohol-20 (ceteareth-20), lecithin, ethylene glycol stearate, polysorbate-60 (polysorbate-60), polysorbate-80 (polysorbate-80), or combinations thereof. More than one emulsifier may be included in the formulation. Other natural and synthetic emulsifiers can also be found in the cosmetic handbook.

Colorants are commonly used to provide a relatively uniform color to the final cosmetic composition. The colorant may be synthetic or natural. Natural colorants may include pigments or colors of vegetable origin. Natural pigments may be inorganic (mineral) or organic, white or non-white and coated or uncoated particles. Natural colorants can include, for example, cerium oxide, chromium oxide, iron oxide, titanium dioxide, zinc oxide, zirconium oxide, carbon black, chromium hydroxide green, iron blue, manganese violet, ultramarine, D & C and FD & C colorants, azo-based colorants, indigo-based colorants, insoluble metal salts of certified color additives, known as lakes, and the like, and mixtures thereof.

Synthetic colorants may include, for example, triphenylmethane, anthraquinone, and xanthine dyes, and mixtures thereof. Other natural and synthetic colorants can be found in cosmetic handbooks and CTFA ingredient information.

The composition may comprise a wax. Waxes may be synthetic or natural. Natural waxes may include, for example, beeswax, carnauba and/or candelilla wax, hydrogenated jojoba oil, hydrogenated jojoba wax, hydrogenated microcrystalline wax, hydrogenated rice bran wax. Synthetic waxes may include, for example, cetyl esters, montan acid wax, paraffin wax, PEG-6 beeswax, PEG-8 beeswax, sulfurized jojoba oil, synthetic beeswax, synthetic candelilla wax, synthetic carnauba wax, synthetic japan wax, synthetic jojoba oil, synthetic waxes, stearoxy dimethicone, dimethicone behenate, stearyl dimethicone, and synthetic homo and copolymer waxes from the ethylene series, or mixtures thereof. Other natural and synthetic waxes and oils can be found in cosmetic handbooks and CTFA ingredient information.

The composition may also include a preservative. Preservatives may be synthetic or natural and may be used to inhibit the growth of undesirable microorganisms. Natural preservatives may include blackcurrant fruit extract, aspen bark, radish root and sorbic acid, alone or in combination.

Synthetic preservatives may include, for example, methylparaben, ethylparaben, propylparaben, imidazolidinyl urea, diazolidinyl urea, DMDM hydantoin, isothiazolinones, chlorinated aromatic compounds, parahydroxybenzoic acid/parahydroxybenzoate, alone or in combination. Other suitable preservatives include, but are not limited to, glycerin-containing compounds (e.g., glycerin or ethylhexyl glycerin or phenoxyethanol), benzyl alcohol, parabens (methyl parahydroxybenzoate, ethyl parahydroxybenzoate, propyl parahydroxybenzoate, butyl parahydroxybenzoate, isobutyl parahydroxybenzoate, etc.), propylene glycol, sodium benzoate, ethylenediamine-tetraacetic acid (EDTA), behenium trimethylammonium chloride (behenrimonia chloride), potassium sorbate, and/or grapefruit seed extract, or combinations thereof. More than one preservative may be included in the composition. Other preservatives known in the cosmetic industry include salicylic acid, DMDM hydantoin, formaldehyde, chlorophenol, triclosan, imidazolidinyl urea, diazolidinyl urea, sorbic acid, methylisothiazolinone, sodium dehydroacetate, dehydroacetic acid, quaternary ammonium salt-15, stearoyl chloride, zinc pyrithione, sodium metabisulfite, 2-bromo-2-nitropropane, chlorhexidine digluconate, polyaminopropyl biguanide, benzalkonium chloride, sodium sulfite, sodium salicylate, citric acid, neem Oil (Neem Oil), essential Oil(s), lactic acid and vitamin E (tocopherol). Other natural and synthetic preservatives can also be found in cosmetic handbooks and CTFA ingredient information. In some cases, one or more preservatives are optionally included in an amount ranging from about 0.1% to about 5% by weight of the composition or from about 0.3% to about 3% by weight of the composition. Preferably, the disclosed compositions are free of parabens.

The composition may also contain a thickener or gelling agent. Thickeners may be synthetic or natural. Thickeners may be used to gel or thicken the cosmetic composition to provide, for example, better deposition properties. Natural thickeners may include waxes, gums and powders and mixtures thereof. The natural wax may include beeswax, carnauba wax and/or candelilla wax and mixtures thereof. Natural gums may include gum arabic, xanthan gum, sclerotium (amigel) and/or cellulose and mixtures thereof. The natural powder may include clay, diatomaceous earth, fuller's earth, silica shell or sphere silica, fumed silica, sphere silica, hydrated silica, silica silicone, mica, titanated mica, talc, cellulose or sphere cellulose beads, microcrystalline cellulose, corn starch, rice starch, glycerol starch, soy flour, walnut shell flour, agar, sericite, dextran, nylon, silk powder, chalk, calcium carbonate, bismuth oxychloride, iron oxide, titanium dioxide, aluminum silicate, magnesium aluminum silicate, calcium silicate, magnesium trisilicate, starch octenyl aluminum succinate, bentonite, hectorite, kaolin, maltodextrin, montmorillonite, zinc laurate, zinc myristate, zinc rosin, aluminum oxide, attapulgite, tin oxide, titanium hydroxide, magnesium trisphosphate, or mixtures thereof.

Synthetic thickeners may include, for example, AMP isostearyl hydrolyzed collagen, AMP isostearyl hydrolyzed wheat protein, cetyl hydroxyethyl cellulose, chondroitin sulfate, cocamidopropyl dimethylamine C _8-16 Isoalkylsuccinyl lactoglobulin sulfonate, cocodimethyl ammonium hydroxypropyl hydrolyzed collagen, di-starch phosphate, ethyl ester of hydrolyzed animal protein, hydroxypropyl guar trimethyl ammonium chloride, hydrolyzed animal or vegetable protein, hydroxypropyl guar, hydroxypropyl methylcellulose, hydroxypropyl cellulose, hydroxyethyl cellulose, isostearyl hydrolyzed collagen,methylcellulose, nitrocellulose, nonoxyhydroxyethyl cellulose, acrylate polymers, acrylamide polymers, acrylic acid polymers (carbomers), PVM/MA decadiene cross-linked polymers, polyvinylpyrrolidone polymers, silicone oils, polyethylene thickeners, aluminum starch octenyl succinate, trihydroxystearin, and mixtures thereof. Other natural and synthetic thickeners are found in the cosmetic handbook and CTFA ingredient information.

The composition may include a conditioning agent or a care agent. The conditioning or conditioning agent may be synthetic or natural. The natural conditioning or care agents may include panthenol, vitamins, lauroyl lysine, isostearic acid, lecithin, soft emollient waxes, fruit/plant complexes, sweet almond oil, coconut oil, jojoba mix, honey, seaweed/algae, aloe, acai berry extract, wild pansy extract, lotus flower extract, papaya extract, zuzu extract, and/or orchid extract. Other suitable conditioning agents may include, but are not limited to, silicone-based agents (e.g., silicone quaternary ammonium salt 8), hydrolyzed wheat and/or soy proteins, amino acids (e.g., wheat amino acids, arginine), rice bran wax, meadow seed oil, mango seed oil, grape seed oil, jojoba seed oil, sweet almond oil, hydroxyethyl behenamidopropyl dimethyl ammonium chloride, aloe leaf extract, aloe leaf juice, phytantriol, retinyl palmitate, behentrimethite, cyclopentasiloxane, quaternary ammonium salt-91, stearamidopropyl dimethylamine, and combinations thereof. In some cases, one or more conditioning agents are optionally included in an amount of about 0.1% to about 5% by weight of the composition or about 0.3% to about 3% by weight of the composition.

Synthetic conditioning and conditioning agents may include: for example, mercapto-containing compounds, such as mercapto-containing quaternary nitrogen compounds; betaine/aliphatic organic acid; silicone oils, silicone gels, silicone polymers, fatty acids, esters of fatty acids, fatty alcohols, ethoxylates, polyol polyesters, glycerol, monoglycerides, glycerol polyesters, cholesterol esters, polyolefin glycols, polyolefin monoesters, polyolefin polyesters. Other natural and synthetic conditioning and care agents can be found in cosmetic handbooks and CTFA ingredient information.

The composition may also include one or more essential oils and natural oils. The essential oils may be synthetic or natural. The natural essential oils may include bergamot, german chamomile, moromile, roman chamomile, cassiterite, clove bud, eucalyptus globulus, olibanum, fennel, achyranthes, juniper, lemon grass, mountain sweet, green nectar, thyme red, rosemary, rose pelargonium, marigold, and ylang. The natural oil may include, for example, jojoba oil, sweet almond oil, coconut oil, shea butter, mango oil, and/or aloe vera oil or mixtures thereof.

Synthetic essential oils may include, for example, esters such as acetylated castor oil, glyceryl stearate, glyceryl dioleate, glyceryl distearate, glyceryl trioctanoate, glyceryl distearate, glyceryl linoleate, glyceryl myristate, glyceryl isostearate, PEG castor oil, PEG glyceryl oleate, PEG glyceryl stearate, PEG glyceryl tallow, PEG-4 diheptanoate, hydrogenated castor oil, isotridecyl isononanoate, isostearyl pivalate, tridecyl pivalate, cetyl octanoate, cetyl palmitate, cetyl ricinoleate, cetyl stearate, cetyl myristate, coco dicaprylate/decanoate, decyl isostearate, isodecyl oleate, isodecyl pivalate, isohexyl pivalate, tridecyl octanoate, octyl palmitate, dioctyl malate, tridecyl octanoate, myristyl myristate, stearyl alcohol; fatty alcohols such as oleyl alcohol, isocetyl alcohol; silicone oils, isoparaffins, hydrogenated polyisobutylenes, petrolatum, lanolin derivatives and sorbitan derivatives. Other natural and synthetic oils can be found in cosmetic handbooks and CTFA ingredient information.

The composition may further comprise one or more herbs and/or extracts and/or filtrates of herbs, such as Acacia Catechu (Acacia Catechu), acanthopanax senticosus (Acanthopanax Gracilistylus), sappan wood (Cacsalpinia Sappan), epimedium (Epimedium Spinosa), paeonia lactiflora (Paeonia lactiflora), paeonia obovata, atractylodes macrocephala (Atractylodes macrocephala), glycyrrhiza (Glycyrrhiza uralexisis), glycyrrhiza glabra (Glycyrrhiza glabra), lycium barbarum (Lycium chinense), smilax (Nauclea rhyncholphylla), cinnamomum cassia (Cinnainomum cassia), astragalus membranaceus (Astragalus membranaceus), scutellaria baicalensis (Scutellaria baicalensis), schizonepeta tenuifolia (Schizonepeta tenuifolia), ephedra (Ephemdra sinica), ophiopogon (Ophiopogon japonicus), paeonia lactiflora (Ophiopogon japonicus), artemisia annua (Ophiopogon japonicus), panax notoginseng (Ophiopogon japonicus), cornus officinalis (Ophiopogon japonicus), acorus gramineus (Ophiopogon japonicus), paeonia (Ophiopogon japonicus), gastrodia elata (Gastrodia elata), aspara (Ophiopogon japonicus), cuscuta (Ophiopogon japonicus), schisandra chinensis (Ophiopogon japonicus), yulan (Ophiopogon japonicus), epimedium (Ophiopogon japonicus), herba Houttuyniae (Ophiopogon japonicus), and herba Houttuyniae (Ophiopogon japonicus); perillae herba (Perilla frutescens) and aloe extract, alone or in any combination.

The composition may also include one or more plant seeds and/or extracts and/or filtrates of plant seeds obtained from plants, such as rapeseed (Brassica spp.), soybean (Glycine max), sunflower (linachus annuus)), oil palm (Elaeis guineeis), cottonseed (Gossypium spp.), peanut (arashis hypogaea), coconut (coco nucifera), castor (ricius communis), safflower (Carthamus tinctorius), mustard (Brassica spp. And Sinapis alba), coriander (Coriandrum sativum), pumpkin (Cucurbita maxima), linseed/flax (Linum usitatissimum), brazil nut (Bertholletia excelsa), jojoba (Simmondsia chinensis) and corn seed (Zea mays), alone or in combination.

The composition may also contain one or more surfactants which reduce the surface tension of the water and allow the hair formulation to slip over or onto the skin or hair. Surfactants also include detergents and soaps. The surfactant may be amphoteric, anionic or cationic. Suitable surfactants that may be used in the formulation include, but are not limited to: heptyl glucoside, 3-aminopropanesulfonic acid, ceteth-10 phosphate, steareth-21, steareth-2, almond amide, almond amidopropyl betaine, almond amidopropyl amine oxide, hydrogenated tallow aluminum glutamate, aluminum wool alkoxide, aminoethyl sulfate, aminopropyl month Gui Jigu amide, C12-15 alkyl ammonium sulfate, C12-15 para-ammonium sulfate, C12-16 alkyl ammonium sulfate, C9-10 perfluoroalkyl ammonium sulfonate, octanol ammonium sulfate, octanol 3-ammonium sulfate, monoglyceride ammonium sulfate, ammonium isosulfate, cocoyl sarcosinate, ammonium cumene sulfonate, polydimethyl silicone copolyol ammonium sulfate, dodecyl benzene ammonium sulfonate, ammonium isostearate, laureth ammonium sulfate, laureth-12 ammonium sulfate, laureth-5 ammonium sulfate ammonium laureth-6 carboxylate, ammonium laureth-7 sulfate, ammonium laureth-8 carboxylate, ammonium laureth-9 sulfate, ammonium lauroyl sarcosinate, ammonium lauryl sulfate, ammonium laurylsulfosuccinate, ammonium laurylsulfate, ammonium myristyl sulfate, ammonium nonylphenol-30 sulfate, ammonium nonylphenol-4 sulfate, ammonium oleate, ammonium palmate, ammonium polyacrylate, ammonium stearate, ammonium tolate, ammonium xylene sulfonate, amp-isostearyl gelatin/keratin amino acid/lysine hydroxypropyl trimethyl ammonium chloride, amp-isostearyl hydrolyzed collagen, almond oil PEG-6 ester, apricot amide propyl betaine, peanut glycoside-20, avocadamide propyl betaine, baba Shu Xianan, the polyoxyethylene ether of behenamide, behenamidopropyl betaine, oxidized behenamine, sodium lauryl polyether sulfate, sodium lauryl sulfate, lauryl alcohol, or cetostearyl-20, or a combination thereof. More than one surfactant may be included in the composition. The surfactant is optionally included in an amount ranging from about 0.1% to about 15% by weight of the formulation or from about 1% to about 10% by weight of the composition.

Suitable anionic surfactants include, but are not limited to, those containing carboxylate, sulfonate, and sulfate ions. Examples of anionic surfactants include sodium, potassium, ammonium of long chain alkyl sulfonates and alkylaryl sulfonates, such as sodium dodecyl benzene sulfonate; sodium dialkylsulfosuccinates, such as sodium dodecylbenzenesulfonate; sodium dialkylsulfosuccinates, such as sodium bis- (2-ethylsulfoxy) -sulfosuccinate; and alkyl sulfates such as sodium lauryl sulfate. Cationic surfactants include, but are not limited to, quaternary ammonium compounds such as benzalkonium chloride, benzethonium chloride, cetrimonium bromide, stearyl dimethylbenzyl ammonium chloride, amonyx cetac, polyoxyethylene and cocoamine. Examples of nonionic surfactants include ethylene glycol monostearate, propylene glycol myristate, glycerol monostearate, glycerol stearate, polyglycerol 4-oleate, sorbitan acylate, sucrose acylate PEG-150 laurate, PEG-400 monolaurate, polyoxyethylene monolaurate, polysorbate, polyoxyethylene octylphenyl ether, PEG-1000 cetyl ether, polyoxyethylene tridecyl ether, polypropylene glycol butyl ether,

401. Stearoyl monoisopropanolamide and polyoxyethylene hydrogenated tallow amide. Examples of amphoteric surfactants include sodium N-dodecyl- β -alanine, sodium N-lauryl- β -iminodipropionate, myristyl amphoacetate, lauryl betaine, and lauryl sulfobetaine.

The composition may also include one or more emollients which prevent moisture or irritation and which provide softening, soothing, coating, lubricating, moisturizing, protecting and/or cleansing. Suitable emollients for the composition may include, but are not limited to: isodecyl pivalate, organosilicon compounds (e.g. polydimethylsiloxane, cyclomethicone, dimethicone copolyol, or a mixture of cyclopentasiloxane and polydimethylsiloxane/vinyl dimethicone cross-linked polymer, cyclopentasiloxane polysiloxane), polyols such as sorbitol, glycerol, propylene glycol, ethylene glycol, polyethylene glycol, octanediol, polypropylene glycol, 1, 3-butanediol, hexylene glycol, isopentylene glycol, xylitol; ethylhexyl palmitate; triglycerides such as caprylic/capric triglyceride and fatty acid esters such as cetylstearyl isononanoate or cetyl palmitate. In particular embodiments, the emollient is polydimethylsiloxane, aminopolydimethylsiloxane, dimethiconol, cyclopentasiloxane, polydimethylsiloxane PEG-7 potassium ubiquitin phosphate, or a combination thereof. More than one emollient may be included in the composition. Emollients may optionally be included in amounts ranging from about 0.5% to about 15% by weight of the formulation or from about 1% to about 10% by weight of the composition.

The composition may also include one or more diluents. Water is a preferred diluent. The composition generally comprises greater than one percent by weight water, preferably greater than five percent by weight water, more preferably greater than 50 percent by weight water, and most preferably greater than 80 percent by weight water. Alcohols, such as ethanol and isopropanol, may be used in low concentrations (about 0.5% by weight of the formulation) to enhance hair penetration and/or reduce odor.

The composition may also include one or more viscosity modifiers, such as viscosity increasing agents. Classes of such agents include, but are not limited to: viscous liquids such as polyethylene glycol, semisynthetic polymers such as semisynthetic cellulose derivatives, synthetic polymers such as carbomers, poloxamers and polyethylenimines (e.g., PEI-10), naturally occurring polymers such as acacia, tragacanth, alginates (e.g., sodium alginate), carrageenan, vegetable gums such as xanthan gum, petrolatum, waxes, microparticle associated colloids such as bentonite, colloidal silica and microcrystalline cellulose, surfactants such as PPG-2 hydroxyethyl coco/isostearamide, emulsifiers such as distearth-75IPDI, and salts such as sodium chloride, and combinations thereof.

The composition may also include one or more antioxidants. Examples include, but are not limited to, tocopherol, BHT, ascorbic acid, camellia leaf extract, ascorbyl palmitate, magnesium ascorbyl phosphate, carotenoids, resveratrol, triethyl citrate, arbutin, kojic acid, tetrahexyldecyl ascorbate, superoxide dismutase, zinc, sodium metabisulfite, lycopene, ubiquinone, and combinations thereof.

The composition may also include one or more opacifiers. Opacifiers are added to the formulation to make it opaque. Suitable opacifiers include, but are not limited to, ethylene glycol distearate and ethoxylated fatty alcohols.

The composition may be in the form of a spray. Sprays typically comprise peptides and a cosmetically acceptable carrier. In some embodiments, the carrier is water or a mixture of water and alcohol. The spray formulation optionally includes antioxidants, sunscreens, vitamins, proteins, peptides, plant extracts, moisturizers, oils, emollients, lubricants, thickeners, hair conditioners, polymers and/or surfactants. The spray formulation may comprise a preservative. In some cases, the spray comprises a fragrance. In some embodiments, the spray comprises a surfactant. The hair spray formulation may be dispensed from a container comprising an aerosol dispenser or a pump spray dispenser. Such dispensers are known in the art and are commercially available from various manufacturers. When the spray composition is dispensed from a pressurized aerosol container, a propellant may be used to squeeze the formulation from the container. Suitable propellants include, but are not limited to, liquefiable gases or halogenated propellants. Examples of suitable propellants include dimethyl ether and hydrocarbon propellants such as propane, n-butane, isobutane, CFCs and CFC replacement propellants. The propellants may be used alone or in combination. The amount of propellant may be from about 10% to about 60% by weight of the spray composition. The propellant may be separated from the composition, such as in a dual compartment container. Other suitable aerosol dispensers feature a propellant that is compressed air that can be filled into the dispenser prior to use using a pump or equivalent device. The peptide-containing composition may also be applied to the hair using a conventional non-aerosol pump sprayer, i.e., a nebulizer.

In some cases, the composition may be in the form of a conditioning agent. Conditioning agents typically include peptides in a suitable carrier. In addition, conditioning agents may include cationic polymers derived from polysaccharides, such as cationic cellulose derivatives, cationic starch derivatives, cationic guar gum derivatives (e.g., guar hydroxypropyl trimethylammonium chloride), cationic locust bean gum derivatives, synthetic cationic polymers, polyquaternary ammonium salt polymers (e.g., polyquaternary ammonium salt-7, polyquaternary ammonium salt-11, polyquaternary ammonium salt-113), and mixtures or combinations of these agents. Conditioning agents may comprise other synthetic or natural polymers or polymers derived from biological preparation processes, which are functionalized where appropriate, for example by cationic or neutral groups. These polymers may have a stabilizing or strengthening effect and/or conditioning effect on hair (deposition on the surface of hair).

In some cases, the composition may be in the form of a shampoo. Shampoos generally comprise peptides in a suitable carrier. Peptides may be included in any suitable concentration. In addition, the shampoo may include from about 0.5% to about 20% by weight of a surfactant. Surfactants for use in shampoo compositions are well known in the art and are disclosed, for example, in U.S. patent No. 6,706,258 to Gallagher et al and U.S. patent No. 7,598,213 to Geary et al.

In some cases, the peptide is in the form of a liquid composition. In these cases, the liquid composition may comprise any suitable concentration of the peptide as described above in a suitable carrier, such as described above, which is typically a diluent.

The peptides may be applied to the hair (i.e., post-treatment application) typically as part of a composition after a hair treatment such as hair coloring, hair bleaching, permanent treatment, hair straightening, or other common hair treatments. In some other cases, the peptides may be applied to the hair (i.e., pretreatment application), typically as part of a composition, prior to hair treatment such as hair coloring, hair bleaching, permanent treatment, hair straightening, or other common hair treatments. Hair dyeing is understood in the art to mean a treatment that alters the color of hair, for example using oxidation dyes and their precursors, or direct dyes. Hair bleaching is understood in the art to mean a treatment for removing color from hair, for example by application of a bleach. The bleaching agent used in the bleaching process comprises the use of a combination of a developer (aqueous hydrogen peroxide) and a bleach powder (a powder containing at least one or more persulfates and one or more alkalizing agents). Such treatments are well known to those skilled in the art. The peptide-containing composition in any suitable form may be administered on the same day after treatment, or may be administered later, for example within 1 to 2 weeks after treatment. In some cases, the amount of peptide-containing composition applied may be sufficient to saturate the hair. The peptide-containing composition may be applied to the hair as a single application, or may be repeated one or more times. The volume of peptide-containing composition applied to the hair in each application may be from about 1mL to about 100mL per person, depending on the length and volume of the hair. In some embodiments, the peptide-containing composition can be repeatedly administered immediately (e.g., within 10 to 15 seconds) or about 1-5 minutes, 5-7.5 minutes, 10 minutes, 5-10 minutes, 12.5 minutes, 10-15 minutes, 10-17.5 minutes, 10-20 minutes, or 15-20 minutes after the first administration. In some cases, it may be desirable to remove the peptide-containing composition from the hair after application, for example by rinsing and/or shampooing after application, for example within 10, 15, 25, 30, 45 or 60 seconds, or within two, three, four or five minutes after application. Alternatively, the peptide-containing composition may be rinsed from the hair within about 30 minutes after application, between about 5 minutes and about 20 minutes, or within about 10 minutes after application of the peptide-containing composition to the hair, depending on the type of hair.

The above description is provided to enable one skilled in the art to make and use the disclosed peptides and is provided in the context of a particular application and its requirements. Various modifications to the embodiments and aspects will be readily apparent to those skilled in the art, and the generic principles defined herein may be applied to other aspects, embodiments, and applications without departing from the spirit and scope of the information disclosed herein. The examples herein are not intended to be limited to the aspects or embodiments described, but are to be accorded the widest scope consistent with the principles and features disclosed herein. A further understanding may be obtained by reference to certain specific examples.

The following peptides were synthesized and provided by commercial suppliers (Genscript USA, inc., piscataway, NJ): SEQ ID NO. 1 and SEQ ID NO. 3-SEQ ID NO. 109.

Example 1: heat treatment only

A bundle of curly Brazilian hair (Brazilian hair) was cut into 1/2 inch wide samples. The bundles were then shampooed and air dried. Hair was straightened using an iron at 460°f. Once the hair is significantly straightened, the hair is tightly wrapped with aluminum foil paper. The iron was applied to a portion of the wrapped hair by holding the iron on the portion for 10 seconds. This process is repeated until all parts of the hair are ironed.

Six separate solutions of each peptide corresponding to SEQ ID NO 3 through SEQ ID NO 8 were dissolved in deionized ("DI") water at a concentration of about 1 milligram per milliliter ("mg/mL") and then applied to the respective hair samples until the hair samples were saturated. The saturated hair was allowed to stand at 37℃for 1 hour. The hair was then blow-dried under moderate heat while gently pulling the hair into a straight shape. The hair is then ironed with an iron at 400F.

The straightened hair was washed with a shampoo and allowed to air dry, and the washing/drying procedure was repeated 10 times in total. After such treatment, each hair sample was significantly straightened and small waves remained in the treated hair, as compared to the untreated sample. There was little recognizable difference in efficacy among the six designed keratin-binding peptides, although the peptides corresponding to SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7 and SEQ ID NO:8 showed slightly higher straightening efficiency than SEQ ID NO:3 and SEQ ID NO: 4.

Example 2: treatment with lye and hydrogen peroxide

A bundle of curled Brazil hair was cut into 1/2 inch wide samples. The bundles were then shampooed and air dried. The hair was then immersed in sodium hydroxide solution at pH 12 for 30 minutes at room temperature. After this time, the hair was rinsed with DI water. The hair was then blow-dried under moderate heat while gently pulling the hair into a straight shape. The hair is then ironed with an iron at 400F.

Six separate solutions of each designed keratin-binding peptide corresponding to SEQ ID No. 3 through SEQ ID No. 8 were dissolved in DI water at a concentration of 1mg/mL and then applied to each hair sample until the hair sample was saturated, and then the hair samples were allowed to stand at room temperature for 30 minutes. The hair samples were then blow dried under moderate heat while gently pulling the hair into a straight shape. The hair is then ironed with an iron at 400F.

Then willThe Oreor Creme 40 volume of developer was applied to the hair sample until the hair sample was saturated and then allowed to stand at room temperature for 30 minutes. The hair samples were then rinsed with DI water.

Each straightened hair sample was shampooed and air dried, and the washing/drying procedure was repeated 10 times in total. After this treatment, each hair sample was significantly straightened and only slightly wavy remained in the treated hair, as compared to the untreated hair sample. There was little difference in the efficacy recognizable among the six peptides, although the peptides corresponding to SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7 and SEQ ID NO:8 showed slightly higher straightening efficiency than SEQ ID NO:3 and SEQ ID NO: 4.

Example 3: treatment with lye and glucose oxidase

A solution of the peptide corresponding to SEQ ID NO:8 in DI water at a concentration of 1mg/mL was then applied to the hair sample until the hair sample was saturated, and the hair was allowed to stand at room temperature for 30 minutes. The hair was then blow-dried under moderate heat while gently pulling the hair into a straight shape. The hair is then ironed with an iron at 400F.

A solution of glucose oxidase (2 mg/mL) and glucose (18 mg/mL) in 50mM sodium phosphate buffer pH 5.8 was then applied to the hair until the hair was saturated, and the hair was allowed to stand at room temperature for 30 minutes. The hair was then rinsed with DI water.

The straightened hair was washed with a shampoo and allowed to air dry, and the washing/drying procedure was repeated 10 times in total. After this treatment, each hair sample was significantly straightened and only slightly wavy remained in the treated hair, as compared to the untreated hair sample.

Example 4: treatment with glutathione reductase and hydrogen peroxide

A bundle of curled Brazil hair was cut into 1/2 inch wide samples. The bundles were then shampooed and air dried. The hair was then immersed in a solution of glutathione reductase (0.01 mg/mL), glutathione (100 mg/mL) and nicotinamide adenine dinucleotide phosphate (0.083 mg/mL) in 50mM sodium phosphate buffer pH 8 for 30 minutes at room temperature. After this time, the hair was rinsed with DI water. The hair was then blow-dried under moderate heat while gently pulling the hair into a straight shape. The hair is then ironed with an iron at 400F.

A solution of the peptide corresponding to SEQ ID NO:8 in DI water at a concentration of 1mg/mL was then applied to the hair until the hair was saturated and allowed to stand at room temperature for 30 minutes. The hair was then blow-dried under moderate heat while gently pulling the hair into a straight shape. The hair is then ironed with an iron at 400F.

Then willThe Oreor Creme 40 volume of developer was applied to the hair until the hair was saturated, and then the hair was left to stand at room temperature for 30 minutes. The hair was then rinsed with DI water.

The straightened hair was washed with shampoo and air-dried, and the washing/drying procedure was repeated 10 times in total. After this treatment, each hair sample was significantly straightened and only slightly wavy remained in the treated hair, as compared to the untreated hair sample.

Example 5: treatment with glutathione and glucose oxidase

A bundle of curled Brazil hair was cut into 1/2 inch wide samples. The bundles were then shampooed and air dried. The hair was then immersed in a solution of glutathione (100 mg/mL) in sodium hydroxide pH 9 for 30 minutes at room temperature. After this time, the hair was rinsed with DI water. The hair was then blow-dried under moderate heat while gently pulling the hair into a straight shape. The hair is then ironed with an iron at 400F.

A solution of glucose oxidase (2 mg/mL) and glucose (18 mg/mL) in 50mM sodium phosphate buffer pH 5.8 was then applied to the hair until the hair was saturated and the hair was allowed to stand at room temperature for 30 minutes. The hair was then rinsed with DI water.

Example 6: treatment with ammonium thioglycolate and hydrogen peroxide

A bundle of curled Brazil hair was cut into 1/2 inch wide samples. The bundles were then shampooed and air dried. The hair was then immersed in a solution of ammonium thioglycolate (10% v/v) in sodium hydroxide pH 10 for 30 minutes at room temperature. After this time, the hair was rinsed with DI water. The hair was then blow-dried under moderate heat while gently pulling the hair into a straight shape. The hair is then ironed with an iron at 400F.

In some samples, a solution of the peptide corresponding to SEQ ID NO:8 in DI water at a concentration of 1mg/mL was then applied to the hair until the hair was saturated and allowed to stand at room temperature for 30 minutes. In these samples, the hair was then blow-dried under moderate heat while gently pulling the hair into a straight shape. The hair is then ironed with an iron at 400F.

For all hair samples, a solution of hydrogen peroxide (2% v/v) was then applied to the hair until the hair was saturated and the hair was allowed to stand at room temperature for 30 minutes. The hair was then rinsed with DI water.

The straightened hair was washed with shampoo and air-dried, and the washing/drying procedure was repeated 30 times in total. After this treatment, the treated hair samples were significantly straightened and only slightly wavy remained in the treated hair as compared to the untreated hair samples.

The breaking force of the treated hair samples was measured using custom-made equipment. Individual hairs were cut into 13 cm long sections. The two ends of the hair are wound by adhesive tapes, and the distance between the adhesive tapes and the two ends is 1 cm respectively. The hair was then held in a vertical position between the two clips (top = fixed, bottom = movable) with a 1 cm long clip, with the clip aligned with the end of the tape wrap of hair. Force was gradually applied to the bottom clamp and the force at break was recorded. Ten replicates were collected for each treatment group.

Example 7: fluorescence binding studies

To a 500. Mu.L DI water solution was added 1mg of SEQ ID NO:8. Then, a solution of 84mg of sodium bicarbonate in 1mL of DI water was prepared, and 12. Mu.L of the solution was added to the SEQ ID NO:8 solution. Prior to conjugation, 1mg Alexa Fluor 647NHS ester (Thermo Fisher Scientific) dye molecules were dissolved in 100. Mu.L DMSO and 15. Mu.L of this solution was added to the SEQ ID NO:8 solution. After the addition of the dye, the solution was incubated at 4℃for 16 hours in the absence of light. Unbound dye molecules were removed using a PD MiniTrap G-10 column (Cytiva) using deionized water as the eluent. Fractions containing dye-labeled SEQ ID NO. 8 were collected.

The hair samples were then treated according to example 6, except that: treatment with dye-labeled SEQ ID NO. 8 instead of SEQ ID NO. 8 was performed while changing the peptide concentration, binding time, number of times SEQ ID NO. 8 was applied, or number of times shampoo was applied at the end of treatment.

Fluorescence images were collected on an EVOS M7000 imaging system (Thermo Fisher Scientific) using a Cy5 filter set. Images were collected at a light intensity of 0.0023 using an exposure time of 0.1 seconds.

Example 8: comparative tensile study

BW2 hair powder whitening agent (bleach) (Clariol) and orer creme 40 volume developer (aqueous hydrogen peroxide) (L' Oreal) were mixed in a 1:2 ratio and stirred for 1 minute until the bleaching mixture became smooth and homogeneous and was used to bleach the brazil hair sample. The hair swatches were saturated in the bleaching mixture and left to stand at room temperature for 45 minutes. The hair swatches were then rinsed with deionized water (DI) for 2 minutes, thoroughly shampooed, and then air dried. The bleaching procedure was repeated two more times to produce bleached brazil hair samples.

The strands of raw and bleached curly brazil hair were cut into 1/2 inch wide samples. The bundles were then shampooed and air dried. The hair was then soaked in a solution of cysteine (100 mg/mL) and ascorbic acid (10 mg/mL) in sodium hydroxide pH 10 for 30 minutes at room temperature. After this time, the hair was rinsed with DI water. The hair was then blow-dried under moderate heat while gently pulling the hair into a straight shape. The hair is then ironed with an iron at 400F.

In some samples, a solution of the peptide corresponding to SEQ ID NO:1, SEQ ID NO:8, SEQ ID NO:9 or SEQ ID NO:10 in DI water at a concentration of 1mg/mL was then applied to the hair until the hair was saturated and allowed to stand at room temperature for 30 minutes. The hair was then blow-dried under moderate heat while gently pulling the hair into a straight shape. The hair is then ironed with an iron at 400F.

The straightened hair is washed with a shampoo and air-dried. The breaking force of the treated hair samples was measured using custom-made equipment. Individual hairs were cut into 13 cm long sections. The two ends of the hair are wound by adhesive tapes, and the distance between the adhesive tapes and the two ends is 1 cm respectively. The hair was then held in a vertical position between the two clips (top = fixed, bottom = movable) with a 1 cm long clip, with the clip aligned with the end of the tape wrap of hair. Force was gradually applied to the bottom clamp and the force at break was recorded. Ten replicates were collected for each treatment group.

Each hair sample was then washed 9 more times with shampoo and air dried. Ten replicates were then used for each sample after these additional washes to re-measure the breaking force of each hair sample.

Example 9: measurement of peptide stability for shampoo washes

To each solution of 500. Mu.L DI water was added 1mg of one of the peptides corresponding to SEQ ID NOS:1 and 2-17. Then, a solution of 84mg of sodium bicarbonate in 1mL of DI water was prepared, and 12. Mu.L of the solution was added to each peptide solution. Prior to conjugation, 5mg Alexa Fluor 647NHS ester (Thermo Fisher Scientific) dye molecules were dissolved in 500. Mu.L DMSO and 15. Mu.L of this solution was added to each peptide solution. After the addition of the dye, the solution was incubated at 4℃for 16 hours in the absence of light. Unbound dye molecules were removed using a PD MiniTrap G-10 column (Cytiva) using DI water as eluent. Fractions containing dye-labeled peptide were collected and diluted to a final peptide concentration of 1 mg/mL.

Hair samples were then treated according to example 8, except that: during treatment with the peptides, the hair was treated with a single dye-labeled peptide according to SEQ ID NOS 1 and 2-17. For each set of conditions, three separate straightening schemes are performed.

Fluorescence images were collected on an EVOS M7000 imaging system (Thermo Fisher Scientific) using a Cy5 filter set. Images were collected at a light intensity of 0.0023 using an exposure time of 0.1 seconds. After fluorescence measurement, the hair samples were washed 9 more times with shampoo, towel dried, and again subjected to fluorescence imaging.

The image file was processed into a 16-bit grayscale image using ImageJ software. A lower threshold of 497 intensity units is first applied to each image to remove background intensity from areas that do not contain hair strands. The mean and standard deviation of fluorescence intensity in the remaining region (corresponding to the hair strand containing the fluorescent-labeled peptide) was then directly calculated.

Analysis of peptides showing strong resistance to shampoo washing showed NO statistically significant decrease in fluorescence intensity between 1 and 10 shampoos in both the original (fig. 9 a) and bleached (fig. 9 b) hair, indicating that almost all of these peptides have Q13C substitutions relative to SEQ ID No. 1. In fact, peptides with this substitution showed significantly smaller percentage of hair loss after 10 shampoo washes (fig. 9 c). Furthermore, SEQ ID NOS:4, 11, 12 and 13 all have Q13C substitutions relative to SEQ ID NO:1, and differ in sequence only in the number of other cysteine substitutions at the common site (3, 2, 1 and 0 additional cysteine substitutions, respectively). However, only hair treated with SEQ ID NOS.4 and 11 showed NO statistically significant decrease in fluorescence intensity between 1 and 10 shampoo washes. SEQ ID NOS 14, 15 and 16 differ from SEQ ID NOS 6, 7 and 8, respectively, in that the former sequence lacks the Q13C substitution found in the corresponding sequence of the latter. Although hair treated with all of the latter peptides showed NO statistically significant decrease in fluorescence intensity between 1 and 10 shampoo washes, SEQ ID NOS 14 and 16 showed significant decreases, which generally supported the theory that Q13C substitution relative to SEQ ID NO 1 was promoting strong binding to hair such that the peptides were not removed from hair during shampoo washes. However, some peptides lacking Q13C substitution also show strong retention in hair by 10 shampoo washes, such as SEQ ID NO:15 (which contains 10 cysteine substitutions relative to SEQ ID NO: 1). Similarly, peptides with Q3C and/or Q8C substitutions also exhibit resistance to repeated shampooing and thus have strong binding properties to the hair.

Example 10: measurement of the retention in the hair of a peptide library subjected to shampoo washing

1g of Brazil hair sample was washed with 70% ethanol and incubated in 20mL of a 2:1 chloroform-methanol (v/v) solution at room temperature for 16 hours to remove lipids from the hair. The hair was then rinsed thoroughly with DI water and added to 20mL of 100mM Tris buffer pH 8.0 containing 8M urea and 10% 2-mercaptoethanol (v/v). The hair was incubated in this mixture for 5 days at 50 ℃ after which the mixture was filtered. The filtrate was dialyzed against deionized water at 4 ℃ using 8 exchanges with at least 3 hours between each exchange. The mixture was centrifuged at 10,000Xg for 30 minutes at 4 ℃, the supernatant was collected, and the concentration of keratin in the supernatant was measured using BCA protein assay (Thermo Fisher Scientific).

The keratin mixture was diluted to a concentration of 5mg/mL and to 1mL of this solution was added 60. Mu.L of 84mg sodium bicarbonate in 1mL DI water. Prior to conjugation, 1mg Alexa Fluor647NHS ester (Thermo Fisher Scientific) dye molecules were dissolved in 100. Mu.L DMSO and 81. Mu.L of this solution was added to the keratin solution. After the addition of the dye, the solution was incubated at 4℃for 16 hours in the absence of light. Unbound dye molecules were removed using a PD MiniTrap G-10 column (Cytiva) using DI water as eluent. The fraction containing dye-labeled keratin was collected.

A4 mg sample of each of 92 peptides corresponding to SEQ ID NOS 18-109, containing 1 to 12 cysteine substitutions and 0 to 4 alanine substitutions, was dissolved in 1mL DI water. Then 50 μl of each solution was added to one of 3 independent Nunc Covalink NH 96 well plates (Thermo Fisher Scientific), where the wells were functionalized with free amine, so that three replicates could be obtained in future experiments. Then, 5.52mg of N-hydroxysulfosuccinimide was dissolved in 15mL of DI water, and 50. Mu.L of the solution was added to each well. Then, 18.45mg of N- (3-dimethylaminopropyl) -N' -ethylcarbodiimide hydrochloride was dissolved in 15mL of DI water, and 50. Mu.L of this solution was added to each well. The well plate was incubated for 2 hours at room temperature. Each well was then washed 5 times with DI water, the last wash using an incubation time of 15 minutes.

Keratin labeled with Alexa Fluor 647 was diluted to a concentration of 0.2mg/mL in sodium hydroxide pH 10 and 80 μl of this solution was added to each well. The well plate was incubated at 37℃for 1 hour. Each well was then washed 5 times with DI water, the last wash using an incubation time of 15 minutes. The wells were then incubated with 10% shampoo solution for 5 minutes at room temperature, washed 3 times with DI water, and air dried in the dark.

Fluorescence images were collected for each of the three duplicate well plates on an EVOS M7000 imaging system (Thermo Fisher Scientific) using a Cy5 filter set. Images were collected at a light intensity of 0.15 using an exposure time of 0.1 seconds. After fluorescence measurement, wells were subjected to 9 additional 5 minutes incubation cycles in 10% shampoo at room temperature. The wells were then washed 3 times with DI water, air dried in the dark, and fluorescence imaged again.

Analysis of the results showed that peptides with Q13C or H6C substitutions showed significantly stronger binding to repeated shampoo washes compared to peptides without these substitutions (fig. 10 a). Peptides containing both Q13C substitutions and at least 1 additional cysteine substitutions showed statistically significant improvements in shampoo wash resistance (fig. 10 b). Similarly, peptides containing H6C substitutions and at least 1 additional cysteine substitutions exhibited statistically significant improvements in shampoo wash resistance (fig. 10C). However, peptides containing neither Q13C nor H6C substitutions but 3 or more cysteine substitutions exhibited significantly greater resistance to repeated shampoo washes compared to peptides having fewer than 3 cysteine substitutions or containing only Q13C and/or H6C substitutions (fig. 10 d).

Sequence listing

<110> PURVALA

<120> compositions for hair straightening and styling and methods of use

<130> 20-10 conversion

<140> 63/205,666

<141> 2020-12-19

<160> 109

<170> patent In version 3.5

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<223> peptide

<400> 32

Cys Cys Gln Cys Cys His Cys Gln Cys Cys Phe Ser Gln Tyr Cys Lys

1 5 10 15

Val Cys Cys Phe Pro Lys

20

<210> 33

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 33

Gln Gly Gln Val Gln His Cys Gln Ala Ala Phe Ser Gln Tyr Lys Cys

1 5 10 15

Val Cys Leu Phe Pro Lys

20

<210> 34

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 34

Cys Gly Cys Cys Gln Cys Leu Ala Ala Ala Cys Ser Gln Tyr Lys Ala

1 5 10 15

Val Cys Ala Cys Pro Lys

20

<210> 35

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 35

Gln Gly Cys Val Gln His Leu Gln Ala Cys Cys Cys Gln Tyr Cys Lys

1 5 10 15

Val Glu Leu Cys Pro Lys

20

<210> 36

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 36

Gln Gly Cys Val Gln His Leu Gln Ala Ala Cys Ser Gln Tyr Lys Lys

1 5 10 15

Val Glu Leu Phe Pro Lys

20

<210> 37

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 37

Gln Gly Gln Val Gln Ala Leu Gln Ala Ala Phe Ser Gln Cys Ala Lys

1 5 10 15

Val Glu Ala Phe Pro Lys

20

<210> 38

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 38

Gln Gly Gln Val Gln His Leu Gln Ala Cys Phe Ser Gln Tyr Lys Lys

1 5 10 15

Cys Glu Leu Phe Pro Lys

20

<210> 39

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 39

Gln Cys Cys Cys Gln His Cys Gln Ala Ala Cys Ser Gln Ala Lys Ala

1 5 10 15

Cys Cys Cys Cys Pro Lys

20

<210> 40

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 40

Gln Cys Ala Cys Ala Cys Leu Cys Cys Ala Cys Cys Cys Cys Lys Ala

1 5 10 15

Ala Glu Cys Phe Cys Lys

20

<210> 41

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 41

Gln Ala Cys Val Gln Ala Leu Ala Ala Cys Phe Ser Gln Cys Lys Cys

1 5 10 15

Val Cys Leu Cys Pro Cys

20

<210> 42

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 42

Cys Cys Gln Val Gln Cys Cys Cys Ala Ala Cys Cys Gln Tyr Cys Lys

1 5 10 15

Val Glu Cys Phe Pro Lys

20

<210> 43

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 43

Gln Gly Gln Val Gln His Cys Cys Ala Ala Phe Ser Gln Tyr Lys Lys

1 5 10 15

Val Glu Leu Phe Pro Lys

20

<210> 44

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 44

Gln Gly Cys Val Cys His Leu Cys Cys Cys Cys Cys Cys Cys Lys Cys

1 5 10 15

Val Glu Cys Phe Cys Lys

20

<210> 45

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 45

Gln Cys Gln Ala Gln Cys Ala Cys Ala Ala Cys Cys Gln Tyr Lys Lys

1 5 10 15

Val Ala Cys Phe Pro Lys

20

<210> 46

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 46

Gln Gly Gln Cys Cys Cys Leu Gln Cys Ala Cys Cys Gln Tyr Cys Lys

1 5 10 15

Cys Glu Cys Phe Pro Cys

20

<210> 47

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 47

Cys Gly Gln Val Cys Cys Cys Gln Ala Cys Phe Ser Cys Cys Cys Lys

1 5 10 15

Cys Cys Leu Phe Cys Lys

20

<210> 48

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 48

Gln Gly Cys Val Ala Cys Leu Gln Cys Ala Phe Ser Gln Tyr Lys Lys

1 5 10 15

Cys Ala Ala Cys Pro Cys

20

<210> 49

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 49

Cys Gly Cys Val Gln His Cys Gln Ala Ala Phe Cys Gln Tyr Ala Lys

1 5 10 15

Val Cys Leu Phe Ala Lys

20

<210> 50

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 50

Gln Gly Cys Cys Cys His Cys Cys Cys Cys Phe Cys Gln Cys Cys Cys

1 5 10 15

Val Glu Leu Phe Pro Cys

20

<210> 51

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 51

Gln Gly Gln Cys Gln His Cys Gln Ala Ala Phe Ser Gln Ala Cys Lys

1 5 10 15

Ala Glu Leu Phe Pro Lys

20

<210> 52

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 52

Cys Cys Cys Val Cys Cys Cys Gln Ala Ala Cys Ser Ala Tyr Cys Cys

1 5 10 15

Cys Cys Ala Cys Pro Lys

20

<210> 53

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 53

Cys Gly Cys Val Gln His Leu Gln Ala Cys Phe Ser Gln Cys Cys Cys

1 5 10 15

Val Glu Leu Cys Cys Cys

20

<210> 54

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 54

Gln Cys Gln Ala Gln His Leu Gln Ala Cys Ala Ser Gln Tyr Lys Lys

1 5 10 15

Val Ala Leu Phe Pro Lys

20

<210> 55

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 55

Gln Gly Cys Cys Gln His Leu Cys Ala Ala Phe Ser Gln Tyr Lys Cys

1 5 10 15

Val Glu Leu Phe Pro Lys

20

<210> 56

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 56

Cys Gly Gln Val Gln His Leu Cys Ala Ala Phe Ser Gln Tyr Cys Lys

1 5 10 15

Val Glu Ala Phe Pro Cys

20

<210> 57

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 57

Gln Gly Ala Cys Gln Cys Cys Cys Ala Ala Ala Ser Gln Tyr Ala Cys

1 5 10 15

Val Glu Leu Phe Pro Lys

20

<210> 58

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 58

Cys Gly Gln Val Cys His Leu Gln Ala Cys Phe Ala Gln Tyr Lys Cys

1 5 10 15

Val Glu Leu Phe Pro Lys

20

<210> 59

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 59

Cys Gly Cys Cys Ala Ala Leu Cys Ala Cys Cys Ser Cys Tyr Lys Lys

1 5 10 15

Ala Cys Cys Phe Pro Ala

20

<210> 60

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 60

Gln Gly Gln Val Gln His Leu Cys Ala Cys Cys Ser Cys Tyr Lys Lys

1 5 10 15

Val Cys Cys Cys Cys Cys

20

<210> 61

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 61

Cys Cys Cys Cys Gln Ala Ala Cys Cys Ala Cys Ser Cys Tyr Cys Lys

1 5 10 15

Val Glu Leu Phe Cys Lys

20

<210> 62

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 62

Gln Cys Gln Val Gln His Leu Gln Ala Ala Phe Cys Gln Cys Lys Cys

1 5 10 15

Cys Glu Leu Cys Pro Lys

20

<210> 63

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 63

Gln Gly Gln Val Gln Cys Leu Cys Ala Ala Phe Ser Gln Tyr Lys Lys

1 5 10 15

Cys Glu Cys Phe Pro Lys

20

<210> 64

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 64

Cys Gly Cys Ala Cys Ala Leu Ala Ala Cys Cys Ser Cys Cys Cys Cys

1 5 10 15

Val Ala Leu Phe Pro Lys

20

<210> 65

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 65

Gln Ala Gln Ala Gln His Leu Cys Cys Ala Phe Cys Cys Cys Lys Lys

1 5 10 15

Cys Glu Leu Cys Pro Lys

20

<210> 66

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 66

Cys Gly Cys Cys Gln His Leu Gln Cys Cys Phe Cys Cys Tyr Lys Cys

1 5 10 15

Val Cys Cys Phe Pro Lys

20

<210> 67

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 67

Cys Cys Gln Cys Gln Cys Leu Cys Ala Ala Phe Ser Cys Tyr Lys Lys

1 5 10 15

Val Cys Cys Cys Pro Lys

20

<210> 68

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 68

Gln Ala Cys Ala Gln Cys Leu Cys Ala Ala Phe Ser Gln Tyr Ala Lys

1 5 10 15

Val Glu Leu Phe Pro Lys

20

<210> 69

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 69

Gln Gly Gln Val Gln His Leu Gln Cys Ala Phe Cys Cys Tyr Lys Lys

1 5 10 15

Val Glu Leu Phe Pro Lys

20

<210> 70

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 70

Gln Gly Gln Val Gln His Leu Gln Ala Cys Phe Ser Cys Tyr Lys Cys

1 5 10 15

Val Glu Leu Phe Pro Cys

20

<210> 71

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 71

Gln Gly Gln Val Cys Cys Cys Cys Ala Ala Phe Cys Cys Cys Lys Cys

1 5 10 15

Val Glu Leu Cys Cys Lys

20

<210> 72

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 72

Gln Gly Gln Val Gln His Cys Gln Ala Ala Phe Ser Gln Tyr Cys Lys

1 5 10 15

Val Glu Leu Ala Ala Lys

20

<210> 73

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 73

Gln Gly Gln Val Gln His Leu Gln Ala Ala Phe Ser Gln Tyr Lys Lys

1 5 10 15

Val Cys Leu Phe Pro Lys

20

<210> 74

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 74

Gln Gly Gln Val Gln Cys Leu Gln Ala Ala Phe Cys Gln Cys Lys Lys

1 5 10 15

Val Glu Cys Phe Pro Lys

20

<210> 75

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 75

Gln Gly Cys Val Gln Cys Leu Gln Cys Ala Cys Cys Ala Cys Lys Cys

1 5 10 15

Cys Cys Leu Phe Cys Ala

20

<210> 76

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 76

Cys Ala Cys Cys Gln Ala Cys Cys Ala Cys Phe Ser Cys Ala Lys Cys

1 5 10 15

Ala Glu Cys Phe Cys Lys

20

<210> 77

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 77

Gln Gly Gln Val Gln His Cys Gln Ala Ala Phe Ser Gln Tyr Lys Lys

1 5 10 15

Cys Cys Leu Phe Pro Lys

20

<210> 78

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 78

Gln Ala Gln Val Gln His Leu Gln Ala Ala Phe Ser Gln Cys Cys Cys

1 5 10 15

Val Glu Leu Phe Cys Lys

20

<210> 79

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 79

Cys Cys Gln Cys Cys Cys Leu Cys Cys Ala Phe Cys Cys Cys Cys Lys

1 5 10 15

Cys Glu Leu Phe Pro Lys

20

<210> 80

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 80

Gln Gly Gln Val Gln Cys Leu Cys Cys Cys Cys Ser Gln Tyr Lys Lys

1 5 10 15

Val Glu Cys Phe Pro Lys

20

<210> 81

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 81

Gln Gly Gln Val Gln His Leu Gln Ala Cys Phe Ser Ala Tyr Lys Lys

1 5 10 15

Val Glu Leu Phe Pro Lys

20

<210> 82

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 82

Gln Gly Gln Val Cys His Cys Cys Cys Ala Phe Ala Gln Tyr Lys Cys

1 5 10 15

Ala Cys Ala Phe Pro Lys

20

<210> 83

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 83

Gln Gly Gln Cys Gln Cys Leu Cys Ala Ala Phe Cys Cys Tyr Lys Lys

1 5 10 15

Val Glu Leu Cys Pro Lys

20

<210> 84

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 84

Gln Gly Gln Val Gln Cys Leu Gln Ala Ala Ala Ser Gln Tyr Lys Lys

1 5 10 15

Cys Glu Leu Phe Cys Lys

20

<210> 85

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 85

Gln Gly Gln Val Gln Cys Cys Gln Ala Ala Cys Ser Gln Tyr Lys Lys

1 5 10 15

Val Glu Leu Phe Pro Cys

20

<210> 86

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 86

Ala Gly Cys Val Gln Cys Leu Cys Cys Cys Cys Cys Cys Tyr Ala Lys

1 5 10 15

Val Cys Ala Phe Pro Lys

20

<210> 87

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 87

Gln Gly Cys Cys Gln Cys Cys Cys Ala Cys Cys Ser Gln Tyr Lys Lys

1 5 10 15

Val Glu Leu Phe Pro Cys

20

<210> 88

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 88

Ala Cys Gln Val Gln His Cys Cys Cys Ala Phe Cys Cys Tyr Cys Cys

1 5 10 15

Val Cys Cys Phe Cys Cys

20

<210> 89

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 89

Cys Cys Cys Cys Gln His Leu Cys Ala Cys Phe Ser Cys Tyr Cys Lys

1 5 10 15

Val Glu Cys Phe Cys Lys

20

<210> 90

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 90

Gln Gly Gln Val Gln His Leu Gln Cys Ala Phe Ser Cys Tyr Lys Lys

1 5 10 15

Val Glu Leu Phe Cys Cys

20

<210> 91

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 91

Cys Gly Gln Val Gln His Leu Gln Ala Ala Cys Ser Gln Tyr Lys Cys

1 5 10 15

Val Glu Leu Phe Cys Lys

20

<210> 92

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 92

Gln Cys Cys Val Cys Cys Ala Gln Ala Cys Phe Cys Gln Tyr Lys Lys

1 5 10 15

Cys Glu Cys Cys Cys Ala

20

<210> 93

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 93

Cys Gly Ala Val Gln Cys Cys Cys Ala Cys Phe Cys Cys Cys Ala Lys

1 5 10 15

Val Glu Cys Phe Cys Ala

20

<210> 94

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 94

Cys Gly Cys Cys Gln Cys Leu Cys Ala Ala Cys Ser Cys Tyr Cys Cys

1 5 10 15

Val Cys Leu Cys Cys Lys

20

<210> 95

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 95

Gln Gly Gln Val Gln Cys Leu Gln Cys Ala Phe Ser Gln Ala Lys Cys

1 5 10 15

Ala Glu Ala Phe Pro Ala

20

<210> 96

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 96

Gln Gly Cys Ala Gln His Ala Cys Ala Ala Phe Ser Gln Tyr Lys Ala

1 5 10 15

Val Glu Leu Phe Pro Cys

20

<210> 97

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 97

Gln Gly Cys Val Gln His Leu Gln Cys Ala Cys Ser Gln Tyr Lys Lys

1 5 10 15

Cys Glu Leu Ala Cys Lys

20

<210> 98

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 98

Gln Gly Gln Cys Cys His Leu Gln Ala Ala Phe Ser Gln Tyr Lys Lys

1 5 10 15

Ala Glu Leu Phe Pro Lys

20

<210> 99

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 99

Cys Cys Cys Cys Ala His Cys Ala Cys Ala Phe Ser Gln Tyr Lys Cys

1 5 10 15

Ala Cys Cys Cys Pro Cys

20

<210> 100

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 100

Cys Cys Gln Cys Gln His Leu Ala Ala Cys Phe Ala Gln Tyr Cys Ala

1 5 10 15

Cys Cys Cys Cys Cys Lys

20

<210> 101

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 101

Cys Cys Cys Val Cys Cys Leu Gln Ala Ala Cys Cys Cys Tyr Lys Lys

1 5 10 15

Cys Cys Leu Cys Cys Lys

20

<210> 102

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 102

Ala Gly Cys Cys Gln Cys Cys Cys Cys Ala Phe Cys Gln Tyr Lys Lys

1 5 10 15

Cys Cys Cys Phe Cys Cys

20

<210> 103

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 103

Gln Gly Gln Val Gln Cys Leu Gln Cys Ala Phe Cys Cys Tyr Lys Lys

1 5 10 15

Val Glu Leu Phe Cys Cys

20

<210> 104

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 104

Cys Cys Gln Val Cys His Leu Gln Cys Cys Ala Ala Cys Tyr Lys Lys

1 5 10 15

Cys Cys Leu Phe Pro Cys

20

<210> 105

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 105

Cys Cys Gln Cys Gln His Ala Gln Cys Ala Phe Cys Ala Cys Cys Cys

1 5 10 15

Cys Ala Cys Cys Cys Lys

20

<210> 106

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 106

Gln Gly Gln Val Gln His Leu Gln Ala Ala Phe Ser Gln Cys Cys Ala

1 5 10 15

Cys Glu Cys Phe Pro Lys

20

<210> 107

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 107

Gln Gly Ala Cys Gln Ala Leu Gln Ala Ala Phe Cys Gln Tyr Lys Lys

1 5 10 15

Val Cys Ala Phe Cys Lys

20

<210> 108

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 108

Gln Cys Cys Cys Gln His Cys Gln Ala Cys Cys Cys Cys Tyr Lys Lys

1 5 10 15

Cys Cys Cys Cys Pro Lys

20

<210> 109

<211> 22

<212> PRT

<213> artificial sequence

<220>

<223> peptide

<400> 109

Gln Gly Cys Val Cys His Leu Gln Ala Ala Cys Ser Gln Tyr Lys Lys

1 5 10 15

Val Glu Leu Phe Pro Cys

20

Claims

1. A peptide comprising a substitution of at least one amino acid of SEQ ID No. 1 with cysteine, wherein the peptide comprises at least 50% sequence homology with respect to SEQ ID No. 1.

2. The peptide according to claim 2, wherein at least one cysteine substitution occurs at any one or more of a glutamine amino acid position, a valine amino acid position, an alanine amino acid position, and a serine amino acid position.

3. The peptide of claim 1 or claim 2, wherein the peptide forms an alpha helix and at least one cysteine substitution is located in an outer region of the alpha helix.

4. A peptide according to any one of claims 1 to 3, wherein one cysteine substitution is in the region of SEQ ID No. 1 consisting of SEQ ID No. 2.

5. The peptide according to claim 4, wherein the one cysteine substitution in the region of SEQ ID NO. 1 consisting of SEQ ID NO. 2 is a V17C substitution relative to the amino acid sequence of SEQ ID NO. 1.

6. The peptide according to any one of claims 1 to 5, comprising a Q13C substitution relative to the amino acid sequence of SEQ ID No. 1.

7. The peptide according to claim 6, comprising an H6C substitution with respect to the amino acid sequence of SEQ ID NO. 1.

8. The peptide of any one of claims 1 or 3 to 5 comprising an H6C substitution relative to the amino acid sequence of SEQ ID No. 1.

9. The peptide according to any one of claims 1 to 8, comprising at least one additional cysteine substitution at any amino acid position.

10. The peptide according to claim 9, wherein the at least one additional cysteine substitution relative to SEQ ID No. 1 is ≡1 and ≡11 amino acids.

11. The peptide according to any one of claims 1 to 10, comprising a substitution of at least 3 amino acids of SEQ ID No. 1 with cysteine.

12. The peptide according to claim 11, wherein the at least one cysteine substitution with respect to SEQ ID No. 1 is ≡3 and ≡11 amino acids.

13. The peptide according to claim 12, comprising a substitution of at least 3 amino acids of SEQ ID No. 1 with cysteine, optionally wherein the cysteine substitution is not at the Q13C or H6C position of SEQ ID No. 1.

14. The peptide of any one of claims 1 to 13, further comprising one or more additional cysteines added to the C-terminus relative to SEQ ID No. 1, one or more additional cysteines added to the N-terminus relative to SEQ ID No. 1, or a combination thereof.

15. The peptide according to claim 1, comprising the amino acid sequence of any one of the following: SEQ ID NO 8, SEQ ID NOS 3-7 or SEQ ID NOS 9-109, or variants thereof having at least 70% sequence homology.

16. The peptide according to claim 1, consisting of the amino acid sequence of any one of SEQ ID NO. 8, SEQ ID NOS:3-7 or SEQ ID NOS: 9-109.

17. The peptide according to any one of claims 1 to 6 or 9 to 14, wherein the peptide is SEQ ID No. 8 or a variant having at least 70% sequence homology thereto.

18. The peptide according to claim 1, consisting of SEQ ID NO. 8.

19. The peptide according to any one of claims 1 to 18, wherein a plurality of said peptides contacted with hair, optionally damaged hair, under the same conditions increases hair strength to a greater extent than the same number of peptides of SEQ ID No. 1 contacted with hair.

20. The peptide according to any one of claims 1 to 19, wherein the peptide binds keratin.

21. The peptide according to claim 19, wherein the keratin-binding peptide is more wash resistant than a keratin-binding peptide consisting of SEQ ID No. 1.

22. A composition comprising a plurality of peptides according to any one of claims 1 to 21.

23. The composition of claim 22, wherein the composition is a liquid.

24. The composition of claim 22 or 23, comprising an effective amount of the peptide to improve one or more properties selected from the group consisting of hair strength, visual properties, tactile properties, or a combination thereof.

25. The composition of any one of claims 22 to 24, comprising about 0.01 wt% to about 0.1 wt% peptide.

26. The composition according to any one of claims 22 to 25, wherein the composition is selected from the group consisting of a shampoo, a conditioner, an oil, or a mask.

27. A method of treating hair, the method comprising: applying the composition of any one of claims 22 to 26 to hair.

28. The method of claim 27, wherein the step of applying occurs after the hair curling formulation, the hair straightening formulation, the hair coloring formulation, or the hair bleaching formulation is applied to the hair.

29. The method of any one of claims 27 to 28, wherein breakage of hair is reduced by at least about 5%, 10%, 20%, 30%, 40% or 50% as compared to when hair is not treated with the composition after the hair curling, hair straightening, hair dyeing or hair bleaching preparation is applied to the hair.

30. A kit comprising the composition of any one of claims 22 to 29.