Composition for protecting hair, repairing damaged hair, or strengthening hair
By using peptides with specific amino acid sequences and their derivatives to bind to hair, hair damage problems are solved, hair strength and elasticity are improved, damaged structures are repaired, and effective protection and strengthening effects are achieved.
Patent Information
- Application Number
- CN202510691404.8
- Authority / Receiving Office
- CN · China
- Patent Type
- Applications(China)
- Current Assignee / Owner
- Priority Date
- 2024-11-27
- Filing Date
- 2025-05-27
- Publication Date
- 2025-08-15
- Estimated Expiration
- 2045-05-27
AI Technical Summary
The prior art is difficult to effectively protect and strengthen hair, especially eyebrows and eyelashes, avoid damage and vulnerability caused by chemical treatment, and traditional compositions are difficult to restore the structural strength of hair.
Using peptides of specific amino acid sequences and their derivatives, fill gaps to strengthen hair structure by binding to the hair epidermal layer, fur and cell membrane complexes of the hair, including tripeptides using amino acid sequences such as CKF, CWK or KCV, and binding fatty acids or organic acids at the N-terminus to improve binding strength.
Significantly improve the tensile strength and elasticity of hair, repair the CMC structure of damaged hair, and improve the hardness, smoothness and elasticity of hair.
Smart Images

Figure CN120478188A_ABST
Abstract
Description
[0001] CROSS-REFERENCE TO RELATED APPLICATIONS
[0002] This application claims priority to Korean Patent Application No. 10-2024-0101975, filed on July 31, 2024, the entire contents of which are incorporated herein by reference. This application claims priority to Korean Patent Application No. 10-2024-0172277, filed on November 27, 2024, the entire contents of which are incorporated herein by reference. Technical Field
[0003] The present disclosure relates to a composition for protecting or strengthening hair and corresponding uses of the composition. Background Art
[0004] For cosmetic purposes, chemical treatments of hair, such as perming and dyeing, are increasingly used, resulting in nonspecific damage to the various structural proteins and lipid components that make up hair. Because eyebrows and eyelashes are shorter, finer, and less abundant than hair on other parts of the body (e.g., head), they are more vulnerable to physical and chemical stimuli, and when damaged, they can cause significant cosmetic loss.
[0005] Hair (e.g., hair, eyebrows, eyelashes) is primarily composed of the cuticle, cortex, cell membrane complex (CMC), and medulla. Physical stimulation primarily damages the cuticle, while chemical stimulation primarily causes loss of the CMC and cortex. Repeated exposure to these stimuli can cause irreversible changes in the hair (e.g., hair, eyebrows, eyelashes), ultimately leading to damage, breakage, and / or loss, or brittleness, making it impossible to achieve the desired aesthetic appearance. To restore the tensile strength of hair to pre-damage levels, one method involves filling the gaps between the lost CMC and the cortex with a predetermined ingredient and combining this ingredient with the desired ingredient to strengthen the hair's structural strength. However, conventional hair compositions containing organic acids, etc., have difficulty restoring the CMC, which is composed of a lipid layer.
[0006]
Prior art literature
[0007] [Patent Literature]
[0008] Korean Patent No. 10-2084765 Summary of the Invention
[0009] Technical issues
[0010] One aspect of the present 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 enhancing the strength and elasticity of hair (e.g., hair, eyebrows, eyelashes).
[0011] One aspect of the present disclosure is to provide a peptide having the effect of protecting hair, repairing damaged hair, or strengthening hair.
[0012] One aspect of the present disclosure is to provide a peptide derivative having the effect of protecting hair, repairing damaged hair or strengthening hair.
[0013] One aspect of the present disclosure is to provide a composition for protecting hair, repairing damaged hair, or strengthening hair.
[0014] Technical Solution
[0015] According to one aspect of the present disclosure, a peptide comprises one or more sequence units consisting of Xaa-Yaa-Zaa, wherein the 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 the Xaa, Yaa and Zaa are different from each other, wherein when Xaa and Yaa are C and K, respectively, Zaa is not L.
[0016] The peptide derivative according to one aspect of the present disclosure may be a derivative in which a fatty acid or an organic acid is bound to the N-terminus of the peptide.
[0017] A composition for protecting hair, repairing damaged hair or strengthening hair according to one aspect of the present disclosure comprises the peptide defined above.
[0018] A composition for protecting hair, repairing damaged hair or strengthening hair according to one aspect of the present disclosure comprises the peptide derivative defined above.
[0019] According to one aspect of the present disclosure, a composition for protecting hair, repairing damaged hair, or strengthening hair includes a mixture of at least three amino acids selected from the group consisting of C, K, W, V, L (Leu; leucine), and F.
[0020] Effects of the Invention
[0021] According to one aspect of the present disclosure, the peptides, peptide derivatives, and / or compositions can increase the strength (or hardness) and / or elasticity of hair (e.g., damaged hair). According to one aspect of the present disclosure, the peptides, peptide derivatives, and / or compositions can bind to the cuticle, cortex, and / or CMC of hair (e.g., damaged hair), thereby increasing the strength of the hair, such as the tensile strength of the hair.
[0022] The peptides, peptide derivatives and / or compositions according to one aspect of the present disclosure 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. BRIEF DESCRIPTION OF THE DRAWINGS
[0023] Figure 1 Shown are the conditions for calculating the binding energy between a three-dimensional peptide molecule file and keratin using the CDocker module of Discovery Studio software (DASSAULT Systems).
[0024] Figure 2 Shown is the change in tensile strength of hair treated with the amino acid mixture.
[0025] Figure 3 Shown are the denaturation enthalpy changes of hair treated with an amino acid mixture, a tripeptide, and a tripeptide having a fatty acid bound to the N-terminus.
[0026] Figure 4 Shown are changes in the tensile strength of hair treated with the tripeptide.
[0027] Figure 5 Shown are changes in the tensile strength of hair treated with a tripeptide having a fatty acid bonded to the N-terminus, an amino acid mixture, and a tripeptide.
[0028] Figure 6 These are confocal microscopic photographs showing how a fluorescently labeled palmitoyl tripeptide (a tripeptide with a fatty acid bound to its N-terminus; left photograph) and a fat-soluble fluorescent substance (right photograph) have penetrated into and bound to hair.
[0029] Figure 7 This is a confocal micrograph showing the state of a water-soluble fluorescent substance penetrating into and binding to hair.
[0030] Figure 8 This is the result of confirming the binding ability of oligopeptides with repeated or combined tripeptide sequences to hair.
[0031] Figure 9 Shown are changes in the tensile strength of eyebrows treated with a tripeptide and a tripeptide having a fatty acid bound to the N-terminus.
[0032] Figure 10 This figure shows the step-by-step method of measuring eyebrow elasticity.
[0033] Figure 11 The elasticity of hair treated with a tripeptide and a tripeptide having a fatty acid bonded to the N-terminus is shown. DETAILED DESCRIPTION
[0034] The various embodiments and terms used in this application are not intended to limit the technical features described in this application using specific embodiments, but should be understood to include various modifications, equivalents or substitutes of the embodiments.
[0035] The present inventors have developed a substance that can combine with 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 exhibit a damaged hair (e.g., hair, eyebrows, eyelashes) repair effect.
[0036] In one embodiment, the present inventors screened for peptides comprising amino acid sequences that exhibited excellent binding affinity to structural proteins found in damaged hair (KRT 33B, KRT 85, and KAP 3-1). Based on the top-ranked amino acid sequences from the screened peptide sequences, i) a tripeptide and ii) a tripeptide with a fatty acid covalently bound to the N-terminus were synthesized, and their ability to enhance the structural strength of hair (e.g., hair, eyebrows, and eyelashes) including tensile strength was confirmed. Furthermore, a mixture was prepared by combining iii) the amino acids that comprise the top-ranked tripeptide sequences from the screened peptide sequences, and the amino acid mixture was confirmed to enhance the structural strength of hair (e.g., hair, eyebrows, and eyelashes) including tensile strength.
[0037] Definition of terms
[0038] In the present disclosure, Xaa, Yaa, and Zaa each represent an amino acid.
[0039] In the present 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 the present disclosure, the amino acid sequence of a peptide is written from the left, in order from the N-terminus to the C-terminus. In contrast, the synthesis direction of a synthetic peptide is opposite to the direction in which the peptide sequence is read, that is, from the C-terminus to the N-terminus. The direction in which a peptide sequence is written / read and the direction in which a peptide sequence is synthesized are well known in the art.
[0041] In the present disclosure, the term "strengthening hair" generally includes increasing the strength of hair, preferably including increasing the tensile strength of hair and / or increasing the denaturation enthalpy of hair. In the present disclosure, strengthening hair can include increasing the strength of undamaged hair or damaged hair. Damaged hair can be caused by thermal or chemical treatments (e.g., hair dyeing, perming, bleaching). Damaged hair can be caused by thermal or chemical treatments (e.g., hair dyeing, perming, bleaching) that damage the main structural components of hair. In one embodiment, the composition for strengthening hair can be a composition for increasing the strength and / or elasticity of hair.
[0042] In the present disclosure, the term "protecting hair" generally includes inhibiting hair damage, but is not limited thereto. In the present disclosure, protecting hair preferably includes preventing undamaged hair from being damaged; or preventing damaged hair from being further damaged, but is not limited thereto.
[0043] In the present disclosure, the term "hair" refers to all hair growing on an individual (e.g., including mammals). For example, in the present disclosure, hair may include at least one selected from the group consisting of head hair, eyebrows, eyelashes, and body hair (e.g., chest hair, leg hair), but is not limited thereto. The structure and composition of other types of hair (e.g., eyebrows, eyelashes) present in different parts from head hair are not significantly different from those of 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.). In addition, although the size or shape of hair follicles in the body are different, their basic structure is the same (Jennifer V. Nguyen MD. The Biology, Structure, and Function of Eyebrow Hair. J Drugs Dermatol. 2014; 13(suppl 1): s12-s16.). Therefore, the effects of the peptide or peptide derivative on hair can also be exerted on hair in other parts of the body (eg, eyebrows and / or eyelashes) besides the head.
[0044] In the present 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 present invention, the term "fatty acid" includes saturated or unsaturated fatty acids.
[0045] In the present disclosure, the term "peptide derivative" refers to a peptide in which one or more amino acids of a parent peptide as defined above are chemically modified, or a peptide in which a parent peptide as defined above is modified by the addition of amino acids. For example, in the present disclosure, a peptide derivative can be a peptide as defined above in which any component (e.g., a compound, a fatty acid, an organic acid, etc., such as a C1 to C30 fatty acid, preferably a C15 to C20 fatty acid) is bound to the N-terminus or C-terminus of the parent peptide.
[0046] Peptide or peptide derivative having hair protection effect, damaged hair repair effect or hair strengthening effect
[0047] In one aspect of the present disclosure, a peptide is provided, comprising one or more sequence units consisting of Xaa-Yaa-Zaa:
[0048] The 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);
[0049] The Xaa, Yaa and Zaa are different from each other, wherein when Xaa and Yaa are C and K respectively, Zaa is not L.
[0050] In one implementation example, two of Xaa, Yaa, and Zaa may be C and K, respectively. When Xaa and Yaa are C and K, respectively, Zaa is not L.
[0051] In one implementation example, two of Xaa, Yaa, and Zaa may be C and K, respectively, and the remaining one may be selected from the group consisting of W, V, and F.
[0052] In one implementation example, 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 embodiment, the peptide may be an oligopeptide composed of a plurality of Xaa-Yaa-Zaa sequence units. In this case, the plurality of Xaa-Yaa-Zaa sequence units may be entirely identical, partially identical, or different.
[0055] In one embodiment, 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 example, the peptide may be an oligopeptide composed of 2 to 5, preferably 2 to 4, Xaa-Yaa-Zaa sequence units.
[0057] In one embodiment, the oligopeptide may be a peptide having 3 to 30 amino acids combined, but is not limited thereto. For example, the oligopeptide may be a peptide having 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, 3 or less, 4 or less ... or less, 6 or less, 7 or less, 8 or less, 9 or less, 10 or less, 11 or less, 12 or less, 13 or less, 14 or less, 15 or less, 16 or less, 17 or less, 18 or less, 19 or less, 20 or less, 21 or less, 22 or less, 23 or less, 24 or less, 25 or less, 26 or less, 27 or less, 28 or less, 29 or less, 30 or less, or a combination thereof (e.g., 3 to 24, 3 to 15, 3 to 12) of amino acids.
[0058] In one implementation example, the peptide may be an oligopeptide composed of 2 to 5, preferably 2 to 4, sequence units of Xaa-Yaa-Zaa, and the sequence units constituting the oligopeptide may be all identical, partially identical, or all different.
[0059] In one implementation example, the peptide may be an oligopeptide composed of 2 to 5, preferably 2 to 4, sequence units of Xaa-Yaa-Zaa, and the sequence units constituting the oligopeptide may all be the same. In one implementation example, the peptide may be an oligopeptide composed of 2 to 5, preferably 2 to 4, sequence units of Xaa-Yaa-Zaa, and at least one of the sequence units constituting the oligopeptide may be the same. In one implementation example, the peptide may be an oligopeptide composed of 2 to 5, preferably 2 to 4, sequence units of Xaa-Yaa-Zaa, and the sequence units constituting the oligopeptide may be partially the same. In one implementation example, the peptide may be an oligopeptide composed of 2 to 5, preferably 2 to 4, sequence units of Xaa-Yaa-Zaa, and the sequence units constituting the oligopeptide may all be different.
[0060] In one embodiment, the peptide is an oligopeptide having an amino acid sequence of 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), CWKCWKCWKCWKCWK (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 an embodiment, the peptide (eg, tripeptide or oligopeptide) having the effect of protecting hair, repairing damaged hair, or strengthening hair, especially the tripeptide, is easy to synthesize due to its short sequence length, further providing time and cost advantages.
[0062] In addition, one aspect of the present disclosure provides a peptide derivative in which a fatty acid or an organic acid is bound to the N-terminus of the aforementioned peptide or oligopeptide.
[0063] In the present disclosure, a peptide derivative having a fatty acid or organic acid bound to the N-terminus may be an acylated N-terminus of the peptide. The acylated N-terminus of the peptide may be derived from a fatty acid or an organic acid. In the present disclosure, a peptide derivative having a fatty acid or organic acid bound to the N-terminus may be an acyl derivative of the N-terminus of the peptide.
[0064] In the present disclosure, the term "a fatty acid or an organic acid is bound to the N-terminus of a peptide (or oligopeptide)" may mean that an acyl group derived from a fatty acid or an organic acid is bound to the N-terminus of the peptide (or oligopeptide).
[0065] For example, a fatty acid bound to the N-terminus of a peptide (or oligopeptide) may mean that an acyl group derived from a fatty acid is bound to the N-terminus of the peptide (or oligopeptide). For example, an organic acid bound to the N-terminus of a peptide (or oligopeptide) may mean that an acyl group derived from an organic acid is bound to the N-terminus of the peptide (or oligopeptide).
[0066] That is, one aspect of the present disclosure provides a peptide derivative having a fatty acid or an organic acid bound to the N-terminus of a peptide comprising one or more sequence units consisting of Xaa-Yaa-Zaa: the Xaa, Yaa and Zaa are each independently selected from the group consisting of C, K, W, V, L and F, and the 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 unit, and peptide are the same as those described above, and therefore detailed descriptions thereof are omitted.
[0068] The “binding” of the fatty acid or organic acid to the N-terminus may be covalent binding.
[0069] In one implementation example, the fatty acid may be a C2 to C80 fatty acid.
[0070] In one embodiment, the fatty acid may be a C8 to C30 fatty acid, but is not limited thereto. For example, the fatty acid may 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 may be an acyl group derived from a C8 to C30 fatty acid, but is not limited thereto. For example, the acyl group derived from the fatty acid may be an acyl group derived from 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 acyl group derived from the fatty acid may be an acyl group derived from 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 acyl group derived from the fatty acid may be an acyl group derived from a C15 to C20 fatty acid, preferably an acyl group derived from a C15 to C17 fatty acid.
[0072] Generally, according to the present invention, the fatty acid may be a saturated or unsaturated fatty acid.
[0073] Generally, according to the present invention, the acyl group derived from the fatty acid may 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, hydroxy, amino, amido, sulfate, and sulfide, but is not limited thereto. Preferably, the fatty acid may be substituted with at least one substituent selected from the group consisting of alkyl, alkoxy, hydroxy, 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, hydroxy, amino, acylamino, sulfate, and sulfide, but is not limited thereto. Preferably, the acyl group may be substituted with at least one substituent selected from the group consisting of alkyl, alkoxy, hydroxy, 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), lignoceric acid (C24:0), cerotic acid (C26:0), myristoleic 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 palmitic acid, oleic acid and eicosenoic acid.
[0077] In one embodiment, the acyl group derived from the fatty acid can be selected from the group consisting of 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), lignoceroyl group (C24:0), cerotoyl group (C26:0), myristoleoyl group (C14:1), palmitoleoyl group (C18:0), oleoyl group (C19:1), oleoyl group (C20:0), oleoyl group (C21:0), oleoyl group (C22:0), oleoyl group (C23:0), oleoyl group (C24:0), oleoyl group (C25:0), oleoyl group (C26:0), oleoyl group (C27:0), oleoyl group (C28:0), oleoyl group (C28:0), oleoyl group (C29:0), oleoyl group (C30:0), oleoyl group (C31:0), oleoyl group (C32:0), oleoyl group (C33:0), oleoyl group (C34:0), oleoyl group (C35:0), oleoyl group (C36:0), oleoyl group (C37:0), oleoyl group (C38:0), oleoyl group (C39:0), oleoyl group (C40:1), oleoyl group (C41:1), oleoyl group (C42:0), oleoyl group (C45:0), oleoyl group (C45:0), oleoyl group (C46:0), oleoyl group ( The acyl group derived from the fatty acid may be at least one selected from the group consisting of, but not limited to, a palmitoyl group, a stearoyl group, and an arachidoyl group. In a preferred embodiment, the acyl group derived from the fatty acid may be at least one selected from the group consisting of a palmitoleoyl group, an oleoyl group, and an icosenoyl group.
[0078] In one implementation, the organic acid may be a saturated or unsaturated organic acid.
[0079] In one embodiment, the acyl group derived from the organic acid may 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, hydroxy, amino, amido, sulfate, and sulfide, but is not limited thereto. Preferably, the organic acid may be substituted with at least one substituent selected from the group consisting of alkyl, alkoxy, hydroxy, 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 an alkyl group, an alkoxy group, an aryl group, a hydroxyl group, an amino group, an acylamino group, a sulfate, and a sulfide, but is not limited thereto. Preferably, the acyl group may be substituted with at least one substituent selected from the group consisting of an alkyl group, an alkoxy group, a hydroxyl group, and an amino group.
[0082] In one embodiment, the organic acid may be at least one selected from 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 can be at least one selected from the group consisting of acetyl group, citrl group, formyl group, trifluoroacetyl group, succinyl group, galloyl group, and lactyl group, but is not limited thereto.
[0084] In one embodiment, the peptide derivative may be a tripeptide composed of one Xaa-Yaa-Zaa sequence unit, the N-terminus of which is bound to a fatty acid or an organic acid. In one embodiment, the peptide derivative may be a tripeptide composed of one Xaa-Yaa-Zaa sequence unit, the N-terminus of which is bound to an acyl group derived from a fatty acid or an 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, the N-terminus of which is bound to a fatty acid or an organic acid. In this case, the sequence units constituting the oligopeptide may all be identical. In one embodiment, the peptide derivative may be an oligopeptide composed of 2 to 5, preferably 2 to 4, Xaa-Yaa-Zaa sequence units, the N-terminus of which is bound to an acyl group derived from a fatty acid or an organic acid. In this case, the sequence units constituting the oligopeptide may all be 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, the N-terminus of which is bound to a fatty acid or an organic acid. In this case, the sequence units constituting the oligopeptide may be partially identical. In one embodiment, the peptide derivative may be an oligopeptide composed of 2 to 5, preferably 2 to 4, Xaa-Yaa-Zaa sequence units, the N-terminus of which is bound to an acyl group derived from a fatty acid or an 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, the N-terminus of which is bound to a fatty acid or an organic acid. In this case, the sequence units constituting the oligopeptide may all be different. In one embodiment, the peptide derivative may be an oligopeptide composed of 2 to 5, preferably 2 to 4, Xaa-Yaa-Zaa sequence units, the N-terminus of which is bound to an acyl group derived from a fatty acid or an organic acid. In this case, the sequence units constituting the oligopeptide may all be different.
[0088] In one embodiment, the peptide derivative may be an amino acid sequence of CWK, CKF, or KCV with a fatty acid or organic acid bound to the N-terminus. In another embodiment, the peptide derivative may be an amino acid sequence of CWK, CKF, or KCV with an acyl group derived from a fatty acid or organic acid bound to the N-terminus. In another embodiment, the peptide derivative may be an amino acid sequence of CWK, CKF, or KCV with an acyl group derived from a fatty acid or organic acid bound to the N-terminus. In another example, the peptide derivative may be an amino acid sequence of CWK, CKF, or KCV with a palmitic acid bound to the N-terminus. In another example, the peptide derivative may be palmitoyl-CWK, palmitoyl-CKF, or palmitoyl-KCV. In another example, the peptide derivative may be CWK, CKF, or KCV with a palmitoyl group bound to the N-terminus.
[0089] According to one embodiment, by binding the N-terminus of the peptide to a fatty acid or an 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 be adsorbed on) at least one selected from the group consisting of the cuticle layer, cortex layer, and CMC layer of hair (e.g., hair, eyebrows, and eyelashes). In one embodiment, the peptide or peptide derivative according to one aspect of the present disclosure can bind to (or be adsorbed on) a structural protein found in damaged hair (e.g., hair, eyebrows, and eyelashes).
[0091] In one implementation, the peptide or peptide derivative according to one aspect of the present disclosure can increase the tensile strength of hair (eg, hair, eyebrows, eyelashes).
[0092] In one embodiment, the peptide or peptide derivative according to one aspect of the present disclosure can increase the denaturation enthalpy of hair (eg, 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 be bound to (or adsorbed on) the cuticle layer, cortex layer 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 the present disclosure can repair damage to the CMC structure in damaged hair (e.g., hair, eyebrows, eyelashes), and ultimately improve the hardness, smoothness, and elasticity of the damaged hair (e.g., hair, eyebrows, eyelashes).
[0095] Composition for protecting hair, repairing damaged hair or strengthening hair
[0096] One aspect of the present disclosure provides a composition for protecting hair, repairing damaged hair, or strengthening hair, comprising the aforementioned peptide, peptide derivative, or amino acid mixture.
[0097] In one embodiment, the hair protection, damaged hair repair, or hair strengthening composition according to one aspect of the present disclosure can be bound to (or adsorbed on) at least one component selected from the group consisting of the hair cuticle, the hair cortex, and the CMC layer of the hair. In one embodiment, the hair protection, damaged hair repair, or hair strengthening composition according to one aspect of the present disclosure can be bound to (or adsorbed on) a structural protein found in damaged hair.
[0098] In one implementation, the composition for protecting hair, repairing damaged hair, or strengthening hair according to one aspect of the present disclosure can increase the tensile strength of hair.
[0099] In one implementation, the composition for protecting hair, repairing damaged hair, or strengthening hair according to one aspect of the present disclosure can increase the denaturation enthalpy of hair.
[0100] In one embodiment, the composition for protecting hair, repairing damaged hair or strengthening hair according to one aspect of the present disclosure can be combined with (or adsorbed on) the hair cuticle layer, hair cortex and / or cell membrane complex layer of the hair, thereby improving the smoothness and elasticity of the surface.
[0101] In one embodiment, the composition for protecting hair, repairing damaged hair, or strengthening hair according to one aspect of the present disclosure can repair damage to the CMC structure in damaged hair, and ultimately improve the hardness, smoothness, and elasticity of the damaged hair.
[0102] In one implementation, the composition for protecting hair, repairing damaged hair, or strengthening hair according to one aspect of the present disclosure may be a composition for protecting hair, repairing damaged hair, or strengthening hair.
[0103] In one implementation, the composition for protecting hair, repairing damaged hair, or strengthening hair according to one aspect of the present disclosure may be a composition for protecting eyebrows, repairing damaged eyebrows, or strengthening eyebrows.
[0104] In one implementation, the composition for protecting hair, repairing damaged hair, or strengthening hair according to one aspect of the present disclosure may be a composition for protecting eyelashes, repairing damaged eyelashes, or strengthening eyelashes.
[0105] 1) Composition for protecting hair, repairing damaged hair or strengthening hair-1
[0106] One aspect of the present disclosure provides a composition for protecting hair, repairing damaged hair, or strengthening hair, comprising the aforementioned peptide or peptide derivative.
[0107] The peptide and peptide derivative are the same as those described above, and therefore detailed descriptions are omitted.
[0108] In one embodiment, the peptide or peptide derivative may contain 0.0001 wt % to 100 wt % or less relative to the total weight of the composition, but is not limited thereto. For example, the peptide or peptide derivative may contain 0.0001% by weight or more, 0.001% by weight or more, 0.005% by weight or more, 0.01% by weight or more, 0.05% by weight or more, 0.1% by weight or more, 0.5% by weight or more, 1% by weight or more, 5% by weight or more, 10% by weight or more, 15% by weight or more, 20% by weight or more, 25% by weight or more, 30% by weight or more, 35% by weight or more, 40% by weight or more, 45% by weight or more, 50% by weight or more, 55% by weight or more, 60% by weight or more, 65% by weight or more, 70% by weight or more, 75% by weight or more, 80% by weight or more, 85% by weight or more, 90% by weight or more, 95% by weight or more, 99% by weight or more, 100% by weight or more, 0.0001% by weight of the total weight of the composition. % or less, 0.001 wt % or less, 0.005 wt % or less, 0.01 wt % or less, 0.05 wt % or less, 0.1 wt % or less, 0.5 wt % or less, 1 wt % or less, 5 wt % or less, 10 wt % or less, 15 wt % or less, 20 wt % or less, 25 wt % or less, 30 wt % or less, 35 wt % or less, 40 wt % or less, 45 wt % or less, 50 wt % or less, 55 wt % or less, 60 wt % or less, 65 wt % or less, 70 wt % or less, 75 wt % or less, 80 wt % or less, 85 wt % or less, 90 wt % or less, 95 wt % or less, 99 wt % or less, 100 wt % or less, or a combination 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% by weight or more, 60% by weight or more, 70% by weight or more, 80% by weight or more, 90% by weight or more, 95% by weight or more, 99% by weight or more, or 100% by weight relative to the total weight of the composition, wherein the peptide or oligopeptide or its derivative is composed of 2 to 5, preferably 2 to 4, sequence units of Xaa-Yaa-Zaa, wherein preferably, two of Xaa, Yaa and Zaa may be C and K, respectively, wherein when Xaa and Yaa are C and K, respectively, Zaa may not be L, more preferably, two of Xaa, Yaa and Zaa may be C and K, respectively, and the remaining one may be selected from the group consisting of W, V and F, more preferably, the peptide is a tripeptide composed of one sequence unit, wherein the peptide is CKF, CWK or KCV.
[0110] In a preferred embodiment, the peptide present in the aforementioned amount is the 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), CWKCWKCWKCWKCWK (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 bound to the N-terminus of the disclosed peptide, among which a C15 to C20 fatty acid is more preferred, a C15 to C17 fatty acid is further preferred, and a palmitic acid and / or palmitoleic acid fatty acid derivative is most preferred.
[0111] Preferably, the peptide derivative having a fatty acid bound to the N-terminus of the disclosed peptide is a peptide derivative having an acyl group derived from 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 bound to the N-terminus of the disclosed peptide, among which an acyl group derived from a C15 to C20 fatty acid is more preferred, an acyl group derived from a C15 to C17 fatty acid is further preferred, and an acyl group derived from palmitic acid and / or palmitoleic acid is most preferred.
[0112] In one embodiment, the peptide or peptide derivative can be administered to the hair of the subject in an amount of 0.1 to 100 mg per 1 g of hair, but is not limited thereto. For example, the peptide or peptide derivative can be administered to the hair of the subject in an amount of 0.1 mg or more, 1 mg or more, 2 mg or more, 3 mg or more, 4 mg or more, 5 mg or more, 6 mg or more, 7 mg or more, 8 mg or more, 9 mg or more, 10 mg or more, 11 mg or less, 12 mg or less, 13 mg or less, 14 mg or less, 15 mg or less, 16 mg or less, 17 mg or less, 18 mg or less, 19 mg or less, 20 mg or less, 30 mg or less, 40 mg or less, 50 mg or less, 60 mg or less, 70 mg or less, 80 mg or less, 90 mg or less, 100 mg or less, or a combination thereof (e.g., 1 to 20 mg, 9 to 11 mg) per 1 g of hair, but is not limited thereto.
[0113] In a preferred embodiment, the peptide or peptide derivative may be administered to the hair of the subject in an amount of 5 to 20 mg or 9 to 15 mg.
[0114] In one embodiment, 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 component that has the effect of protecting hair, repairing damaged hair, or strengthening hair, but is not limited thereto.
[0116] In one embodiment, the composition for protecting hair, repairing damaged hair, 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 composition for protecting hair, repairing damaged hair, or strengthening hair can be formulated as at least one selected from the group consisting of shampoo, conditioner, hair lotion, hair cream, hair oil, hair milk, hair mask, hair nutrient solution, hair spray, hair treatment cream, essence, hair essence lotion, hair gel, hair wax, hair essence, hair spray, eyebrow nutrient, eyebrow essence, eyelash nutrient, and eyelash essence, but is not limited thereto.
[0118] In one embodiment, the composition for protecting hair, repairing damaged hair or strengthening hair can be a wash-off type (a rinse-off type, such as shampoo) or a leave-in type (a non-rinsing type, such as hair essence), but is not limited thereto.
[0119] The composition for protecting hair, repairing damaged hair, or strengthening hair according to one aspect of the present disclosure may further include ingredients that can be included in cosmetics.
[0120] The composition for protecting hair, repairing damaged hair or strengthening hair according to one aspect of the present disclosure may further include additives such as preservatives, thickeners, viscosity regulators, stabilizers, pearlescent agents, metal ion blocking agents, cationic surfactants, pH regulators, fragrances and dyes, which can be easily purchased commercially for use.
[0121] In one implementation, the hair may include hair, eyebrows, and / or eyelashes, but is not limited thereto.
[0122] 2) Composition for protecting hair, repairing damaged hair or strengthening hair-2
[0123] In addition, one aspect of the present disclosure provides a composition for protecting hair, repairing damaged hair, or strengthening hair, comprising at least three amino acids selected from the group consisting of C, K, W, V, L (Leu, leucine), and F.
[0124] The application (cosmetic, pharmaceutical, or external use composition) and dosage form of the composition, as well as additives that can be added to the composition, are the same as those described in the aforementioned "1) Composition for protecting hair, repairing damaged hair, or strengthening hair - 1", and therefore detailed descriptions are omitted.
[0125] The composition comprising at least three amino acids according to one aspect of the present disclosure can protect hair, repair damaged hair, or strengthen hair without requiring a peptide synthesis process. Therefore, using the composition comprising at least three amino acids according to one aspect of the present disclosure for protecting hair, repairing damaged hair, or strengthening hair is economically advantageous.
[0126] In one implementation example, the at least three amino acids may be contained in an amount of 0.0001 wt % to 100 wt % or less relative to the total weight of the composition, but is not limited thereto. For example, the at least three amino acids may comprise 0.0001% by weight or more, 0.001% by weight or more, 0.005% by weight or more, 0.01% by weight or more, 0.05% by weight or more, 0.1% by weight or more, 0.5% by weight or more, 1% by weight or more, 5% by weight or more, 10% by weight or more, 15% by weight or more, 20% by weight or more, 25% by weight or more, 30% by weight or more, 35% by weight or more, 40% by weight or more, 45% by weight or more, 50% by weight or more, 55% by weight or more, 60% by weight or more, 65% by weight or more, 70% by weight or more, 75% by weight or more, 80% by weight or more, 85% by weight or more, 90% by weight or more, 95% by weight or more, 99% by weight or more, 100% by weight or more, 0.0001% by weight of the total weight of the composition. % or less, 0.001 wt % or less, 0.005 wt % or less, 0.01 wt % or less, 0.05 wt % or less, 0.1 wt % or less, 0.5 wt % or less, 1 wt % or less, 5 wt % or less, 10 wt % or less, 15 wt % or less, 20 wt % or less, 25 wt % or less, 30 wt % or less, 35 wt % or less, 40 wt % or less, 45 wt % or less, 50 wt % or less, 55 wt % or less, 60 wt % or less, 65 wt % or less, 70 wt % or less, 75 wt % or less, 80 wt % or less, 85 wt % or less, 90 wt % or less, 95 wt % or less, 99 wt % or less, 100 wt % or less, or a combination thereof (e.g., 0.005 to 0.05 wt %, 0.05 to 0.5 wt %), but not limited thereto).
[0127] In a preferred embodiment, the at least three amino acids may be contained in an amount of 0.005 to 0.5 wt % or 0.05 to 0.5 wt %.
[0128] In one embodiment, the composition may include C; K; and one of W, V, L, or F.
[0129] In one implementation, 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 C, K, W, V, L, and F can effectively improve hair strength compared to a composition 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 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, 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, the hair may include hair, eyebrows, and / or eyelashes, but is not limited thereto.
[0133] Methods for protecting hair, repairing damaged hair or strengthening hair
[0134] In one aspect of the present disclosure, a method for protecting hair, repairing damaged hair or strengthening hair is provided, comprising the step of applying the aforementioned peptide, peptide derivative or amino acid mixture.
[0135] In one implementation, the method for protecting hair, repairing damaged hair, or strengthening hair according to one aspect of the present disclosure can increase the tensile strength of hair.
[0136] In one implementation, the method for protecting hair, repairing damaged hair, or strengthening hair according to one aspect of the present disclosure can increase the denaturation enthalpy of hair.
[0137] In one implementation, the method for protecting hair, repairing damaged hair, or strengthening hair according to one aspect of the present disclosure can repair damage to the CMC structure in damaged hair, and ultimately improve the hardness, smoothness, and elasticity of the damaged hair.
[0138] In one implementation, the method for protecting hair, 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 hair, repairing damaged hair, or strengthening hair according to one aspect of the present disclosure may be a method for protecting eyebrows, repairing damaged eyebrows, or strengthening eyebrows.
[0140] In one implementation, the method for protecting hair, repairing damaged hair, or strengthening hair according to one aspect of the present disclosure may be a method for protecting eyelashes, repairing damaged eyelashes, or strengthening eyelashes.
[0141] 1) Methods for protecting hair, repairing damaged hair or strengthening hair-1
[0142] In one aspect of the present disclosure, a method for protecting hair, repairing damaged hair or strengthening hair is provided, comprising the step of administering an effective amount of the aforementioned peptide or peptide derivative to a subject in need of protecting hair, repairing damaged hair or strengthening hair.
[0143] The peptide and peptide derivative are the same as those described above, and therefore detailed descriptions are omitted.
[0144] In one embodiment, the subject may be an animal including mammals (eg, humans), but is not limited thereto.
[0145] In one embodiment, the subject can be an individual with damaged hair or an individual with undamaged hair. In one embodiment, the subject can be an individual whose CMC structure of hair is damaged due to hair damage.
[0146] In the present disclosure, administration may be oral administration, transdermal administration, subcutaneous administration, intravenous administration, intraperitoneal administration, intramuscular administration, or topical application, but is not limited thereto. Preferably, topical application may include applying an effective amount of the aforementioned peptide or peptide derivative to the hair.
[0147] In one embodiment, the daily dosage of the active ingredient can be 0.0001 to 10,000 mg / kg, but is not limited thereto. In one embodiment, the active ingredient can be administered once or in multiple doses per day. However, it should be understood that the dosage of the active ingredient should be determined based on multiple factors such as the route of administration, the age, sex, and weight of the subject, and therefore, the dosage does not limit the scope of the present invention in any way.
[0148] In one embodiment, the peptide or peptide derivative can be administered to the subject's hair in an amount of 0.1 to 100 mg per 1 g of hair, but is not limited thereto. For example, the peptide or peptide derivative can be administered to the subject's hair in an amount of 0.1 mg or more, 1 mg or more, 2 mg or more, 3 mg or more, 4 mg or more, 5 mg or more, 6 mg or more, 7 mg or more, 8 mg or more, 9 mg or more, 10 mg or more, 11 mg or less, 12 mg or less, 13 mg or less, 14 mg or less, 15 mg or less, 16 mg or less, 17 mg or less, 18 mg or less, 19 mg or less, 20 mg or less, 30 mg or less, 40 mg or less, 50 mg or less, 60 mg or less, 70 mg or less, 80 mg or less, 90 mg or less, 100 mg or less, or a combination thereof (e.g., 1 to 20 mg, 9 to 11 mg) per 1 g of hair, but is not limited thereto.
[0149] In a preferred embodiment, the peptide or peptide derivative can be administered to the hair of the subject in an amount of 5 mg to 50 mg, 10 mg to 40 mg, or 15 mg to 30 mg.
[0150] In one embodiment, the peptide or peptide derivative may be administered to a 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 component that has the effect of protecting hair, repairing damaged hair, or strengthening hair, but is not limited thereto.
[0152] In one implementation, the hair may include hair, eyebrows, and / or eyelashes, but is not limited thereto.
[0153] 2) Methods for protecting hair, repairing damaged hair or strengthening hair-2
[0154] In addition, one aspect of the present disclosure provides a method for protecting, repairing damaged hair, or strengthening hair, comprising the step of administering 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 in need of hair protection, damaged hair repair, or hair strengthening.
[0155] The subjects, administration, administration amount, etc. are the same as those in the aforementioned "1) Method 1 for protecting hair, repairing damaged hair, or strengthening hair, so detailed description is omitted.
[0156] In one embodiment, the step of administering a combination of at least three amino acids as an active ingredient to a subject may include administering a combination of C; K; and one of W, V, L, or F to the subject as an active ingredient. In one embodiment, the step of administering a combination of at least three amino acids as an active ingredient to a subject may include administering a combination of C, K, and W to the subject as an active ingredient.
[0157] In one embodiment, the step of administering a combination of at least three amino acids as an active ingredient to a subject may be administering a composition comprising at least three amino acids of C, K, W, V, L, and F to a subject as an active ingredient. In one embodiment, the step of administering a combination of at least three amino acids as an active ingredient to a subject may be administering a composition comprising C; K; and one of W, V, L, or F to a subject as an active ingredient. In one embodiment, the step of administering a combination of at least three amino acids as an active ingredient to a subject may be administering a composition comprising C, K, and W to a subject as an active ingredient.
[0158] In one embodiment, i) C; ii) K; and iii) one of W, V, L, or F may be administered to the subject at a molar mass ratio of 1:0.1 to 5:0.1 to 5, but is not limited thereto. For example, i) C; ii) K; and iii) one of W, V, L, or F can be administered to a 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 embodiment, a combination of at least three amino acids selected from the group consisting of C, K, W, V, L, and F can be administered to a subject once or multiple times, but is not limited thereto.
[0160] In one embodiment, 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 component that has a hair protection effect, a damaged hair repair effect, or a hair strengthening effect, but is not limited thereto.
[0161] In one implementation, the hair may include hair, eyebrows, and / or eyelashes, but is not limited thereto.
[0162] Use of compositions comprising peptides, peptide derivatives or amino acids
[0163] In one aspect of the present disclosure, there is provided a use of a composition comprising the aforementioned peptide, peptide derivative or amino acid mixture.
[0164] 1) Use of peptides or peptide derivatives-1
[0165] One aspect of the present disclosure provides a use of the aforementioned peptide for protecting hair, repairing damaged hair, or strengthening hair.
[0166] One aspect of the present disclosure provides a use of the aforementioned peptide derivative for protecting hair, repairing damaged hair, or strengthening hair.
[0167] One aspect of the present disclosure provides a use of the aforementioned peptide for preparing a composition for protecting hair, repairing damaged hair, or strengthening hair.
[0168] One aspect of the present disclosure provides a use of the aforementioned peptide derivative for preparing a composition for protecting hair, repairing damaged hair, or strengthening hair.
[0169] The peptide and peptide derivative are the same as those described above, and therefore detailed descriptions are omitted.
[0170] In one embodiment, the use can be therapeutic or non-therapeutic.
[0171] In one implementation, the hair may include hair, eyebrows, and / or eyelashes, but is not limited thereto.
[0172] 2) Use of the composition comprising amino acids-2
[0173] One aspect of the present disclosure provides 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 hair, repairing damaged hair, or strengthening hair.
[0174] One aspect of the present disclosure provides 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 hair, repairing damaged hair, or strengthening hair.
[0175] The composition comprising at least three amino acids selected from the group consisting of C, K, W, V, L, and F is the same as described above, and thus a detailed description thereof is omitted.
[0176] In one implementation, the hair may include hair, eyebrows, and / or eyelashes, but is not limited thereto.
[0177] The present invention will be described in detail below by way of examples. The following examples are provided for the purpose of illustration only in order to facilitate understanding of the present invention, and the category and scope of the present invention are not limited thereto.
[0178] Experimental Example 1. Construction of candidate tripeptide sequences and determination of their binding ability to hair
[0179] After constructing multiple candidate tripeptide sequences composed of arbitrary amino acid sequences, their binding affinity to hair was determined through three-dimensional molecular docking simulations. Tripeptide sequences with excellent binding were selected by predicting sequences that exhibited superior hair protection, damaged hair repair, or hair strengthening effects.
[0180] Specifically, the 20 essential amino acids suitable for hair application are divided into three groups. Group 1 (C) includes cysteine (Cys, C), a sequence effective for disulfide bonding in hair. Group 2 (HPO) includes alanine (Ala, A), leucine (Leu, L), phenylalanine (Phe, F), proline (Pro, P), valine (Val, V), and tryptophan (Trp, W), a sequence excellent for hair penetration. Group 3 (POS) consists of sequences that contribute to improving hair tensile strength and includes the cationic amino acids arginine (Arg, R), lysine (Lys, K), and histidine (His, H). According to the amino acid arrangement patterns (nine cases) shown in Table 1 below, the amino acids in these three groups (Group 1 (C), Group 2 (HPO), and / or Group 3 (POS)) can be arranged in the first, second, and third order, respectively, to construct candidate tripeptide sequences with various sequence combinations. In Table 1, "amino acid number" indicates the number of amino acids that can be placed at positions 1, 2, and 3. Finally, a total of 216 candidate tripeptide sequences were calculated as one-letter codes (represented by letters) for amino acids (see Table 1).
[0181]
Table 1
[0182]
[0183]
[0184] After the calculated one-letter codes were sequentially input into an Excel file based on rows, the calculated one-letter codes were unified into a three-dimensional peptide molecule file (*.sd or *.sdf) including atomic coordinate information using DS software.
[0185] To calculate the binding forces of the calculated three-dimensional peptide molecular files, three three-dimensional molecular files (*.pdb) of hair keratin, the binding target, were obtained from AlphaFold (alphafold.ebi.ac.uk). Specifically, the three-dimensional molecular files (*.pdb) used were those for keratin 85 (Uniprot code: P78386), keratin 33b (Uniprot code: Q14525), and keratin-associated protein 3-1 (Uniprot code: Q9BYR8).
[0186] Use the CDocker module of Discovery Studio (DS) software, according to Figure 1 The binding energy between the three-dimensional peptide molecule file and the binding regions of the three keratin proteins was calculated using the following conditions. The lower the binding energy, the stronger the binding force.
[0187] The results showed that among the 216 candidate tripeptide sequences, those with binding energies below -50 kcal / mol for the three keratin proteins included CKF, CKW, CWK, KCF, KCL, and KCV. Meanwhile, PCP was the tripeptide with the weakest binding force, with a binding energy above 0 kcal / mol.
[0188] Experimental Example 2. Evaluation of the efficacy of amino acid combinations
[0189] First, the amino acid components constituting the top-ranked tripeptide identified in Experimental Example 1 above were mixed to prepare a mixture. Specifically, the amino acid components constituting the top-ranked tripeptide CWK were mixed according to the molar mass ratios shown in Table 2 below to prepare a mixture (Example 1) (Refer to Table 2). For comparison, the amino acid components constituting the bottom-ranked tripeptide CPP were mixed according to the molar mass ratios shown in Table 2 below to prepare a mixture (Comparative Example 1). The numerical 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 respectively, and the tensile strength was compared.
[0194] Specifically, prepare a bleached hair tress (1 g, manufactured by Beaulax). Wash the tress with a standard non-conditioning shampoo, rinse for 1 minute, and dry for 2 minutes. Soak the dried hair tress (1 g) in 100 g of a solution containing a 0.1% by weight test substance (the mixture of Example 1 or the mixture of Comparative Example 1 in Table 2 above) (in this case, the test substance (0.1% by weight) dissolved in purified water (the remainder)) for approximately 30 minutes. Rinse the soaked hair tress with running water for 1 minute and then air dry for at least 12 hours. Randomly select 30 hairs from each test substance-treated hair tress. Randomly select 30 hairs from a control group of hair tresses 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 the tensile strength of hair treated with the amino acid mixture that constitutes the tripeptide of CWK increased significantly compared to bleached hair strands (ref. Figure 2 : Figure 2 In the table, "Blank" indicates the control group hair that was not treated with the test substance, "CWKaminomix" indicates the hair that was treated with the mixture of Example 1, and "CPPaminomix" indicates the hair that was treated with the mixture of Comparative Example 1). Figure 2 In the graph, the y-axis is the tensile strength (break load) in gmf.
[0196] (2) Determination of enthalpy of change
[0197] Using a DSC (Differential Scanning Calorimetry) analyzer, the denaturation enthalpy of hair structural proteins was compared between treated and untreated subjects. DSC is used as an analytical method to determine the stability of hair structural proteins. The greater the damage to the hair, the less stable the hair structural proteins, resulting in a lower denaturation enthalpy.
[0198] Specifically, a bleached hair tress (1 g, manufactured by Beaulax) was prepared. The tress was washed with a standard non-conditioning shampoo, rinsed for 1 minute, and dried for 2 minutes. The dried hair tress (1 g) was immersed in 100 g of a solution containing a 0.01 wt% test substance (the mixture from Example 1 in Table 2 above) (in this case, the solution consisted of the mixture from Example 1 (0.01 wt%) dissolved in purified water (the remainder) and ethanol (80 wt%)) for 30 minutes. The immersed hair tress was rinsed with running water for 1 minute and then naturally dried for at least 12 hours. Each treated hair tress was cut into 1 mm pieces and combined with 3-5 mg and 6-15 mg of distilled water in an aluminum autoclave. The mixture was allowed to stand for at least 12 hours to achieve phase equilibrium within the autoclave, thereby preparing the sample for DSC measurement (DSC sample). The denaturation enthalpy of the prepared DSC sample was measured using a DSC (Discovery DSC 250, TA Instruments) device (50-190 degrees, 10 degrees / min).
[0199] The results showed that the denaturation enthalpy of hair structural proteins in hair treated with the amino acid mixture of the tripeptide constituting the CWK sequence increased significantly compared to the control hair (refer to Figure 3 ; Figure 3 Here, "bleach" represents the control hair that was not treated with the test substance, and "aminomix" represents the hair that was treated with the mixture of Example 1).
[0200] Experimental Example 3. Evaluation of the efficacy of tripeptide-1
[0201] Among the tripeptides calculated in Experimental Example 1 above, peptides with the sequences of 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, a total of three amino acids were added in the form of a single amino acid Fmoc (fluorenylmethoxycarbonyl protecting group)-amino acid-OH for coupling (Step 2). A cleavage solution was added to the coupled material to precipitate the peptide for recovery.
[0202] (1) Determination of tensile strength
[0203] The test substances (the above five tripeptides) were applied to the hair in the same manner as in "Experimental Example 2. (1) Measurement of tensile strength" and the tensile strength was compared.
[0204] Specifically, a bleached hair tress (1 g, manufactured by Beaulax) was prepared. The tress was washed with a standard non-conditioning shampoo, rinsed for 1 minute, and dried for 2 minutes. The dried hair tress (1 g) was immersed in 100 g of a 0.01% by weight solution of a test substance (synthetic tripeptide) (in this case, the solution consisted of the test substance (0.01% by weight) dissolved in purified water (the remainder) and ethanol (80% by weight)) for approximately 30 minutes. The immersed hair tress was rinsed with running water for 1 minute and then naturally dried for at least 12 hours. Thirty hairs were randomly selected from each hair tress treated with the test substance. Thirty hairs were randomly selected from a control group of hair tresses not treated with the test substance. The tensile strength of each selected hair was measured using an MTT175 (manufactured by DiaStron).
[0205] The results showed that the tensile strength of hair treated with CKF, CWK, KCL and KCV was significantly increased compared to the bleached hair bundles used as the control group. On the other hand, the tensile strength of hair treated with PCP was not significantly increased (refer to Figure 4 ; Figure 4 In the table, “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 enthalpy of change
[0207] The measurement was performed by the same method as in "Experimental Example 2. (2) Measurement of denaturation enthalpy", and CWK tripeptide was applied to the hair as a test substance to compare the denaturation enthalpy.
[0208] The results showed that the denaturation enthalpy of hair structural proteins in hair treated with CWK tripeptide was significantly increased compared with the control group (reference Figure 3 ; Figure 3 In the figure, "bleach" indicates the control hair that was not treated with the test substance, and "CWK" indicates the hair that was treated with CWK tripeptide).
[0209] Experimental Example 4. Evaluation of the efficacy of tripeptides with fatty acids bound to the N-terminus
[0210] (1) Determination of binding strength with keratin
[0211] Palmitic acid was added to the sequences of the four tripeptides (CKF, CWK, KCL, and KCV) whose effects were confirmed in "Experimental Example 3" to generate a molecular file. Then, a molecular docking simulation was performed under the same conditions as in Experimental Example 1 above to measure the binding energy of the tripeptides added with palmitic acid to the three keratins.
[0212] The results showed that the tripeptide with added palmitic acid had lower binding capacity to the three types of keratin than the tripeptide without added palmitic acid. This confirms that the tripeptide with added palmitic acid has a stronger binding capacity to hair.
[0213] (2) Determination of tensile strength
[0214] Among the tripeptides whose effects were confirmed in "Experimental Example 4. (1) Measurement of binding strength to keratin," palmitic acid was covalently bound to three tripeptides (CKF, CWK, and KCV), and then the tensile strength was measured.
[0215] Specifically, a tripeptide was synthesized using the same method as the peptide synthesis method described 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), at room temperature for 1 hour, concentration 0.3 M) to synthesize a tripeptide with palmitic acid covalently bound 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 (tripeptide with palmitic acid covalently bound to the N-terminus) was applied to the 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 the control group (refer to Figure 5 ;exist Figure 5In the table, "aminomix" indicates hair treated with the mixture of Example 1 in Table 2, "Con" indicates control hair not treated with the test substance, "CWK" indicates hair treated with the CWK tripeptide, "pal-CKF" indicates hair treated with CKF having palmitic acid covalently bound to the N-terminus (palmitoyl-CKF), "pal-CWK" indicates hair treated with CWK having palmitic acid covalently bound to the N-terminus (palmitoyl-CWK), "pal-KCV" indicates hair treated with KCV having palmitic acid covalently bound to the N-terminus (palmitoyl-KCV), and "palmitic acid" indicates hair treated with palmitic acid. Furthermore, hair treated with the tripeptide having palmitic acid covalently bound to the N-terminus exhibited higher tensile strength than hair treated with the tripeptide not having palmitic acid covalently bound to the N-terminus or hair treated with the amino acid mixture.
[0217] (3) Determination of enthalpy of change
[0218] The measurement was performed using the same method as in "Experimental Example 2. (2) Measurement of denaturation enthalpy." A tripeptide having palmitic acid covalently bonded to the N-terminus (i.e., palmitoyl tripeptide) was applied to the hair as a test substance, and the denaturation enthalpy was compared.
[0219] The results showed that the denaturation enthalpy of hair structural proteins was significantly increased in hair treated with a tripeptide covalently bound to palmitic acid at the N-terminus compared to the control hair (refer to Figure 3 ;exist Figure 3 In the table, “palmitic acid” indicates hair treated with palmitic acid, “pal-CWK” indicates hair treated with CWK having palmitic acid covalently bound to the N-terminus (palmitoyl-CWK), “pal-KCV” indicates hair treated with KCV having palmitic acid covalently bound to the N-terminus (palmitoyl-KCV), and “pal-CKF” indicates hair treated with CKF having palmitic acid covalently bound to the N-terminus (palmitoyl-CKF).
[0220] (4) Confirmation of penetration and binding effects in hair using confocal microscopy
[0221] Palmitoyl-CWK, a tripeptide with palmitic acid covalently bound to its N-terminus (i.e., palmitoyl tripeptide), was conjugated (fluorescently labeled) with a green fluorescent substance (FITC; fluorescein isothiocyanate) and applied to the hair. The colored areas were then compared using a confocal microscope to examine changes in hair structure that affect increases in hair tensile strength.
[0222] The results show that Figure 6As shown, the hair cuticle, hair cortex and CMC parts are shown in green ( Figure 6 It is shown in gray in the figure), which confirms that palmitoyl tripeptide is strongly bound to the hair cuticle, hair cortex and CMC (reference Figure 6 (left photo; gray). This result showed a tendency similar to that of applying Nile Red, a fat-soluble fluorescent substance, to hair (refer to Figure 6 right photo; gray).
[0223] On the other hand, in order to compare the hair penetration path, 5-(4-Dimethylaminobenzylidene) rhodanine, a water-soluble fluorescent substance, was applied to the hair, and the coloring site (in Figure 7 The results show that, if Figure 7 As shown, the water-soluble fluorescent substance hardly remains in the cuticle on the surface of the hair and does not fill the missing parts of CMC inside the hair (reference Figure 7 ;grey).
[0224] The experimental results show that palmitoyl tripeptide targets CMC in hair through a penetration path different from that of water-soluble substances, thereby improving the structural function of hair.
[0225] Experimental Example 5. Evaluation of the efficacy of oligopeptides combining tripeptide sequences
[0226] Among the tripeptide sequences ranked highly for binding affinity in Experimental Example 1 above, three-dimensional molecular files (molecular structure files) were generated for i) a single sequence repeating oligopeptide (12mer; AP 3mer*4 (repeat; for example, CWKCWKCWKCWK (SEQ ID NO: 6)) and ii) an oligopeptide comprising any combination of two or more sequences (12mer; AP 3mer*4 (random)). The binding affinity of each generated peptide molecular file to hair was measured. Three-dimensional molecular files of the test peptides were generated using the same methods and conditions as in Experimental Example 1 above. Molecular docking simulations were performed using the generated molecular files to measure the binding affinity to hair.
[0227] For comparison, molecular files of known peptides from other companies or similar peptides were generated and their binding ability to hair was confirmed (reference Figure 8Specifically, (a) the amino acids (arginine, cysteine, and glycine) known to constitute the well-known tetrapeptide-97 (Caregen; INCI Full Monograph ID: 37801) were randomly combined to generate molecular files for all possible tetrapeptides. The hair binding ability of each of the generated tetrapeptide molecular files was then measured. Furthermore, (b) the amino acids (cysteine, glycine, isoleucine, phenylalanine, serine, threonine, and valine) known to constitute the well-known oligopeptide sh-Oligopeptide-78 (INCI Full Monograph ID: 28756) were randomly combined to generate molecular files for all possible oligopeptides (a total of 13 amino acids). Furthermore, (c) molecular files were generated for 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), and GGVCGPSPPCITT (KP; SEQ ID NO: 17). The hair-binding abilities of all the oligopeptides generated as molecular files in (b) and (c) above were then measured.
[0228] exist Figure 8 In the molecule file, "CG 4mer" is the peptide that exhibited the highest binding affinity among all tetrapeptides generated as a molecule file in (a) above. "CG 4mer*3" is an oligopeptide (12 amino acids in total) obtained by repeating the sequence of the peptide that exhibited the highest binding affinity among all tetrapeptides generated as a molecule file in (a) above three times. "K18 (13mer)" is the peptide that exhibited the highest binding affinity among all oligopeptides generated as molecule files in (b) and (c) above. "AP 3mer" is the peptide that exhibited the highest binding affinity among the tripeptide candidate sequences in Experimental Example 1 above. "AP 3mer-Pal" is the peptide that exhibited the highest binding affinity to hair among the molecule files of the tripeptide candidate sequences in Experimental Example 1 above, which have palmitic acid added to the N-terminus. "AP 3mer*4 (repeat)" is the peptide that exhibited the highest binding affinity to hair among the oligopeptides obtained by repeating any one of the tripeptide candidate sequences in Experimental Example 1 above four times. “AP 3mer*4 (random)” is an oligopeptide obtained by randomly combining two or more of the candidate tripeptide sequences of Experimental Example 1, and is the peptide with the highest binding ability to hair.
[0229] like Figure 8 As shown, the oligopeptides of the tripeptide sequence repeats or combinations (AP 3mer*4 (repeat), AP 3mer*4 (random)) of the embodiment showed a maximum binding capacity of 150% compared to known peptides or similar peptides from other companies (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. This confirms that the oligopeptides of the examples can bind to hair more effectively and improve hair strength than 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 than oligopeptides containing repeated or combined tripeptide sequences (AP 3mer*4 (repeated), AP 3mer*4 (random)), as disclosed in Experimental Examples 1 to 4, they exhibited a significant effect on improving hair strength compared to the untreated control group. Furthermore, the tripeptide (AP 3mer) and palmitoyl tripeptide (AP 3mer-Pal) are easily synthesized due to their short sequence length, thus offering advantages in terms of time and cost.
[0231] Experimental Example 6. Evaluation of the efficacy of tripeptide-2
[0232] A tripeptide of the KCV sequence was synthesized using the same method as disclosed in Experimental Example 3 above, and its efficacy was evaluated.
[0233] (1) Preparation of hair to simulate eyebrows
[0234] To confirm that the test substance exhibited the same effects on eyebrows, additional experiments were conducted using hair simulating eyebrows. As previously mentioned, the structure and composition of eyebrows are similar to those of hair in other parts of the body (e.g., head hair), and the basic structure and composition of hair follicles in the body are the same. Therefore, the test substance's effects on eyebrows and / or eyelashes should be comparable to those on hair in other parts of the body.
[0235] Specifically, since it is difficult to directly obtain eyebrows for evaluation, human hair of a thickness equivalent to eyebrows was selected using Fibra.one (manufactured by DiaStron). The hair was prepared to a length suitable for use with a machine for measuring tensile strength. Heat-treated hair was prepared by manually applying pressure 20 times at 160°C to the prepared human hair bundle using a hair straightener. As a control group, hair ( Figure 9 and Figure 11 In Experimental Example 6, the test substance was not applied to the untreated hair.
[0236] Then, KCV ( Figure 9 and Figure 11 KCV-treated hair). Specifically, a prepared hair bundle (1 g, manufactured by Beaulax) was washed with a basic cleanser without a conditioning function, rinsed for 1 minute, and dried for 2 minutes. The dried hair bundle (1 g) was immersed in 100 g of a solution containing a test substance dissolved at 0.01% by weight (in this case, the solution was a solution in which the test substance (0.01% by weight) was dissolved in purified water (the remainder)) for about 30 minutes. The immersed hair bundle was rinsed with running water for 1 minute and then naturally dried for more than 12 hours. In order to compare the effect of the KCV treatment, hair (1 g) that was washed and dried under the same conditions as above but was not treated with the test substance was prepared. Figure 9 and Figure 11 heat-damaged hair).
[0237] (2) Determination of tensile strength
[0238] The tensile strength of KCV-treated hair, heat-damaged hair, and untreated hair was compared using the same method as in "Experimental Example 2. (1) Determination of tensile strength."
[0239] Specifically, 30 hairs were randomly selected from each hair bundle treated with the test substance (KCV-treated hair). 30 hairs were randomly selected from a control group of hair bundles not treated with the test substance (heat-damaged hair and untreated hair, respectively). The tensile strength of each selected hair was measured using a Fibra.one (manufactured by DiaStron).
[0240] The results showed that the tensile strength of KCV-treated hair bundles increased significantly after heat treatment compared with that of heat-damaged hair bundles (ref. Figure 9 ;exist Figure 9 In the figure, "KCV-treated hair" refers to hair treated with KCV tripeptide after heat treatment, "untreated hair" refers to control hair that was not heat-treated and not treated with the test substance, and "heat-damaged hair" refers to hair that was heat-treated). Figure 9 In the figure, the y-axis is the tensile strength (break load) relative to the area, and the unit is gmf / μm 2 .
[0241] (3) Determination of elasticity
[0242] The elasticity of KCV-treated hair, heat-damaged hair, and untreated hair was compared. The elasticity of the hair was defined as the horizontal resistance force, and the elasticity was measured according to the following [Hair Elasticity Measurement Method] (refer to Figure 10 ).
[0243] Hair elasticity measurement method
[0244] (i) Place the module (M) containing the eyebrow hair on a horizontally movable track. (ii) Place a total of 10 strands of clipped hair (15 mm) vertically on a clamp fixed to the module M. (iii) Move the module M toward a 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 after heat treatment, the elastic force of KCV-treated hair bundles was significantly increased compared with that of heat-damaged hair bundles (ref. Figure 11 ;exist Figure 11 In the figure, "KCV-treated hair" refers to hair treated with KCV tripeptide after heat treatment, "untreated hair" refers to control hair that was not heat-treated and not treated with the test substance, and "heat-damaged hair" refers to hair that was heat-treated). Figure 11 In the figure, the y-axis is the elastic force, and the unit is 10 -3 N.
[0246] The present disclosure is further illustrated by the following implementation examples which do not limit the scope of the claims.
[0247] Implementation Example 1. A peptide comprising one or more amino acid sequence units consisting of Xaa-Yaa-Zaa, wherein:
[0248] Xaa, Yaa and Zaa are each independently selected from the group consisting of C (cysteine), K (lysine), W (tryptophan), V (valine), L (leucine) and F (phenylalanine),
[0249] The Xaa, Yaa and Zaa are different from each other, wherein when Xaa and Yaa are C and K respectively, Zaa is not L.
[0250] Implementation Example 2. A peptide, which is the peptide of Implementation Example 1, wherein:
[0251] Two of Xaa, Yaa, and Zaa are C and K, respectively. When Xaa and Yaa are C and K, respectively, Zaa is not L.
[0252] Implementation Example 3. A peptide, which is the peptide described in any one of Implementation Examples 1 and 2, wherein:
[0253] The peptide is a tripeptide composed of one Xaa-Yaa-Zaa sequence unit.
[0254] Implementation Example 4. A peptide, which is the peptide according to 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 according to 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] Implementation Example 6. A peptide derivative, wherein an acyl group derived from a fatty acid or an organic acid is bound to the N-terminus of the peptide according to any one of Implementation Examples 1 to 5.
[0260] Implementation Example 7. A peptide derivative, which is 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] Implementation Example 8. A peptide derivative, which is the peptide derivative described in any one of Implementation 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] Implementation Example 9. A peptide derivative, which is the peptide derivative according to any one of Implementation Examples 6 to 8, wherein:
[0264] The peptide derivative is CKF having a palmitoyl group bound to the N-terminus, CWK having a palmitoyl group bound to the N-terminus, or KCV having a palmitoyl group bound to the N-terminus.
[0265] Implementation Example 10. A composition for protecting hair, repairing damaged hair, or strengthening hair, comprising the peptide described in any one of Implementation Examples 1 to 5.
[0266] Implementation Example 11. A composition for protecting hair, repairing damaged hair or strengthening hair, comprising the peptide derivative described in any one of Implementation Examples 6 to 9.
[0267] Implementation Example 12. A composition for protecting hair, repairing damaged hair, or strengthening hair, comprising at least three amino acids selected from the group consisting of C, K, W, V, L (leucine), and F.
[0268] Implementation Example 13. A composition for protecting hair, repairing damaged hair, or strengthening hair, which is the composition of Implementation Example 12, wherein:
[0269] The composition includes C; K; and one of W, V, L or F.
[0270] Implementation Example 14. A composition for protecting hair, repairing damaged hair, or strengthening hair, which is the composition described in any one of Implementation Examples 12 to 13, wherein:
[0271] The composition includes C; K; and one of W, V, L or F.
[0272] Implementation Example 15. A composition for protecting hair, repairing damaged hair, or strengthening hair, which is the composition described in any one of Implementation 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 Listing]
[0275] SEQ ID NO: 1 (peptide sequence of an embodiment): CKFCKF
[0276] SEQ ID NO: 2 (peptide sequence of an embodiment): CKFCKFCKF
[0277] SEQ ID NO: 3 (peptide sequence of an embodiment): CKFCKFCKFCKF
[0278] SEQ ID NO: 4 (peptide sequence of an embodiment): CWKCWK
[0279] SEQ ID NO: 5 (peptide sequence of an embodiment): CWKCWKCWK
[0280] SEQ ID NO: 6 (peptide sequence of an embodiment): CWKCWKCWKCWK
[0281] SEQ ID NO: 7 (peptide sequence of an embodiment): KCVKCV
[0282] SEQ ID NO: 8 (peptide sequence of an embodiment): KCVKCVKCV
[0283] SEQ ID NO: 9 (peptide sequence of an embodiment): KCVKCVKCVKCV
[0284] SEQ ID NO: 18 (peptide sequence of an embodiment): CWKCWKKCLKCLKCV
[0285] SEQ ID NO: 19 (peptide sequence of an embodiment): CKWCWKKCLKCVKCL
[0286] SEQ ID NO: 20 (peptide sequence of an embodiment): CKWKCFCKFCWKKCV
[0287] SEQ ID NO: 21 (peptide sequence of an embodiment): KCFKCFCKWCKFKCV
[0288] SEQ ID NO: 22 (peptide sequence of an 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. A composition for protecting hair, repairing damaged hair or strengthening hair comprising a peptide or a peptide derivative, wherein: The peptide is KCV (Lys-Cys-Val), The peptide derivative is KCV (palmitoyl-Lys-Cys-Val) having a palmitoyl group bound to the N-terminus.
2. The composition according to claim 1, wherein The peptide or the peptide derivative increases the tensile strength of hair.
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