A composition for protecting hair, repairing damaged hair, or strengthening hair
By using peptides and their derivatives with specific amino acid sequences to bind to hair, the problem of hair structure damage is solved, achieving the strengthening and protection of hair, especially eyebrows and eyelashes.
Patent Information
- Authority / Receiving Office
- CN · China
- Patent Type
- Patents(China)
- Current Assignee / Owner
- AMOREPACIFIC CORP
- Filing Date
- 2025-05-27
- Publication Date
- 2026-05-08
AI Technical Summary
Existing technologies are insufficient to effectively protect and strengthen hair, especially eyebrows and eyelashes, particularly due to structural damage and fragility caused by chemical treatments.
Peptides and their derivatives with specific amino acid sequences are used to fill gaps and strengthen hair structure by binding to the hair cuticle, cortex and cell membrane complex. This includes using tripeptides with amino acid sequences such as CKF, CWK or KCV and binding fatty acids or organic acids at the N-terminus to enhance binding force.
It significantly improves the tensile strength and elasticity of hair, repairs the CMC structure of damaged hair, improves the hardness and smoothness of hair, and enhances the protective and repair effects of hair.
Smart Images

Figure CN120478188B_ABST
Abstract
Description
[0001] Cross-reference to related applications
[0002] This application claims priority to Korean Patent Application No. 10-2024-0101975, filed July 31, 2024, the entire contents of which are incorporated herein by reference. This application also claims priority to Korean Patent Application No. 10-2024-0172277, filed November 27, 2024, the entire contents of which are incorporated herein by reference. Technical Field
[0003] This disclosure relates to a composition for protecting or strengthening hair and the corresponding use of said composition. Background Technology
[0004] For cosmetic purposes, chemical treatments such as perming and dyeing of hair are increasingly common, leading to non-specific damage to various structural proteins and lipids that make up hair. Eyebrows and eyelashes are shorter, thinner, and fewer in number than hair in other parts of the body (e.g., head hair), making them more vulnerable to physical and chemical stimuli, and resulting in greater cosmetic losses when damaged.
[0005] Hair (e.g., scalp, eyebrows, eyelashes) is mainly composed of the cuticle, cortex, cell membrane complex (CMC), and medulla. Physical stimuli primarily damage the cuticle, while chemical stimuli mainly cause the loss of CMC and cortex. Repeated exposure to these stimuli can lead to irreversible changes in hair (e.g., scalp, eyebrows, eyelashes), ultimately resulting in damage, breakage, and / or loss, or brittleness that prevents the formation of the desired aesthetic style. To restore the tensile strength of hair to its pre-damage level, methods exist for filling the gaps between the lost CMC and cortex with predetermined components and combining them to strengthen the hair's structural strength. However, traditional hair-care compositions containing organic acids and the like struggle to restore the CMC, which is composed of a lipid layer.
[0006] [Existing Technical Documents]
[0007] [Patent Documents]
[0008] Korean Patent No. 10-2084765 Summary of the Invention
[0009] Technical issues
[0010] One aspect of this disclosure is to provide a peptide or peptide derivative composed of substances present in the human body, thereby significantly reducing the risk of irritation while replenishing damaged components in hair (e.g., hair, eyebrows, eyelashes) and strengthening the strength and elasticity of hair (e.g., hair, eyebrows, eyelashes).
[0011] One aspect of this disclosure is to provide a peptide that has the effects of protecting hair, repairing damaged hair, or strengthening hair.
[0012] One aspect of this disclosure is to provide a peptide derivative that has the effects of protecting hair, repairing damaged hair, or strengthening hair.
[0013] One aspect of this disclosure is to provide a composition for protecting hair, repairing damaged hair, or strengthening hair.
[0014] Technical solution
[0015] According to one aspect of this disclosure, a peptide comprising one or more sequence units consisting of Xaa-Yaa-Zaa, wherein Xaa, Yaa, and Zaa are each independently selected from the group consisting of C (Cys; cysteine), K (Lys; lysine), W (Trp; tryptophan), V (Val; valine), L (Leu; leucine), and F (Phe; phenylalanine), and Xaa, Yaa, and Zaa are distinct from each other, wherein when Xaa and Yaa are C and K respectively, Zaa is not L.
[0016] According to one aspect of this disclosure, a peptide derivative may be a derivative in which a fatty acid or an organic acid is bound to the N-terminus of the peptide.
[0017] A hair protection, hair repair, or hair strengthening composition according to one aspect of this disclosure includes the peptides defined herein.
[0018] A hair protection, hair repair, or hair strengthening composition according to one aspect of this disclosure includes the peptide derivatives defined herein.
[0019] A hair protection, hair repair, or hair strengthening composition according to one aspect of this disclosure comprises a mixture of at least three amino acids selected from the group consisting of C, K, W, V, L (Leu; leucine) and F.
[0020] Invention Effects
[0021] The peptides, peptide derivatives, and / or compositions according to one aspect of this disclosure can improve the strength (or stiffness) and / or elasticity of hair (e.g., damaged hair). The peptides, peptide derivatives, and / or compositions according to one aspect of this disclosure can bind to the hair cuticle, cortex, and / or CMC of hair (e.g., damaged hair), thereby improving hair strength, such as tensile strength.
[0022] According to one aspect of the present disclosure, peptides, peptide derivatives and / or compositions can repair damage to the CMC structure in damaged hair, ultimately repairing the hair, for example, improving the hardness, smoothness and elasticity of damaged hair. Attached Figure Description
[0023] Figure 1 The conditions for calculating the binding energy of a three-dimensional peptide molecule file and keratin using the CDocker module of Discovery Studio software (DASSAULT Systems) are shown.
[0024] Figure 2 The changes in tensile strength of hair treated with an amino acid mixture are shown.
[0025] Figure 3 The denaturation enthalpy change of hair treated with a mixture of amino acids, tripeptides, and tripeptides with fatty acids bound to their N-terminus is shown.
[0026] Figure 4 The changes in tensile strength of hair treated with tripeptides are shown.
[0027] Figure 5 The changes in tensile strength of hair treated with tripeptides, amino acid mixtures, and tripeptides with fatty acid-bound N-terminus are shown.
[0028] Figure 6 These are confocal micrographs showing the morphology of fluorescently labeled palmitoyl tripeptide (a tripeptide with an N-terminus bound to a fatty acid; left image) and lipid-soluble fluorescent material (right image) penetrating into and binding to hair.
[0029] Figure 7 These are confocal microscope images showing the morphology of water-soluble fluorescent substances penetrating into and binding to hair.
[0030] Figure 8 This is a confirmation of the binding affinity of oligopeptides with repeating or combining tripeptide sequences to hair.
[0031] Figure 9 The changes in tensile strength of eyebrows treated with tripeptides and tripeptides with fatty acids bound to their N-terminus are shown.
[0032] Figure 10 This diagram illustrates the step-by-step method for measuring eyebrow elasticity.
[0033] Figure 11 This demonstrates hair elasticity treated with tripeptides and tripeptides with fatty acids bound to their N-terminus. Detailed Implementation
[0034] The various embodiments and terminology used in this application are not intended to limit the technical features described in this application to specific embodiments, but should be understood to include various modifications, equivalents or alternatives to the embodiments.
[0035] The inventors have developed a substance that can bind to the cuticle, CMC (cell membrane complex), and / or cortex of damaged hair (e.g., hair, eyebrows, eyelashes) to fill gaps, strengthen the structural strength of the hair, and / or demonstrate the repair effect of damaged hair (e.g., hair, eyebrows, eyelashes).
[0036] In one embodiment, the inventors screened peptides comprising amino acid sequences that exhibited excellent binding affinity to structural proteins (KRT 33B, KRT 85, KAP 3-1) found in damaged hair. Based on the top-ranking amino acid sequences among the screened peptide sequences, i) tripeptides and ii) tripeptides with N-terminal covalently bound fatty acids were synthesized, and their ability to enhance the tensile strength and structural strength of hair (e.g., hair, eyebrows, eyelashes) was confirmed. Furthermore, a mixture was prepared by combining iii) amino acids constituting the top-ranking tripeptide sequences among the screened peptide sequences, and the amino acid mixture was confirmed to enhance the tensile strength and structural strength of hair (e.g., hair, eyebrows, eyelashes).
[0037] Terminology Definition
[0038] In this disclosure, Xaa, Yaa, and Zaa represent amino acids, respectively.
[0039] In this disclosure, C or Cys represents cysteine, K or Lys represents lysine, W or Trp represents tryptophan, V or Val represents valine, L or Leu represents leucine, and F or Phe represents phenylalanine.
[0040] In this disclosure, the amino acid sequence of the peptide is written from left to right, in the order from the N-terminus to the C-terminus. Conversely, the direction of peptide synthesis is opposite to the direction of peptide sequence reading, starting from the C-terminus and proceeding to the N-terminus. The direction of peptide sequence writing / reading and the direction of peptide sequence synthesis are obvious facts in the art.
[0041] In this disclosure, the term "strengthening hair" generally includes increasing the strength of hair, such as preferably increasing the tensile strength of hair and / or increasing the denaturation enthalpy of hair. In this disclosure, strengthening hair can include increasing the strength of undamaged hair or damaged hair. Damaged hair may be caused by heat or chemical treatments (e.g., dyeing, perming, bleaching). Damaged hair may be caused by heat or chemical treatments (e.g., dyeing, perming, bleaching) that damage the main structural components of hair. In one embodiment, the hair strengthening composition can be a composition for increasing hair strength and / or elasticity.
[0042] In this disclosure, the term "protecting hair" generally includes, but is not limited to, inhibiting hair damage. In this disclosure, protecting hair preferably includes preventing damage to undamaged hair; or preventing further damage to damaged hair, but is not limited to.
[0043] In this disclosure, the term "hair" refers to all hair growing on an individual (e.g., including mammals). For example, in this disclosure, hair may include, but is not limited to, at least one selected from the group consisting of head hair, eyebrows, eyelashes, and body hair (e.g., chest hair, leg hair). Other types of hair present in different locations than head hair (e.g., eyebrows, eyelashes) do not differ significantly in structure and composition from head hair (Qianqian Su, Cheng Zhou, Congfen He, Qian Jiao, Zidi Wang, Yan Jia. Research Progress in Composition, Classification and Influencing Factors of Hair. Asian J Beauty Cosmetol 2023; 21(3):503-516.). Furthermore, although the size or shape of hair follicles in the body may differ, their basic structure is the same (Jennifer V. Nguyen MD. The Biology, Structure, and Function of Eyebrow Hair. J Drugs Dermatol. 2014; 13(suppl1):s12-s16.). Therefore, the effects of peptides or peptide derivatives on hair can essentially be the same on hair in other parts of the body (e.g., eyebrows and / or eyelashes).
[0044] In this disclosure, the term "C8 to C30 fatty acids" refers to fatty acids having 8 to 30 carbon atoms. The term "Cn1 (integer) to Cn2 (integer) fatty acids" refers to fatty acids having n1 (integer) to n2 (integer) carbon atoms. According to the invention, the term "fatty acid" includes saturated or unsaturated fatty acids.
[0045] In this disclosure, the term "peptide derivative" refers to a peptide in which one or more amino acids of the defined parent peptide are chemically modified, or a peptide in which the defined parent peptide is modified by adding amino acids. For example, in this disclosure, a peptide derivative may be a peptide in which any component (e.g., compound, fatty acid, organic acid, etc., such as C1 to C30 fatty acids, preferably C15 to C20 fatty acids) is attached to the N-terminus or C-terminus of the defined peptide.
[0046] Peptides or peptide derivatives that have the effect of protecting hair, repairing damaged hair, or strengthening hair.
[0047] In one aspect, this disclosure provides a peptide comprising one or more sequence units consisting of Xaa-Yaa-Zaa:
[0048] Xaa, Yaa, and Zaa are each independently selected from groups formed by C (Cys, cysteine), K (Lys, lysine), W (Trp, tryptophan), V (Val, valine), L (Leu, leucine), and F (Phe, phenylalanine).
[0049] Xaa, Yaa, and Zaa are all different from each other. When Xaa and Yaa are C and K respectively, Zaa is not L.
[0050] In one implementation example, two of Xaa, Yaa, and Zaa can be C and K respectively, where Zaa is not L when Xaa and Yaa are C and K respectively.
[0051] In one implementation example, two of Xaa, Yaa, and Zaa can be C and K respectively, and the remaining one can be chosen from the group consisting of W, V, and F.
[0052] In one implementation, the peptide may be a tripeptide consisting of a sequence unit of Xaa-Yaa-Zaa.
[0053] In one embodiment, the peptide is a tripeptide selected from the group consisting of CKF, CWK, or KCV.
[0054] In one implementation, the peptide may be an oligopeptide composed of multiple Xaa-Yaa-Zaa sequence units. In this case, the multiple Xaa-Yaa-Zaa sequence units may be all identical, partially identical, or different.
[0055] In one implementation, the peptide may be an oligopeptide composed of 2 to 10 Xaa-Yaa-Zaa sequence units, but is not limited thereto. For example, the peptide may be an oligopeptide composed of 2, 3, 4, 5, 6, 7, 8, 9, or 10 Xaa-Yaa-Zaa sequence units, but is not limited thereto.
[0056] In one implementation, the peptide may be an oligopeptide consisting of 2 to 5, preferably 2 to 4 Xaa-Yaa-Zaa sequence units.
[0057] In one implementation example, the oligopeptide can be a peptide containing 3 to 30 amino acids, but is not limited thereto. For example, the oligopeptide can contain 3 or more, 4 or more, 5 or more, 6 or more, 7 or more, 8 or more, 9 or more, 10 or more, 11 or more, 12 or more, 13 or more, 14 or more, 15 or more, 16 or more, 17 or more, 18 or more, 19 or more, 20 or more, 21 or more, 22 or more, 23 or more, 24 or more, 25 or more, 26 or more, 27 or more, 28 or more, 29 or more, 30 or more, less than 3, less than 4, or 5 amino acids. Peptides containing less than 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more amino acids, or combinations thereof (e.g., 3 to 24, 3 to 15, 3 to 12).
[0058] In one implementation, the peptide may be an oligopeptide composed of 2 to 5, preferably 2 to 4 Xaa-Yaa-Zaa sequence units, and the sequence units constituting the oligopeptide may be all identical, partially identical, or all different.
[0059] In one embodiment, the peptide may be an oligopeptide composed of 2 to 5, preferably 2 to 4 Xaa-Yaa-Zaa sequence units, wherein all sequence units constituting the oligopeptide may be identical. In another embodiment, the peptide may be an oligopeptide composed of 2 to 5, preferably 2 to 4 Xaa-Yaa-Zaa sequence units, wherein at least one sequence unit constituting the oligopeptide may be identical. In another embodiment, the peptide may be an oligopeptide composed of 2 to 5, preferably 2 to 4 Xaa-Yaa-Zaa sequence units, wherein some sequence units constituting the oligopeptide may be identical. In yet another embodiment, the peptide may be an oligopeptide composed of 2 to 5, preferably 2 to 4 Xaa-Yaa-Zaa sequence units, wherein all sequence units constituting the oligopeptide are different.
[0060] In one embodiment, the peptide is an oligopeptide with the amino acid sequence CKFCKF (SEQ ID NO: 1), CKFCKFCKF (SEQ ID NO: 2), CKFCKFCKFCKF (SEQ ID NO: 3), CWKCWK (SEQ ID NO: 4), CWKCWKCWK (SEQ ID NO: 5), CWKCWKCWKCWK (SEQ ID NO: 6), KCVKCV (SEQ ID NO: 7), KCVKCVKCV (SEQ ID NO: 8), KCVKCVKCVKCV (SEQ ID NO: 9), CWKCWKKCLKCLKCV (SEQ ID NO: 18), CKWCWKKCLKCVKCL (SEQ ID NO: 19), CKWKCFCKFCWKKCV (SEQ ID NO: 20), KCFKCFCKWCKFKCV (SEQ ID NO: 21), or CKFCKWKCFKCVKCF (SEQ ID NO: 22).
[0061] According to one embodiment, a peptide (e.g., tripeptide or oligopeptide) has the effect of protecting hair, repairing damaged hair, or strengthening hair. In particular, tripeptides are easy to synthesize due to their short sequence length, and further, provide time and cost advantages.
[0062] Furthermore, in one aspect of this disclosure, a peptide derivative having a fatty acid or organic acid bound to the N-terminus of the aforementioned peptide or oligopeptide is provided.
[0063] In this disclosure, peptide derivatives with an N-terminus bound to a fatty acid or organic acid can be N-terminal acylated peptides. The N-terminus acylation of a peptide can be derived from a fatty acid or organic acid. In this disclosure, peptide derivatives with an N-terminus bound to a fatty acid or organic acid can be acyl derivatives of N-terminal acylated peptides.
[0064] In this disclosure, the term "N-terminus of a peptide (or oligopeptide) is bound to a fatty acid or an organic acid" can refer to the N-terminus of a peptide (or oligopeptide) having an acyl group derived from a fatty acid or an organic acid.
[0065] For example, the N-terminus of a peptide (or oligopeptide) being bound to a fatty acid can mean that the N-terminus of the peptide (or oligopeptide) is bound to an acyl group derived from a fatty acid. Similarly, the N-terminus of a peptide (or oligopeptide) being bound to an organic acid can mean that the N-terminus of the peptide (or oligopeptide) is bound to an acyl group derived from an organic acid.
[0066] That is, in one aspect of this disclosure, a peptide derivative is provided in which a fatty acid or organic acid is bound to the N-terminus of a peptide comprising one or more sequence units consisting of Xaa-Yaa-Zaa: wherein Xaa, Yaa and Zaa are each independently selected from the group consisting of C, K, W, V, L and F, and wherein Xaa, Yaa and Zaa are different from each other, wherein when Xaa and Yaa are C and K respectively, Zaa may not be L.
[0067] Xaa, Yaa, Zaa, sequence units, and peptides are the same as described above, so specific details are omitted.
[0068] The “binding” of the fatty acid or organic acid in the N-terminus can be covalent.
[0069] In one implementation, the fatty acid may be a C2 to C80 fatty acid.
[0070] In one embodiment, the fatty acid can be a C8 to C30 fatty acid, but is not limited thereto. For example, the fatty acid can be a C8 fatty acid, a C9 fatty acid, a C10 fatty acid, a C11 fatty acid, a C12 fatty acid, a C13 fatty acid, a C14 fatty acid, a C15 fatty acid, a C16 fatty acid, a C17 fatty acid, a C18 fatty acid, a C19 fatty acid, a C20 fatty acid, a C21 fatty acid, a C22 fatty acid, a C23 fatty acid, a C24 fatty acid, a C25 fatty acid, a C26 fatty acid, a C27 fatty acid, a C28 fatty acid, a C29 fatty acid, or a C30 fatty acid, but is not limited thereto. For example, the fatty acid can be a C8 to C30 fatty acid, a C9 to C29 fatty acid, a C9 to C28 fatty acid, a C9 to C27 fatty acid, a C9 to C26 fatty acid, a C9 to C25 fatty acid, a C9 to C24 fatty acid, a C10 to C24 fatty acid, a C9 to C23 fatty acid, a C10 to C22 fatty acid, a C11 to C21 fatty acid, a C12 to C20 fatty acid, a C13 to C19 fatty acid, a C14 to C18 fatty acid, a C15 to C20 fatty acid, or a C15 to C17 fatty acid, but is not limited thereto. In a preferred embodiment, the fatty acid can be a C15 to C20 fatty acid, preferably a C15 to C17 fatty acid.
[0071] In one embodiment, the acyl group derived from the fatty acid can be an acyl group derived from fatty acids of C8 to C30, but is not limited thereto. For example, the acyl group derived from the fatty acid can be an acyl group derived from fatty acids of C8, C9, C10, C11, C12, C13, C14, C15, C16, C17, C18, C19, C20, C21, C22, C23, C24, C25, C26, C27, C28, C29, or C30, but is not limited thereto. For example, the acyl group derived from the fatty acid can be an acyl group derived from fatty acids of C8 to C30, C9 to C29, C9 to C28, C9 to C27, C9 to C26, C9 to C25, C9 to C24, C10 to C24, C9 to C23, C10 to C22, C11 to C21, C12 to C20, C13 to C19, C14 to C18, C15 to C20, or C15 to C17, but is not limited thereto. In a preferred embodiment, the acyl group derived from the fatty acid can be an acyl group derived from fatty acids of C15 to C20, preferably an acyl group derived from fatty acids of C15 to C17.
[0072] Generally, according to the present invention, the fatty acid can be a saturated or unsaturated fatty acid.
[0073] Typically, according to the present invention, the acyl group derived from the fatty acid can be saturated or unsaturated.
[0074] In one embodiment, the fatty acid may be unsubstituted or substituted. For example, the fatty acid may be unsubstituted or substituted with at least one substituent selected from the group consisting of alkyl, alkoxy, aryl, hydroxyl, amino, amide, sulfate and sulfide, but is not limited thereto. Preferably, it may be substituted with at least one substituent selected from the group consisting of alkyl, alkoxy, hydroxyl and amino.
[0075] In one embodiment, the acyl group derived from the fatty acid may be unsubstituted or substituted. For example, the acyl group derived from the fatty acid may be unsubstituted or substituted with at least one substituent selected from the group consisting of alkyl, alkoxy, aryl, hydroxyl, amino, amide, sulfate and sulfide, but is not limited thereto. Preferably, it may be substituted with at least one substituent selected from the group consisting of alkyl, alkoxy, hydroxyl and amino.
[0076] In one embodiment, the fatty acid may be at least one selected from the group consisting of caprylic acid (C8:0), capric acid (C10:0), lauric acid (C12:0), myristic acid (C14:0), palmitic acid (C16:0), stearic acid (C18:0), arachidic acid (C20:0), behenic acid (C22:0), ceramide (C24:0), ceramide (C26:0), myristenoic acid (C14:1), palmitoleic acid (C16:1), oleic acid (C18:1), and eicosenoic acid (C20:1), but is not limited thereto. In a preferred embodiment, the fatty acid may be at least one selected from the group consisting of palmitic acid, stearic acid, and arachidic acid. In a preferred embodiment, the fatty acid may be at least one selected from the group consisting of palmitoleic acid, oleic acid, and eicosenoic acid.
[0077] In one embodiment, the acyl group derived from the fatty acid may be selected from capryloyl group (C8:0), decanoyl group (C10:0), lauroyl group (C12:0), myristoyl group (C14:0), palmitoyl group (C16:0), stearoyl group (C18:0), arachidoyl group (C20:0), behenoyl group (C22:0), lignocaroyl group (C24:0), cerotoyl group (C26:0), myristoleoyl group (C14:1), and palmitoleoyl group. The acyl group is selected from at least one of the group consisting of oleoyl group (C16:1), oleoyl group (C18:1), and eicosenoyl group (C20:1), but is not limited thereto. In a preferred embodiment, the acyl group derived from the fatty acid may be at least one selected from the group consisting of palmitoyl, stearoyl, and arachidoyl. In a preferred embodiment, the acyl group derived from the fatty acid may be at least one selected from the group consisting of palmitoleoyl, oleoyl, and eicosenoyl.
[0078] In one implementation, the organic acid may be a saturated or unsaturated organic acid.
[0079] In one implementation, the acyl group derived from the organic acid can be saturated or unsaturated.
[0080] According to the present invention, the organic acid may be unsubstituted or substituted. For example, the organic acid may be unsubstituted or substituted with at least one substituent selected from the group consisting of alkyl, alkoxy, aryl, hydroxyl, amino, amide, sulfate and sulfide, but is not limited thereto. Preferably, it may be substituted with at least one substituent selected from the group consisting of alkyl, alkoxy, hydroxyl and amino.
[0081] According to the present invention, the acyl group derived from the organic acid may be unsubstituted or substituted. For example, the acyl group derived from the organic acid may be unsubstituted or substituted with at least one substituent selected from the group consisting of alkyl, alkoxy, aryl, hydroxyl, amino, amide, sulfate and sulfide, but is not limited thereto. Preferably, it may be substituted with at least one substituent selected from the group consisting of alkyl, alkoxy, hydroxyl and amino.
[0082] In one embodiment, the organic acid may be selected from at least one of the group consisting of acetic acid, citric acid, formic acid, trifluoroacetic acid, succinic acid, gallic acid, and lactic acid, but is not limited thereto.
[0083] In one embodiment, the acyl group derived from the organic acid may be selected from at least one of the group consisting of acetyl, citrl, formyl, trifluoroacetyl, succinyl, galloyl, and lactyl, but is not limited thereto.
[0084] In one embodiment, the peptide derivative may be a tripeptide consisting of a single Xaa-Yaa-Zaa sequence unit, with the N-terminus bound to a fatty acid or organic acid. In another embodiment, the peptide derivative may be a tripeptide consisting of a single Xaa-Yaa-Zaa sequence unit, with the N-terminus bound to an acyl group derived from a fatty acid or organic acid.
[0085] In one embodiment, the peptide derivative may be an oligopeptide composed of 2 to 5, preferably 2 to 4 Xaa-Yaa-Zaa sequence units, with the N-terminus bound to a fatty acid or organic acid. In this case, the sequence units constituting the oligopeptide may be all identical. In another embodiment, the peptide derivative may be an oligopeptide composed of 2 to 5, preferably 2 to 4 Xaa-Yaa-Zaa sequence units, with the N-terminus bound to an acyl group derived from a fatty acid or organic acid. In this case, the sequence units constituting the oligopeptide may be all identical.
[0086] In one embodiment, the peptide derivative may be an oligopeptide composed of 2 to 5, preferably 2 to 4 Xaa-Yaa-Zaa sequence units, with its N-terminus bound to a fatty acid or organic acid. In this case, the sequence units constituting the oligopeptide may be partially identical. In another embodiment, the peptide derivative may be an oligopeptide composed of 2 to 5, preferably 2 to 4 Xaa-Yaa-Zaa sequence units, with its N-terminus bound to an acyl group derived from a fatty acid or organic acid. In this case, the sequence units constituting the oligopeptide may be partially identical.
[0087] In one embodiment, the peptide derivative may be an oligopeptide composed of 2 to 5, preferably 2 to 4 Xaa-Yaa-Zaa sequence units, with the N-terminus bound to a fatty acid or organic acid. In this case, the sequence units constituting the oligopeptide may be completely different. In another embodiment, the peptide derivative may be an oligopeptide composed of 2 to 5, preferably 2 to 4 Xaa-Yaa-Zaa sequence units, with the N-terminus bound to an acyl group derived from a fatty acid or organic acid. In this case, the sequence units constituting the oligopeptide may be completely different.
[0088] In one embodiment, the peptide derivative can be an amino acid sequence of CWK, CKF, or KCV with a fatty acid or organic acid attached to its N-terminus. In another embodiment, the peptide derivative can be an amino acid sequence of CWK, CKF, or KCV with an acyl group derived from a fatty acid or organic acid attached to its N-terminus. In one embodiment, the peptide derivative can be an amino acid sequence of CWK, CKF, or KCV with a palmitic acid attached to its N-terminus. In one embodiment, the peptide derivative can be an amino acid sequence of CWK, CKF, or KCV with a palmitic acid attached to its N-terminus. In one embodiment, the peptide derivative can be palmitoyl-CWK, palmitoyl-CKF, or palmitoyl-KCV. In one embodiment, the peptide derivative can be a CWK, CKF, or KCV with a palmitoyl group attached to its N-terminus.
[0089] According to one embodiment, by binding the N-terminus of a peptide to a fatty acid or organic acid, the penetration of the peptide into hair (e.g., hair, eyebrows, eyelashes) can be improved, further enhancing the binding force between the peptide and hair (e.g., hair, eyebrows, eyelashes).
[0090] In one embodiment, the peptide or peptide derivative according to one aspect of the present disclosure can bind to (or adsorb onto) at least one of the group consisting of the hair cuticle, hair cortex, and CMC layer of hair (e.g., scalp, eyebrows, eyelashes). In one embodiment, the peptide or peptide derivative according to one aspect of the present disclosure can bind to (or adsorb onto) structural proteins found in damaged hair (e.g., scalp, eyebrows, eyelashes).
[0091] In one implementation, the peptide or peptide derivative according to one aspect of this disclosure can improve the tensile strength of hair (e.g., hair, eyebrows, eyelashes).
[0092] In one implementation, the peptide or peptide derivative according to one aspect of this disclosure can increase the denaturation enthalpy of hair (e.g., head hair, eyebrows, eyelashes). A high denaturation enthalpy of hair indicates high hair strength.
[0093] In one embodiment, the peptide or peptide derivative according to one aspect of the present disclosure can bind (or adsorb) to the hair cuticle, hair cortex and / or cell membrane complex layer of hair (e.g., hair, eyebrows, eyelashes), thereby improving the smoothness and elasticity of the surface.
[0094] In one embodiment, the peptide or peptide derivative according to one aspect of this disclosure can repair damage to the CMC structure in damaged hair (e.g., hair, eyebrows, eyelashes), ultimately improving the hardness, smoothness, and elasticity of the damaged hair (e.g., hair, eyebrows, eyelashes).
[0095] Compositions for protecting, repairing, or strengthening hair
[0096] In one aspect of this disclosure, a composition comprising the aforementioned peptides, peptide derivatives, or amino acids is provided for protecting hair, repairing damaged hair, or strengthening hair.
[0097] In one embodiment, the hair protection, hair repair, or hair strengthening composition according to one aspect of the present disclosure can bind (or adsorb) onto at least one of the group consisting of the hair cuticle, hair cortex, and CMC layer of hair. In one embodiment, the hair protection, hair repair, or hair strengthening composition according to one aspect of the present disclosure can bind (or adsorb) onto structural proteins found in damaged hair.
[0098] In one embodiment, the hair protection, hair repair, or hair strengthening composition according to one aspect of the present disclosure can improve the tensile strength of hair.
[0099] In one embodiment, the hair protection, hair repair, or hair strengthening composition according to one aspect of the present disclosure can increase the denaturation enthalpy of hair.
[0100] In one embodiment, the hair protection, hair repair, or hair strengthening composition according to one aspect of the present disclosure can bind (or adsorb) to the hair cuticle, cortex, and / or cell membrane complex layer of the hair, thereby improving the smoothness and elasticity of the surface.
[0101] In one embodiment, the hair protection, hair repair, or hair strengthening composition according to one aspect of the present disclosure can repair the damage to the CMC structure in damaged hair, and ultimately improve the hardness, smoothness, and elasticity of the damaged hair.
[0102] In one embodiment, the hair protection, hair repair, or hair strengthening composition according to one aspect of the present disclosure can be a hair protection, hair repair, or hair strengthening composition.
[0103] In one embodiment, the hair protection, hair repair, or hair strengthening composition according to one aspect of the present disclosure can be a hair protection, eyebrow repair, or eyebrow strengthening composition.
[0104] In one embodiment, the hair protection, hair repair, or hair strengthening composition according to one aspect of the present disclosure can be a hair protection, eyelash repair, or eyelash strengthening composition.
[0105] 1) Compositions for protecting, repairing damaged hair, or strengthening hair - 1
[0106] In one aspect of this disclosure, a composition comprising the aforementioned peptides or peptide derivatives is provided for protecting hair, repairing damaged hair, or strengthening hair.
[0107] Peptides and peptide derivatives are the same as described above, so specific details are omitted.
[0108] In one embodiment, the peptide or peptide derivative may contain from 0.0001% by weight to less than 100% by weight relative to the total weight of the composition, but is not limited thereto. For example, the peptide or peptide derivative may contain more than 0.0001% by weight, more than 0.001% by weight, more than 0.005% by weight, more than 0.01% by weight, more than 0.05% by weight, more than 0.1% by weight, more than 0.5% by weight, more than 1% by weight, more than 5% by weight, more than 10% by weight, more than 15% by weight, more than 20% by weight, more than 25% by weight, more than 30% by weight, more than 35% by weight, more than 40% by weight, more than 45% by weight, more than 50% by weight, more than 55% by weight, more than 60% by weight, more than 65% by weight, more than 70% by weight, more than 75% by weight, more than 80% by weight, more than 85% by weight, more than 90% by weight, more than 95% by weight, more than 99% by weight, more than 100% by weight, or more than 0.0001% by weight, relative to the total weight of the composition. Less than 0.001 wt%, less than 0.005 wt%, less than 0.01 wt%, less than 0.05 wt%, less than 0.1 wt%, less than 0.5 wt%, less than 1 wt%, less than 5 wt%, less than 10 wt%, less than 15 wt%, less than 20 wt%, less than 25 wt%, less than 30 wt%, less than 35 wt%, less than 40 wt%, less than 45 wt%, less than 50 wt%, less than 55 wt%, less than 60 wt%, less than 65 wt%, less than 70 wt%, less than 75 wt%, less than 80 wt%, less than 85 wt%, less than 90 wt%, less than 95 wt%, less than 99 wt%, less than 100 wt%, or combinations thereof (e.g., 0.005 to 0.05 wt%, 0.05 to 0.5 wt%), but not limited thereto.
[0109] In a preferred embodiment, the peptide or peptide derivative may contain 50% or more, 60% or more, 70% or more, 80% or more, 90% or more, 95% or more, 99% or more, or 100% by weight relative to the total weight of the composition. The peptide or oligopeptide or its derivative is composed of 2 to 5, preferably 2 to 4 Xaa-Yaa-Zaa sequence units. Preferably, two of Xaa, Yaa, and Zaa can be C and K, respectively. When Xaa and Yaa are C and K, Zaa may not be L. More preferably, two of Xaa, Yaa, and Zaa can be C and K, and the remaining one can be selected from the group consisting of W, V, and F. More preferably, the peptide is a tripeptide composed of a single sequence unit, wherein the peptide is CKF, CWK, or KCV.
[0110] In a preferred embodiment, the peptide present in the mentioned amount is an oligopeptide CKFCKF (SEQ ID NO: 1), CKFCKFCKF (SEQ ID NO: 2), CKFCKFCKFCKF (SEQ ID NO: 3), CWKCWK (SEQ ID NO: 4), CWKCWKCWK (SEQ ID NO: 5), CWKCWKCWKCWK (SEQ ID NO: 6), KCVKCV (SEQ ID NO: 7), KCVKCVKCV (SEQ ID NO: 8), KCVKCVKCVKCV (SEQ ID NO: 9), CWKCWKKCLKCLKCV (SEQ ID NO: 18), CKWCWKKCLKCVKCL (SEQ ID NO: 19), CKWKCFCKFCWKKCV (SEQ ID NO: 20), KCFKCFCKWCKFKCV (SEQ ID NO: 21), or CKFCKWKCFKCVKCF (SEQ ID NO: 22). Preferably, the peptide derivative having a fatty acid bound to the N-terminus of the disclosed peptide is a peptide derivative having a C8 to C30 fatty acid, a C9 to C29 fatty acid, a C9 to C28 fatty acid, a C9 to C27 fatty acid, a C9 to C26 fatty acid, a C9 to C25 fatty acid, a C9 to C24 fatty acid, a C10 to C24 fatty acid, a C9 to C23 fatty acid, a C10 to C22 fatty acid, a C11 to C21 fatty acid, a C12 to C20 fatty acid, a C13 to C19 fatty acid, a C14 to C18 fatty acid, a C15 to C20 fatty acid, or a C15 to C17 fatty acid, wherein, more preferably, it is a C15 to C20 fatty acid, further preferably, it is a C15 to C17 fatty acid, and most preferably, it is a peptide derivative of palmitic acid and / or palmitoleic acid.
[0111] Preferably, the disclosed peptide derivative with a fatty acid bound to its N-terminus is a peptide derivative having an acyl group derived from a fatty acid of C8 to C30, C9 to C29, C9 to C28, C9 to C27, C9 to C26, C9 to C25, C9 to C24, C10 to C24, C9 to C23, C10 to C22, C11 to C21, C12 to C20, C13 to C19, C14 to C18, C15 to C20, or C15 to C17, more preferably an acyl group derived from a fatty acid of C15 to C20, further preferably an acyl group derived from a fatty acid of C15 to C17, and most preferably a peptide derivative with an acyl group derived from palmitic acid and / or palmitoleic acid.
[0112] In one implementation, the peptide or peptide derivative may be applied to the subject's hair in an amount of 0.1 to 100 mg per 1g of hair, but is not limited thereto. For example, the peptide or peptide derivative may be applied to the subject's hair in amounts of more than 0.1 mg, more than 1 mg, more than 2 mg, more than 3 mg, more than 4 mg, more than 5 mg, more than 6 mg, more than 7 mg, more than 8 mg, more than 9 mg, more than 10 mg, less than 11 mg, less than 12 mg, less than 13 mg, less than 14 mg, less than 15 mg, less than 16 mg, less than 17 mg, less than 18 mg, less than 19 mg, less than 20 mg, less than 30 mg, less than 40 mg, less than 50 mg, less than 60 mg, less than 70 mg, less than 80 mg, less than 90 mg, less than 100 mg, or combinations thereof (e.g., 1 to 20 mg, 9 to 11 mg), but is not limited thereto.
[0113] In a preferred embodiment, the peptide or peptide derivative may be applied to the subject's hair in an amount of 5 to 20 mg or 9 to 15 mg.
[0114] In one implementation, the peptide or peptide derivative may be administered to the subject once or multiple times, but is not limited thereto.
[0115] In one embodiment, the peptide or peptide derivative may be used in combination with any other ingredient that can have the effects of protecting hair, repairing damaged hair, or strengthening hair, but is not limited thereto.
[0116] In one embodiment, the composition for protecting, repairing, or strengthening hair can be a cosmetic composition, an oral composition, a non-therapeutic composition, a non-therapeutic oral composition, a pharmaceutical composition, or a topical composition. For example, the composition can be a cosmetic composition. For example, the topical composition can be a skin topical composition or a hair topical composition.
[0117] In one embodiment, the hair protection, hair repair, or hair strengthening composition may be formulated as at least one of the following groups: shampoo, conditioner, hair cream, hair oil, hair lotion, hair mask, hair nourishing liquid, hair spray, hair treatment, serum, hair essence, hair gel, hair wax, hair essence, hair spray, eyebrow nourishing agent, eyebrow essence, eyelash nourishing agent, and eyelash essence, but is not limited thereto.
[0118] In one embodiment, the hair protection, hair repair, or hair strengthening composition may be a wash-off type (rinsing formulation, such as shampoo) or a leave-in type (non-rinsing formulation, such as hair serum), but is not limited thereto.
[0119] The hair protection, hair repair, or hair strengthening composition according to one aspect of this disclosure may also include ingredients that can be included in cosmetics.
[0120] The hair protection, repair, or strengthening composition according to one aspect of this disclosure may further include additives such as preservatives, thickeners, viscosity modifiers, stabilizers, pearlescent agents, metal ion blocking agents, cationic surfactants, pH adjusters, fragrances, and dyes, which are readily available for commercial use.
[0121] In one implementation example, hair may include, but is not limited to, hair, eyebrows, and / or eyelashes.
[0122] 2) Compositions for protecting, repairing damaged hair, or strengthening hair - 2
[0123] Furthermore, in one aspect of this disclosure, a composition is provided that comprises at least three amino acids selected from the group consisting of C, K, W, V, L (Leu, leucine) and F, for protecting hair, repairing damaged hair, or strengthening hair.
[0124] Regarding the use of the composition (cosmetic, pharmaceutical or topical composition) or dosage form and the additives that may be added to the composition, the details are the same as those in “1) Composition for protecting hair, repairing damaged hair or strengthening hair – 1” above, so specific details are omitted.
[0125] A composition comprising at least three amino acids according to one aspect of this disclosure can achieve hair protection, damaged hair repair, or hair strengthening effects without the need for peptide synthesis. Therefore, using the composition comprising at least three amino acids according to one aspect of this disclosure in protecting, repairing, or strengthening hair has economic advantages.
[0126] In one embodiment, the at least three amino acids may be present in an amount ranging from 0.0001% by weight to less than 100% by weight relative to the total weight of the composition, but are not limited thereto. For example, the at least three amino acids may contain more than 0.0001% by weight, more than 0.001% by weight, more than 0.005% by weight, more than 0.01% by weight, more than 0.05% by weight, more than 0.1% by weight, more than 0.5% by weight, more than 1% by weight, more than 5% by weight, more than 10% by weight, more than 15% by weight, more than 20% by weight, more than 25% by weight, more than 30% by weight, more than 35% by weight, more than 40% by weight, more than 45% by weight, more than 50% by weight, more than 55% by weight, more than 60% by weight, more than 65% by weight, more than 70% by weight, more than 75% by weight, more than 80% by weight, more than 85% by weight, more than 90% by weight, more than 95% by weight, more than 99% by weight, more than 100% by weight, or more than 0.0001% by weight, relative to the total weight of the composition. Less than 0.001 wt%, less than 0.005 wt%, less than 0.01 wt%, less than 0.05 wt%, less than 0.1 wt%, less than 0.5 wt%, less than 1 wt%, less than 5 wt%, less than 10 wt%, less than 15 wt%, less than 20 wt%, less than 25 wt%, less than 30 wt%, less than 35 wt%, less than 40 wt%, less than 45 wt%, less than 50 wt%, less than 55 wt%, less than 60 wt%, less than 65 wt%, less than 70 wt%, less than 75 wt%, less than 80 wt%, less than 85 wt%, less than 90 wt%, less than 95 wt%, less than 99 wt%, less than 100 wt%, or combinations thereof (e.g., 0.005 to 0.05 wt%, 0.05 to 0.5 wt%), but not limited thereto.
[0127] In a preferred embodiment, at least three amino acids may be present in amounts of 0.005 to 0.5% by weight or 0.05 to 0.5% by weight.
[0128] In one implementation, the composition may include one of C, K, and W, V, L, or F.
[0129] In one embodiment, the composition may consist of C; K; and one of W, V, L, or F. In one embodiment, the composition includes C, K, and W.
[0130] A composition comprising at least three amino acids selected from the group consisting of the aforementioned C, K, W, V, L and F, can effectively improve hair strength compared to compositions comprising three or more different amino acids.
[0131] In one embodiment, the composition may contain i) C; ii) K; and iii) one of W, V, L or F in a molar mass ratio of 1:0.1 to 5:0.1 to 5, but is not limited thereto. For example, the composition may contain one of i) C; ii) K; and iii) W, V, L or F in molar mass ratios of 1:0.1 to 5:0.1 to 5, 1:0.1 to 4:0.1 to 4, 1:0.1 to 3:0.1 to 3, 1:0.1 to 2:0.1 to 2, 1:0.5 to 2:0.5 to 2, 1:0.5 to 1.5:0.5 to 2, 1:0.6 to 1.5:0.6 to 2, 1:0.7 to 1.4:0.7 to 1.9, 1:0.8 to 1.3:0.8 to 1.8, 1:0.9 to 1.3:0.9 to 1.7, 1:1 to 1.3:1 to 1.7, 1:1.2 to 1.3:1.6 to 1.7, or 1:1:1, but is not limited thereto.
[0132] In one implementation example, hair may include, but is not limited to, hair, eyebrows, and / or eyelashes.
[0133] Methods to protect hair, repair damaged hair, or strengthen hair
[0134] In one aspect of this disclosure, a method is provided for protecting, repairing, or strengthening hair, the method comprising the step of applying a mixture of the aforementioned peptides, peptide derivatives, or amino acids.
[0135] In one implementation example, the method for protecting, repairing damaged hair, or strengthening hair according to one aspect of the present disclosure can improve the tensile strength of hair.
[0136] In one implementation, the method for protecting, repairing damaged hair, or strengthening hair according to one aspect of the present disclosure can increase the denaturation enthalpy of hair.
[0137] In one embodiment, the method for protecting, repairing, or strengthening hair according to one aspect of the present disclosure can repair the damage to the CMC structure in the damaged hair, and ultimately improve the hardness, smoothness, and elasticity of the damaged hair.
[0138] In one implementation example, the method for protecting, repairing damaged hair, or strengthening hair according to one aspect of the present disclosure may be a method for protecting hair, repairing damaged hair, or strengthening hair.
[0139] In one implementation example, the method for protecting, repairing damaged hair, or strengthening hair according to one aspect of the present disclosure can be a method for protecting, repairing, or strengthening eyebrows.
[0140] In one implementation example, the method for protecting, repairing damaged hair, or strengthening hair according to one aspect of the present disclosure can be a method for protecting eyelashes, repairing damaged eyelashes, or strengthening eyelashes.
[0141] 1) Methods to protect, repair, or strengthen hair - 1
[0142] In one aspect of this disclosure, a method for protecting, repairing, or strengthening hair is provided, the method comprising the step of applying an effective amount of the aforementioned peptide or peptide derivative to a subject who requires protection, repair of damaged hair, or strengthening of hair.
[0143] Peptides and peptide derivatives are the same as described above, so specific details are omitted.
[0144] In one implementation, the subject may be an animal including, but not limited to, mammals (e.g., humans).
[0145] In one implementation, the subject can be an individual with damaged hair or an individual with undamaged hair. In another implementation, the subject can be an individual whose hair CMC structure is damaged due to hair damage.
[0146] In this disclosure, administration can be by oral administration, transdermal administration, subcutaneous administration, intravenous administration, intraperitoneal administration, intramuscular administration, or topical application, but is not limited thereto. Preferably, it can include topical application by applying an effective amount of the aforementioned peptide or peptide derivative to the hair.
[0147] In one implementation, the daily dose of the active ingredient can be from 0.0001 to 10000 mg / kg, but is not limited thereto. In one implementation, the active ingredient can be administered once or in multiple divided doses throughout the day. However, it should be understood that the dosage of the active ingredient should be determined based on several relevant factors such as the route of administration, the age, sex, and weight of the subject, and therefore, the dosage described does not limit the scope of the invention in any way.
[0148] In one implementation, the peptide or peptide derivative may be applied to the subject's hair in amounts ranging from 0.1 to 100 mg per 1 gram of hair, but is not limited thereto. For example, the peptide or peptide derivative may be applied to the subject's hair in amounts of more than 0.1 mg, more than 1 mg, more than 2 mg, more than 3 mg, more than 4 mg, more than 5 mg, more than 6 mg, more than 7 mg, more than 8 mg, more than 9 mg, more than 10 mg, less than 11 mg, less than 12 mg, less than 13 mg, less than 14 mg, less than 15 mg, less than 16 mg, less than 17 mg, less than 18 mg, less than 19 mg, less than 20 mg, less than 30 mg, less than 40 mg, less than 50 mg, less than 60 mg, less than 70 mg, less than 80 mg, less than 90 mg, less than 100 mg, or combinations thereof (e.g., 1 to 20 mg, 9 to 11 mg), but is not limited thereto.
[0149] In a preferred embodiment, the peptide or peptide derivative may be applied to the subject's hair in amounts of 5 mg to 50 mg, 10 mg to 40 mg, or 15 mg to 30 mg.
[0150] In one implementation, the peptide or peptide derivative may be administered to the subject once or multiple times, but is not limited thereto.
[0151] In one embodiment, the peptide or peptide derivative may be used in combination with any other ingredient that can have the effects of protecting hair, repairing damaged hair, or strengthening hair, but is not limited thereto.
[0152] In one implementation example, hair may include, but is not limited to, hair, eyebrows, and / or eyelashes.
[0153] 2) Methods to protect, repair, or strengthen hair - 2
[0154] Furthermore, in one aspect of this disclosure, a method for protecting, repairing, or strengthening hair is provided, the method comprising: applying an effective amount of a combination of at least three amino acids selected from the group consisting of C, K, W, V, L, and F as an active ingredient to a subject who requires protection, repair of damaged hair, or strengthening of hair.
[0155] Regarding the subjects, application, dosage, etc., they are the same as those in “1) Method for protecting, repairing or strengthening hair - 1” above, so specific details are omitted.
[0156] In one implementation example, the step of administering a combination of at least three amino acids as an active ingredient to the subject can be to administer a combination of C; K; and one of W, V, L or F as an active ingredient to the subject. In another implementation example, the step of administering a combination of at least three amino acids as an active ingredient to the subject can be to administer a combination of C, K, and W as an active ingredient to the subject.
[0157] In one embodiment, the step of administering a combination of at least three amino acids as an active ingredient to the subject can be administering a composition comprising at least three amino acids selected from C, K, W, V, L, and F as an active ingredient to the subject. In another embodiment, the step of administering a combination of at least three amino acids as an active ingredient to the subject can be administering a composition comprising C; K; and one of W, V, L, or F as an active ingredient to the subject. In yet another embodiment, the step of administering a combination of at least three amino acids as an active ingredient to the subject can be administering a composition comprising C, K, and W as an active ingredient to the subject.
[0158] In one implementation example, one of i)C; ii)K; and iii)W, V, L, or F may be administered to the subject in a molar mass ratio of 1:0.1 to 5:0.1 to 5, but is not limited thereto. For example, one of i) C; ii) K; and iii) W, V, L, or F may be administered to the subject in a molar mass ratio of 1:0.1 to 5:0.1 to 5, 1:0.1 to 4:0.1 to 4, 1:0.1 to 3:0.1 to 3, 1:0.1 to 2:0.1 to 2, 1:0.5 to 2:0.5 to 2, 1:0.5 to 1.5:0.5 to 2, 1:0.6 to 1.5:0.6 to 2, 1:0.7 to 1.4:0.7 to 1.9, 1:0.8 to 1.3:0.8 to 1.8, 1:0.9 to 1.3:0.9 to 1.7, 1:1 to 1.3:1 to 1.7, 1:1.2 to 1.3:1.6 to 1.7, or 1:1:1, but is not limited thereto.
[0159] In one implementation example, a combination of at least three amino acids selected from the group consisting of C, K, W, V, L, and F may be administered to the subject once or multiple times, but is not limited thereto.
[0160] In one implementation example, a combination of at least three amino acids selected from the group consisting of C, K, W, V, L, and F can be used in combination with any other ingredients that can have the effects of protecting hair, repairing damaged hair, and strengthening hair, but is not limited thereto.
[0161] In one implementation example, hair may include, but is not limited to, hair, eyebrows, and / or eyelashes.
[0162] Uses of compositions including peptides, peptide derivatives, or amino acids
[0163] One aspect of this disclosure provides the use of a composition comprising the aforementioned peptides, peptide derivatives, or mixtures of amino acids.
[0164] 1) Uses of peptides or peptide derivatives - 1
[0165] One aspect of this disclosure provides the use of the aforementioned peptide for protecting hair, repairing damaged hair, or strengthening hair.
[0166] One aspect of this disclosure provides the use of the aforementioned peptide derivative for protecting hair, repairing damaged hair, or strengthening hair.
[0167] In one aspect of this disclosure, the aforementioned peptide is provided for use in preparing compositions for protecting, repairing, or strengthening hair.
[0168] In one aspect of this disclosure, there is a use of the aforementioned peptide derivative for preparing compositions for protecting hair, repairing damaged hair, or strengthening hair.
[0169] Peptides and peptide derivatives are the same as described above, so specific details are omitted.
[0170] In one implementation example, the use can be therapeutic or non-therapeutic.
[0171] In one implementation example, hair may include, but is not limited to, hair, eyebrows, and / or eyelashes.
[0172] 2) Uses of compositions including amino acids - 2
[0173] One aspect of this disclosure provides the use of a composition comprising at least three amino acids selected from the group consisting of C, K, W, V, L, and F for protecting, repairing, or strengthening hair.
[0174] One aspect of this disclosure provides the use of a composition comprising at least three amino acids selected from the group consisting of C, K, W, V, L, and F, for preparing a composition for protecting, repairing, or strengthening hair.
[0175] Compositions comprising at least three amino acids selected from the group consisting of C, K, W, V, L, and F are the same as described above, and therefore specific details are omitted.
[0176] In one implementation example, hair may include, but is not limited to, hair, eyebrows, and / or eyelashes.
[0177] The present invention will now be described in detail with reference to specific embodiments. These embodiments are provided for illustrative purposes only and are intended to aid in understanding the invention; the scope and extent of the invention are not limited thereto.
[0178] Experimental Example 1. Construction of Tripeptide Candidate Sequences and Determination of Their Binding Ability to Hair
[0179] After constructing multiple candidate tripeptide sequences composed of arbitrary amino acid sequences, the binding affinity of each candidate tripeptide sequence to hair was determined by three-dimensional molecular docking simulation. By predicting sequences that exhibit excellent hair protection, damaged hair repair, or hair strengthening effects, the tripeptide sequences with superior binding affinity were selected.
[0180] Specifically, the amino acids suitable for application to hair from the 20 essential amino acids were divided into three groups. Group 1 (C) consists of sequences effective for disulfide bonds in hair, including cysteine (Cys, C). Group 2 (HPO) consists of sequences with excellent hair penetration properties, including alanine (Ala, A), leucine (Leu, L), phenylalanine (Phe, F), proline (Pro, P), valine (Val, V), and tryptophan (Trp, W). Group 3 (POS) consists of sequences that help improve the tensile strength of hair, including arginine (Arg, R), lysine (Lys, K), and histidine (His, H), which are cationic amino acids. According to the amino acid configurations in Table 1 below (9 cases), the amino acids contained in the three groups (Group 1 (C), Group 2 (HPO), and / or Group 3 (POS)) can be configured in the first, second, and third order, respectively, to construct tripeptide candidate sequences with various sequence combinations. In Table 1, "Number of amino acids" indicates the number of amino acids that can be configured in the 1st, 2nd, and 3rd positions. Ultimately, a total of 216 tripeptide candidate sequences were calculated as one-letter codes for the amino acids (represented by letters) (see Table 1).
[0181] Table 1
[0182]
[0183]
[0184] After inputting the calculated single-letter codes into an Excel file in order based on rows, use DS software to generate a unified three-dimensional peptide molecule file (*.sd or *.sdf) including atomic coordinate information.
[0185] To calculate the binding affinity of the calculated three-dimensional peptide molecular files, three three-dimensional molecular files (*.pdb) of hair keratin, which served as binding targets, were obtained from AlphaFold (alphafold.ebi.ac.uk). Specifically, the three-dimensional molecular files (*.pdb) of Keratin 85 (Uniprot code: P78386), Keratin 33b (Uniprot code: Q14525), and Keratin-associated protein 3-1 (Uniprot code: Q9BYR8) were used.
[0186] Using the CDocker module of Discovery Studio (DS) software, follow Figure 1 Under the given conditions, the binding energy between the three-dimensional peptide molecule file and the binding regions of the three types of keratin was calculated. The lower the binding energy, the stronger the binding force.
[0187] The results showed that among the 216 candidate tripeptide sequences, tripeptides with binding energies to the three keratins below -50 kcal / mol included CKF, CKW, CWK, KCF, KCL, and KCV. On the other hand, PCP was the tripeptide with a binding energy above 0 kcal / mol and the weakest binding affinity.
[0188] Experimental Example 2. Evaluation of the efficacy of amino acid combinations
[0189] First, the amino acid components constituting the tripeptide with the highest binding strength identified in Experimental Example 1 above were mixed to prepare a mixture. Specifically, the amino acid components constituting the tripeptide CWK with the highest binding strength were mixed according to the molar mass ratios shown in Table 2 below to prepare a mixture (Example 1) (refer to Table 2). As a comparison, the amino acid components constituting the tripeptide CPP with the lowest binding strength were mixed according to the molar mass ratios shown in Table 2 below to prepare a mixture (Comparative Example 1). The values in Table 2 represent the molar mass ratios of the amino acids constituting the mixture.
[0190] Table 2
[0191]
[0192] (1) Determination of tensile strength
[0193] The compositions in Table 2 above were applied to human hair, and their tensile strength was compared.
[0194] Specifically, bleached hair bundles (1g, manufactured by Beaulax) were prepared. The hair bundles were washed with a regular shampoo without conditioning, rinsed for 1 minute, and dried for 2 minutes. The dried hair bundles (1g) were then immersed in 100g of a solution containing 0.1% by weight of the test substance (the mixture of Example 1 or Comparative Example 1 in Table 2 above) (in this case, the solution was the test substance (0.1% by weight) dissolved in purified water (the remainder)) for approximately 30 minutes. After rinsing the soaked hair bundles with running water for 1 minute, they were allowed to air dry for at least 12 hours. Thirty hairs were randomly selected from each hair bundle treated with the test substance. Thirty hairs were randomly selected from the control group hair bundles that were not treated with the test substance. The tensile strength of each selected hair was measured using an MTT175 (manufactured by DiaStron).
[0195] The results showed that, compared with bleached hair tufts, hair treated with the amino acid mixture that constitutes the tripeptide of CWK had significantly increased tensile strength (reference). Figure 2 : Figure 2 In this context, "Blank" represents untreated control hair, "CWKaminomix" represents hair treated with the mixture of Example 1, and "CPP aminomix" represents hair treated with the mixture of Comparative Example 1. Figure 2 In the figure, the y-axis represents the tensile strength (break load), and the unit is gmf.
[0196] (2) Determination of denaturation enthalpy
[0197] The denaturation enthalpy of hair structural proteins was compared using a DSC (Differential Scanning Calorimetry) analyzer, based on whether the subject's hair had been treated. DSC is used as an analytical method to confirm the stability of hair structural proteins; the greater the hair damage, the lower the stability of the hair structural proteins, and thus the lower the denaturation enthalpy.
[0198] Specifically, bleached hair bundles (1g, manufactured by Beaulax) were prepared. The hair bundles were washed with a non-conditioning shampoo, rinsed for 1 minute, and dried for 2 minutes. The dried hair bundles (1g) were then immersed in 100g of a solution containing 0.01% by weight of the test substance (the mixture from Example 1 in Table 2 above). (This solution was a solution of the 0.01% by weight mixture from Example 1 dissolved in purified water (the remainder) and ethanol (80% by weight)) for 30 minutes. After rinsing the soaked hair bundles with running water for 1 minute, they were allowed to air dry for at least 12 hours. The treated hair bundles were then cut into 1mm lengths and combined with 3-5mg of distilled water and 6-15mg of water in an aluminum high-pressure capsule. The mixture was allowed to stand for at least 12 hours to achieve phase equilibrium within the high-pressure capsule, thus preparing the sample for DSC determination (DSC sample). The denaturation enthalpy (50–190 degrees, 10 degrees / min) of the prepared DSC sample was determined using a DSC (DiscoveryDSC 250, TA Instruments) instrument.
[0199] The results showed that hair treated with the amino acid mixture that constitutes the CWK sequence tripeptide had a significantly increased denaturation enthalpy of hair structural proteins compared to control hair (reference). Figure 3 ; Figure 3 In this context, "bleach" refers to the control group hair that was not treated with the test substance, and "aminomix" refers to the hair that was treated with the mixture from Example 1.
[0200] Experimental Example 3. Efficacy Evaluation of Tripeptides - 1
[0201] From the tripeptide calculated in Experiment 1 above, peptides with the sequences CKF, CWK, KCL, KCV, and PCP were synthesized according to the following three steps. First, a reaction resin (2-Cl-(Trt)-Cl resin; CAS No: 27144-18-9) was prepared (Step 1). Then, using a peptide synthesizer, three amino acids were coupled by adding them in the form of a single amino acid Fmoc (fluorenylmethoxycarbonyl protecting group)-amino acid-OH (Step 2). Cleavage buffer was added to the coupled material, and the precipitated peptide was recovered.
[0202] (1) Determination of tensile strength
[0203] Using the same method as in "Experimental Example 2.(1) Determination of tensile strength", the test substances (the above 5 tripeptides) were applied to hair and the tensile strength was compared.
[0204] Specifically, bleached hair bundles (1g, manufactured by Beaulax) were prepared. The hair bundles were washed with a non-conditioning shampoo, rinsed for 1 minute, and dried for 2 minutes. The dried hair bundles (1g) were then immersed in 100g of a solution containing 0.01% by weight of the test substance (a synthetic tripeptide) (the solution being a solution of the test substance (0.01% by weight) dissolved in purified water (the remainder) and ethanol (80% by weight)) for approximately 30 minutes. After rinsing the soaked hair bundles with running water for 1 minute, they were allowed to air dry for at least 12 hours. Thirty hairs were randomly selected from each hair bundle treated with the test substance. Thirty hairs were randomly selected from the control group hair bundles that were not treated with the test substance. The tensile strength of each selected hair was determined using an MTT175 (manufactured by DiaStron).
[0205] The results showed that, compared with the bleached hair bundles used as a control group, the tensile strength of hair treated with CKF, CWK, KCL, and KCV was significantly increased. On the other hand, the increase in tensile strength of hair treated with PCP was not significant (see reference). Figure 4 ; Figure 4 In this context, "CKF" indicates hair treated with CKF tripeptide, "CTL-BLEACH" indicates control hair that was not treated with the test substance, "CWK" indicates hair treated with CWK tripeptide, "KCL" indicates hair treated with KCL tripeptide, "KCV" indicates hair treated with KCV tripeptide, and "PCP" indicates hair treated with PCP tripeptide.
[0206] (2) Determination of denaturation enthalpy
[0207] The denaturation enthalpy was determined using the same method as in "Experimental Example 2.(2) Determination of Denaturation Enthalpy", and CWK tripeptide was applied to hair as the test substance to compare the denaturation enthalpy.
[0208] The results showed that, compared with the control group, hair treated with CWK tripeptide had a significantly increased denaturation enthalpy of hair structural proteins (reference). Figure 3 ; Figure 3 In this context, "bleach" refers to the control group hair that was not treated with the test substance, and "CWK" refers to the hair that was treated with CWK tripeptide.
[0209] Example 4. Efficacy evaluation of tripeptides with fatty acids bound at the N-terminus.
[0210] (1) Measurement of binding affinity with keratin
[0211] Palmitic acid was added to the sequences of the four tripeptides (CKF, CWK, KCL and KCV) whose effects were confirmed by "Experimental Example 3" to generate molecular files. Then, molecular docking simulation was performed under the same conditions as in Experimental Example 1 above, and the binding energy of the tripeptides with added palmitic acid to the three keratins was measured.
[0212] The results showed that the tripeptide with added palmitic acid had a lower binding energy to the three types of keratin compared to the tripeptide without added palmitic acid. Therefore, it can be confirmed that the tripeptide with added palmitic acid has a higher binding affinity to hair.
[0213] (2) Determination of tensile strength
[0214] In the tripeptide whose effectiveness was confirmed by “Experimental Example 4.(1) and keratin binding force determination”, palmitic acid was covalently bound to three tripeptides (CKF, CWK, KCV), and tensile strength was measured.
[0215] Specifically, a tripeptide was synthesized using the same method as the peptide synthesis method in "Experimental Example 3" above, and palmitic acid was added to the N-terminus of the peptide (reagents: HBTU (Hexafluorophosphate Benzotriazole), NMM (N-Methylmorpholine), DMF (Dimethylformamide), 0.3M, at room temperature for 1 hour). This resulted in a tripeptide covalently bonded to the N-terminus (i.e., palmitoyl tripeptide). Then, using the same method as in "Experimental Example 3.(1) Determination of Tensile Strength", the test substance (the tripeptide covalently bonded to the N-terminus) was applied to hair, and the tensile strength was compared.
[0216] The results showed that the tensile strength of hair treated with a tripeptide covalently bound to palmitic acid at the N-terminus was significantly increased compared to the bleached hair bundles used as a control group (reference). Figure 5 ;exist Figure 5In the table, "aminomix" indicates hair treated with the mixture of Example 1 in Table 2, "Con" indicates control hair untreated with the test substance, "CWK" indicates hair treated with CWK tripeptide, "pal-CKF" indicates hair treated with CKF (palmitoyl-CKF) covalently bonded to the N-terminus with palmitic acid, "pal-CWK" indicates hair treated with CWK (palmitoyl-CWK) covalently bonded to the N-terminus with palmitic acid, "pal-KCV" indicates hair treated with KCV (palmitoyl-KCV) covalently bonded to the N-terminus with palmitic acid, and "palmitic acid" indicates hair treated with palmitic acid. Furthermore, hair treated with tripeptides covalently bonded to the N-terminus with palmitic acid exhibited higher tensile strength compared to hair treated with tripeptides without covalently bonded palmitic acid at the N-terminus or hair treated with the amino acid mixture.
[0217] (3) Determination of denaturation enthalpy
[0218] The denaturation enthalpy was determined using the same method as in “Experimental Example 2.(2) Determination of denaturation enthalpy”, and as the test substance, a tripeptide with palmitic acid covalently bound to its N-terminus (i.e., palmitoyl tripeptide) was applied to hair and the denaturation enthalpy was compared.
[0219] The results showed that hair treated with a tripeptide covalently bound to palmitic acid at the N-terminus had a significantly increased denaturation enthalpy of structural proteins compared to control hair (reference). Figure 3 ;exist Figure 3 In this context, "palmitic acid" indicates hair treated with palmitic acid, "pal-CWK" indicates hair treated with CWK (palmitoyl-CWK) where palmitic acid is covalently bonded to the N-terminus, "pal-KCV" indicates hair treated with KCV (palmitoyl-KCV) where palmitic acid is covalently bonded to the N-terminus, and "pal-CKF" indicates hair treated with CKF (palmitoyl-CKF) where palmitic acid is covalently bonded to the N-terminus.
[0220] (4) Confirmation of hair penetration and binding effect using confocal microscopy
[0221] A palmitoyl-CWK-bound (fluorescently labeled) green fluorescent substance (FITC; fluorescein isothiocyanate) was applied to hair as a tripeptide (i.e., palmitoyl tripeptide) covalently bound to palmitic acid at its N-terminus. The stained areas were then compared using confocal microscopy to confirm changes in hair structure that influenced the increase in tensile strength.
[0222] The results showed that, Figure 6As shown, the cuticle, cortex, and CMC areas are green ( Figure 6 (Represented in gray), thus confirming that palmitoyl tripeptide strongly binds to the hair cuticle, cortex, and CMC (see reference). Figure 6 (Left-side photo; gray). The results show a similar tendency to those obtained by applying Nile Red, a lipid-soluble fluorescent substance, to hair (reference). Figure 6 The photo on the right; gray).
[0223] On the one hand, to compare hair penetration pathways, after applying 5-(4-Dimethylaminobenzylidene)rhodanine, a water-soluble fluorescent substance, to hair, confocal microscopy was used to confirm the stained areas (in...). Figure 7 (Represented in gray). The results show that, as... Figure 7 As shown, the water-soluble fluorescent substance left almost no residue in the keratin layer of the hair surface and did not fill the missing areas of CMC inside the hair (reference). Figure 7 ;grey).
[0224] The experimental results indicate that palmitoyl tripeptide targets the CMC within hair follicles via a penetration pathway different from that of water-soluble substances, thereby improving the structural function of hair.
[0225] Experimental Example 5. Efficacy Evaluation of Oligopeptides with Combined Tripeptide Sequences
[0226] In Experiment 1 above, three-dimensional molecular files (molecular structure files) were generated from the tripeptide sequences with the highest binding affinity: i) oligopeptides with a single repeating sequence (12mer; AP 3mer*4 (repeat; for example, CWKCWKCWKCWK (SEQ ID NO: 6)) and ii) oligopeptides with arbitrary combinations of two or more sequences (12mer; AP 3mer*4 (random)). The binding affinity of each generated peptide molecular file to hair was measured. Following the same methods and conditions as in Experiment 1 above, three-dimensional molecular files of the test peptides were generated, and molecular docking simulations were performed using the generated molecular files to measure the binding affinity to the hair.
[0227] For comparison, molecular files of other known company peptides or similar peptides were generated, and their binding affinity to hair was confirmed (see reference). Figure 8Specifically, (a) the amino acids (arginine, cysteine, and glycine) known to constitute the known tetrapeptide-97 (Caregen; INCI Monograph ID: 37801) were arbitrarily combined to generate molecular files for all possible tetrapeptides. Then, the binding affinity to hair was measured using each of the generated tetrapeptide molecular files. Furthermore, (b) the amino acids (cysteine, glycine, isoleucine, phenylalanine, serine, threonine, and valine) known to constitute the known oligopeptide sh-Oligopeptide-78 (INCI Monograph ID: 28756) were arbitrarily combined to generate molecular files for all possible oligopeptides (total of 13 amino acids). In addition, (c) molecular files of eight known oligopeptides (CCQSSCCKPSC (PepA; SEQ ID NO: 10), CVSSCCKPQCC (PepB; SEQ ID NO: 11), PIYCRRTCYH (PepC; SEQ ID NO: 12), DCKLPCNPCA (PepD; SEQ ID NO: 13), CLPCLPAASC (PepE; SEQ ID NO: 14), CEPAICEPSC (PepF; SEQ ID NO: 15), CQCSCCKPYCS (PepG; SEQ ID NO: 16), GGVCGPSPPCITT (KP; SEQ ID NO: 17)) were generated. The binding affinity of all oligopeptides generated as molecular files in (b) and (c) above to hair was then determined.
[0228] exist Figure 8 In the above, "CG 4mer" is the peptide with the highest binding affinity among all tetrapeptides generated as molecular files in (a). "CG 4mer*3" is an oligopeptide (total amino acid number 12) that repeats the sequence of the peptide with the highest binding affinity among all tetrapeptides generated as molecular files in (a) three times. "K18(13mer)" is the peptide with the highest binding affinity among all oligopeptides generated as molecular files in (b) and (c) above. "AP 3mer" is the peptide with the highest binding affinity among the tripeptide candidate sequences in Experimental Example 1 above. "AP 3mer-Pal" is the peptide with the highest binding affinity for hair in the molecular file of the tripeptide candidate sequences in Experimental Example 1 above, which contains a palmitic acid added to the N-terminus. "AP 3mer*4(repeat))" is the peptide with the highest binding affinity for hair among the oligopeptides that repeat any one of the tripeptide candidate sequences in Experimental Example 1 four times. “AP 3mer*4(random)” is the peptide with the highest binding affinity to hair among the oligopeptides formed by randomly combining two or more sequences from the tripeptide candidate sequences in Experiment Example 1 above.
[0229] like Figure 8 As shown, the oligopeptides with repeating or combined tripeptide sequences (AP 3mer*4 (repeated), AP 3mer*4 (random)) of the examples exhibited a maximum binding affinity of 150% compared to other known peptides or similar peptides (see reference). Figure 8 ). Figure 8 The y-axis represents negative values. Therefore, it can be considered as... Figure 8 The higher the value on the y-axis, the lower the binding energy and the higher the binding force. Therefore, it can be confirmed that the oligopeptide of this embodiment can bind to hair more effectively and improve hair strength compared to other known peptides from other companies.
[0230] On the one hand, although the tripeptide (AP 3mer) and palmitoyl tripeptide (AP 3mer-Pal) have lower binding affinity to hair compared to oligopeptides with repeating or combined tripeptide sequences (AP 3mer*4 (repeated), AP 3mer*4 (random)), they still showed a significant improvement in hair strength compared to the untreated control group, as disclosed in Examples 1 to 4. At the same time, the tripeptide (AP 3mer) and palmitoyl tripeptide (AP 3mer-Pal) are easy to synthesize due to their short sequence length, thus offering advantages in terms of time and cost.
[0231] Experimental Example 6. Efficacy Evaluation of Tripeptides - 2
[0232] The KCV-sequence tripeptide was synthesized using the same method as disclosed in Experimental Example 3 above, and its efficacy was evaluated.
[0233] (1) Preparation of simulated eyebrow hairs
[0234] To confirm that the test substance exhibits the same effect in eyebrows, additional experiments were conducted using simulated eyebrow hair. On the one hand, as mentioned earlier, the structure and composition of eyebrows are no different from those of hair in other parts of the body (e.g., head hair), and the basic structure / composition of hair follicles in the body is the same. Therefore, the test substance can also show the same effect in eyebrows and / or eyelashes as it does in hair in other parts of the body.
[0235] Specifically, since it is difficult to obtain eyebrow hairs directly from living organisms for evaluation, human hairs of equivalent eyebrow thickness were selected using Fibra.one (manufactured by DiaStron). The hairs were prepared to a length suitable for use with a machine capable of measuring tensile strength. The prepared hair bundles were then heat-treated by manually applying pressure 20 times at 160°C using a hair straightener. Control hairs were used as a reference. Figure 9 and Figure 11 Untreated hair was prepared. In Experiment 6, the test substance was not treated on the untreated hair.
[0236] Then, KCV (as the test substance) was applied to heat-treated hair bundles. Figure 9 and Figure 11 KCV-treated hair). Specifically, the prepared hair bundle (1g, manufactured by Beaulax) was washed with a basic cleanser without conditioning properties, rinsed for 1 minute, and dried for 2 minutes. The dried hair bundle (1g) was then immersed in 100g of a solution containing 0.01% by weight of the test substance (at this time, the solution is a solution of the test substance (0.01% by weight) dissolved in purified water (the remainder)) for approximately 30 minutes. After rinsing the soaked hair bundle with running water for 1 minute, it was then allowed to air dry for at least 12 hours. To compare the effects of KCV-based treatment, hair that was washed and dried under the same conditions as above, but without the test substance, was prepared. Figure 9 and Figure 11 Heat damage to hair.
[0237] (2) Determination of tensile strength
[0238] Using the same method as in "Experimental Example 2.(1) Determination of tensile strength", the tensile strength of KCV-treated wool, heat-damaged wool and untreated wool were compared.
[0239] Specifically, 30 hairs were randomly selected from each hair bundle treated with the test substance (KCV-treated hairs). Similarly, 30 hairs were randomly selected from each control group (each consisting of heat-damaged hairs and untreated hairs). The tensile strength of each selected hair was measured using a Fibra.one (manufactured by DiaStron).
[0240] The results showed that, compared with heat-damaged hair tracts, the tensile strength of KCV-treated hair tracts was significantly increased after heat treatment (reference). Figure 9 ;exist Figure 9 In this context, "KCV-treated hair" refers to hair treated with KCV tripeptide after heat treatment, "untreated hair" refers to control hair that has not undergone heat treatment or treatment with the test substance, and "heat-damaged hair" refers to hair that has undergone heat treatment. Figure 9 In the diagram, the y-axis represents the tensile strength (break load) relative to the area, with units of gmf / μm. 2 .
[0241] (3) Measurement of elasticity
[0242] The elasticity of KCV-treated hair, heat-damaged hair, and untreated hair was compared. The force resisted by the hair in the horizontal direction was defined as elasticity, and the elasticity was measured according to the steps outlined in the "Methods for Measuring Hair Elasticity" (see reference). Figure 10 ).
[0243] Methods for measuring hair elasticity
[0244] (i) Place the module (M) containing the eyebrows on the horizontally moving track. (ii) Place a total of 10 strands of cut hair (15mm) vertically onto the clips fixed to module M. (iii) Move module M toward the fixed micromanometer (DS2-5N, OPTECH). (iv) Measure the force transmitted by the hair strands to the tip of the micromanometer.
[0245] The results showed that, compared with heat-damaged hair tracts, the elasticity of KCV-treated hair tracts was significantly increased after heat treatment (reference). Figure 11 ;exist Figure 11 In this context, "KCV-treated hair" refers to hair treated with KCV tripeptide after heat treatment, "untreated hair" refers to control hair that has not undergone heat treatment or treatment with the test substance, and "heat-damaged hair" refers to hair that has undergone heat treatment. Figure 11 In the diagram, the y-axis represents the elastic force, with units of 10. -3 N.
[0246] This disclosure is further illustrated by the following implementation examples, which do not limit the scope of the claims.
[0247] Example 1. A peptide comprising one or more amino acid sequence units consisting of Xaa-Yaa-Zaa, wherein,
[0248] The Xaa, Yaa, and Zaa are each independently selected from groups formed by C (cysteine), K (lysine), W (tryptophan), V (valine), L (leucine), and F (phenylalanine).
[0249] Xaa, Yaa, and Zaa are all different from each other. When Xaa and Yaa are C and K respectively, Zaa is not L.
[0250] Implementation Example 2. A peptide, which serves as the peptide in Implementation Example 1, wherein,
[0251] Two of Xaa, Yaa and Zaa are C and K respectively, wherein when Xaa and Yaa are C and K respectively, Zaa is not L.
[0252] Implementation Example 3. A peptide, which is the peptide of any one of Implementation Examples 1 and 2, wherein,
[0253] The peptide is a tripeptide composed of a sequence unit of Xaa-Yaa-Zaa.
[0254] Implementation Example 4. A peptide, which is the peptide of any one of Implementation Examples 1 to 3, wherein,
[0255] The peptide is an oligopeptide composed of 2 to 4 Xaa-Yaa-Zaa sequence units.
[0256] The sequence units constituting the oligopeptide are all identical, partially identical, or all different.
[0257] Implementation Example 5. A peptide, which is the peptide of any one of Implementation Examples 1 to 4, wherein,
[0258] The peptides are CKF, CWK, KCV, CKFCKF (SEQ ID NO: 1), CKFCKFCKF (SEQ ID NO: 2), CKFCKFCKFCKF (SEQ ID NO: 3), CWKCWK (SEQ ID NO: 4), CWKCWKCWK (SEQ ID NO: 5), CWKCWKCWKCWK (SEQ ID NO: 6), KCVKCV (SEQ ID NO: 6) NO: 7), KCVKCVKCV (SEQ ID NO: 8), KCVKCVKCVKCV (SEQ ID NO: 9), CWKCWKKCLKCLKCV (SEQ ID NO: 18), CKWCWKKCLKCVKCL (SEQ ID NO: 19), CKWKCFCKFCWKKCV (SEQ ID NO: 20), KCFKCFCKWCKFKCV (SEQ ID NO: 19) NO: 21), or CKFCKWKCFKCVKCF (SEQ ID NO: 22).
[0259] Example 6. A peptide derivative having an acyl group derived from a fatty acid or organic acid attached to the N-terminus of the peptide described in any one of Examples 1 to 5.
[0260] Implementation Example 7. A peptide derivative, which serves as the peptide derivative of Implementation Example 6, wherein,
[0261] The fatty acid is a C10 to C30 fatty acid, preferably a C15 to C20 fatty acid, and more preferably a C15 to C17 fatty acid.
[0262] Example 8. A peptide derivative, which is a peptide derivative as described in any one of Examples 6 to 7, wherein the fatty acid is at least one selected from the group consisting of palmitic acid, stearic acid, arachidic acid, palmitoleic acid, oleic acid and eicosenoic acid, more preferably palmitic acid.
[0263] Example 9. A peptide derivative, which is a peptide derivative as described in any one of Examples 6 to 8, wherein,
[0264] The peptide derivative is CKF with a palmitoyl group attached to the N-terminus, CWK with a palmitoyl group attached to the N-terminus, or KCV with a palmitoyl group attached to the N-terminus.
[0265] Example 10. A composition comprising the peptide described in any one of Examples 1 to 5 for protecting hair, repairing damaged hair, or strengthening hair.
[0266] Example 11. A composition comprising the peptide derivatives described in any one of Examples 6 to 9 for protecting hair, repairing damaged hair, or strengthening hair.
[0267] Example 12. A composition comprising at least three amino acids selected from the group consisting of C, K, W, V, L (leucine) and F, for protecting hair, repairing damaged hair, or strengthening hair.
[0268] Example 13. A composition for protecting hair, repairing damaged hair, or strengthening hair, which is the composition of Example 12, wherein,
[0269] The composition includes C; K; and one of W, V, L or F.
[0270] Example 14. A composition for protecting hair, repairing damaged hair, or strengthening hair, as described in any of Examples 12 to 13, wherein,
[0271] The composition includes C; K; and one of W, V, L or F.
[0272] Example 15. A composition for protecting hair, repairing damaged hair, or strengthening hair, as described in any one of Examples 12 to 14, wherein,
[0273] The molar mass ratio of C, K, and one of W, V, L, or F is 1:0.1-5:0.1-5.
[0274] [Sequence List]
[0275] SEQ ID NO: 1 (peptide sequence of one embodiment): CKFCKF
[0276] SEQ ID NO: 2 (peptide sequence of one embodiment): CKFCKFCKF
[0277] SEQ ID NO: 3 (peptide sequence of one embodiment): CKFCKFCKFCKF
[0278] SEQ ID NO: 4 (peptide sequence of one embodiment): CWKCWK
[0279] SEQ ID NO: 5 (peptide sequence of one embodiment): CWKCWKCWK
[0280] SEQ ID NO: 6 (peptide sequence of one embodiment): CWKCWKCWKCWK
[0281] SEQ ID NO: 7 (peptide sequence of one embodiment): KCVKCV
[0282] SEQ ID NO: 8 (peptide sequence of one embodiment): KCVKCVKCV
[0283] SEQ ID NO: 9 (peptide sequence of one embodiment): KCVKCVKCVKCV
[0284] SEQ ID NO: 18 (peptide sequence of one embodiment): CWKCWKKCLKCLKCV
[0285] SEQ ID NO: 19 (peptide sequence of one embodiment): CKWCWKKCLKCVKCL
[0286] SEQ ID NO: 20 (peptide sequence of one embodiment): CKWKCFCKFCWKKCV
[0287] SEQ ID NO: 21 (peptide sequence of one embodiment): KCFKCFCKWCKFKCV
[0288] SEQ ID NO: 22 (peptide sequence of one embodiment): CKFCKWKCFKCVKCF
[0289] SEQ ID NO: 10 (PepA peptide sequence): CCQSSCCKPSC
[0290] SEQ ID NO: 11 (PepB peptide sequence): CVSSCCKPQCC
[0291] SEQ ID NO: 12 (PepC peptide sequence): PIYCRRTCYH
[0292] SEQ ID NO: 13 (PepD peptide sequence): DCKLPCNPCA
[0293] SEQ ID NO: 14 (PepE peptide sequence): CLPCLPAASC
[0294] SEQ ID NO: 15 (PepF peptide sequence): CEPAICEPSC
[0295] SEQ ID NO: 16 (PepG peptide sequence): CQCSCCKPYCS
[0296] SEQ ID NO: 17 (KP peptide sequence): GGVCGPSPPCITT
Claims
1. Use of a peptide or peptide derivative for preparing compositions for protecting, repairing, or strengthening hair, wherein, The peptide is KCV (Lys-Cys-Val). The peptide derivative is KCV (palmitoyl-Lys-Cys-Val) with a palmitoyl group bound to the N-terminus.
2. The use according to claim 1, wherein, The peptide or peptide derivative increases the tensile strength of hair.
Citation Information
Patent Citations
Method and Apparatus for Evaluation of Taekwondo Strike Posture Using Artificial Intelligence Model for Discrimination of Taekwondo Motion
KR1020240101975A
Casing for heat exchanger and heat exchanger having the same
KR1020240172277A
Hair cosmetic composition comprising an extract of Aphanizomenon Flos-Aquae
KR102084765B1
Hair treatment composition with naturally - derived peptide identical to human hair
US20120052034A1
Anti-microbial peptides and uses of same
US20140087997A1