Cosmetic composition for improving skin

By developing peptides with specific amino acid sequences to apply to the skin, the side effects and unstable effects of existing skin improvement peptides have been solved, and safe and efficient improvement of skin status has been achieved, and it is suitable for a variety of skin topical dosage forms.

CN120303284APending Publication Date: 2025-07-11LG HOUSEHOLD & HEALTH CARE LTD
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Patent Information

Application Number
CN202380083541.2
Authority / Receiving Office
CN · China
Patent Type
Applications(China)
Current Assignee / Owner
Priority Date
2023-08-01
Filing Date
2023-12-11
Publication Date
2025-07-11

AI Technical Summary

Technical Problem

The existing skin improvement peptides have problems such as large side effects, unstable effects and limited use. In particular, botulinum toxin requires a doctor's injection and the effect lasts for a short time. Commercially available peptides such as Ac-Glu-Glu-Met-Gln-Arg-Arg-NH2 have weak and unstable effects.

Method used

A peptide or derivative thereof containing a specific amino acid sequence was developed, through variation and sequence optimization, the peptide forming formula I was applied to the skin, significantly improving the skin state, including skin wrinkles and elasticity.

Benefits of technology

This peptide significantly improves skin condition, provides excellent skin improvement effects and is safe for the human body. It is suitable for a variety of skin topical dosage forms, including cosmetics and pharmaceutical compositions, and can effectively reduce muscle contraction without toxin side effects.

✦ Generated by Eureka AI based on patent content.

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Abstract

The present disclosure relates to a cosmetic composition for improving a skin condition, comprising a peptide for improving a skin condition. The skin condition-improving peptide or the derivative thereof according to the present disclosure has a significantly excellent skin condition-improving effect. The peptide or the derivative thereof can be usefully used as an active ingredient of a functional cosmetic composition or an external preparation composition for the skin which can be used for the skin.
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Description

Technical Field

[0001] This application claims priority based on Korean Application No. 10-2022-0172978 filed on December 12, 2022, and Korean Application No. 10-2023-0100598 filed on August 1, 2023. All content disclosed in the specification and drawings of these applications is incorporated herein by reference.

[0002] The present disclosure relates to a cosmetic composition for improving skin condition, which contains a peptide for improving skin condition. Background Art

[0003] Skin wrinkles are generally caused by strong muscle contractions or are generated due to maintaining a posture that induces strong muscle contractions for a long time. Currently, wrinkles generated when making expressions and aging wrinkles are usually treated with botulinum toxin (botox) (botulinum toxin A). Botulinum toxin improves skin wrinkles by paralyzing the muscles around the eyes or on the forehead. However, botulinum toxin must be administered by a doctor through subcutaneous injection, so its use is limited, and it has the disadvantages of being expensive and highly toxic. In addition, the effect of botulinum toxin lasts for 3 to 6 months, so the treatment with botulinum toxin must be repeated.

[0004] The mechanism of action of botulinum toxin is to selectively block the secretion of acetylcholine at the neuromuscular synapse, thereby paralyzing the muscle. This is achieved by the cleavage of a protein called SNAP-25. In addition, the N-terminal amino acid sequence (H-Glu-Glu-Met-Gln-Arg-Arg-NH2) of SNAP-25 also induces muscle relaxation by hindering the secretion of Ca ++ -dependent neurotransmitters at the synapse. The locally applicable compound Ac-Glu-Glu-Met-Gln-Arg-Arg-NH2 (sold under the trade name Argirelline TM developed therefrom) is 5000 times weaker in action than botulinum toxin, so it can be easily administered and has almost no toxicity. However, its muscle relaxation effect is very weak and unstable, so it cannot show a satisfactory wrinkle improvement effect, and its protein degradation stability is also insufficient.

[0005] Small peptides or peptide compounds are formed by enzymatic degradation in the extracellular matrix of the skin. Since these peptides or peptide compounds, called "matrikines", have important signal functions, they can regulate cell activity. Therefore, various peptides or peptide compounds obtained by extraction or synthesis have been proposed as active ingredients in cosmetics. For example, there is MATRIXYL as a lipopeptide TMPal-KTTKS and Pal-GHK / Pal-GQPR mixtures sold under a trademark name, which correspond to fragments of collagen. Their effects of stimulating collagen synthesis were determined through in vitro experiments, and improvements in skin firmness, elasticity, density, thickness, and microrelief (wrinkles and fine lines) were determined through in vivo experiments. Such a novel peptide compound that can aesthetically improve the skin condition by repairing skin defects is an active ingredient attracting much attention in the cosmetic industry.

[0006] Drug delivery through the skin is convenient to use and is used in various fields and in various forms. Such drugs through the skin are mainly for delivering to the systemic circulation system through the skin, but atopy treatment agents, cosmetics for whitening or wrinkle improvement, etc. are also used to directly deliver active ingredients to the organs of the skin itself.

[0007] Recently, peptides that exhibit effects similar to botulinum toxin on the skin but reduce muscle contraction in a non-paralytic manner without toxin side effects are being developed. Such peptides relieve the occurrence of wrinkles by temporarily blocking the secretion of neurotransmitters such as acetylcholine responsible for muscle cell contraction. However, when such peptides are used in excess, there is a risk of side effects, and there are limitations in use such as acting only on parts with dense nerves. Summary of the Invention

[0008] Technical Problem

[0009] The problem to be solved by the present disclosure is to improve the disadvantages of existing peptides for skin improvement, and thus provide a composition having excellent skin improvement effects and being safe for the human body.

[0010] Technical Solution

[0011] The inventors of the present invention, in order to improve the skin condition, worked on improving problems such as side effects or precautions in the use of previously used peptides for skin improvement, and developed a composition that is safe for the human body and has excellent effects in improving the skin condition without disadvantages such as weak effects. As a result, the inventors of the present invention discovered a specific peptide sequence showing the efficacy of improving the skin condition. The inventors of the present invention surprisingly found that when a peptide composed of a specific amino acid sequence whose efficacy is stabilized by mutation and sequence optimization is coated on the skin, the skin condition is significantly improved, thereby completing the present invention.

[0012] The present disclosure provides a peptide or a derivative thereof comprising the amino acid sequence of the following Chemical Formula I. The peptide or a derivative thereof of the present disclosure can be used for improving the skin condition, preferably the skin appearance condition.

[0013] <Chemical Formula I>

[0014] X1-X2-X3-(S-S-C-F)-Y1-Y2-Y3

[0015] In the amino acid sequence of Formula I above, X1 may be K or absent; X2 may be G or absent; X3 may be R or absent; Y1 may be V or absent; Y2 may be D or absent; and Y3 may be C or absent.

[0016] In one aspect of the present disclosure, preferably, the amino acid sequence of Formula I above may include at least one amino acid sequence among X1 to X3 and Y1 to Y3 above.

[0017] In one aspect of the present disclosure, the amino acid sequence of Formula I above may be any one of the amino acid sequences in the following sequence numbers.

[0018] - Sequence number 1: KGRSSCFVDC

[0019] - Sequence number 2: KGRSSCFVD

[0020] - Sequence number 3: KGRSSCF

[0021] - Sequence number 4: KGRSSCFV

[0022] - Sequence number 5: RSSCFVDC

[0023] - Sequence number 6: SSCFVDC

[0024] - Sequence number 7: GRSSCFVD

[0025] - Sequence number 8: RSSCFVD

[0026] - Sequence number 9: SSCFVD

[0027] - Sequence number 10: KGSSCFVDC

[0028] - Sequence number 11: KGRSSCFDC

[0029] - Sequence number 12: KGRSSCFVC

[0030] - Sequence number 13: RSSCF

[0031] The present disclosure provides a cosmetic, a topical skin agent, or a pharmaceutical composition for improving skin condition, which contains a peptide or a derivative thereof, and the peptide contains the amino acid sequence of Formula I selected from any one of the amino acid sequences in the above sequence numbers 1 to 13. Preferably, the composition for improving skin condition above may be a cosmetic composition.

[0032] In one aspect of the present disclosure, the above-mentioned peptide or its derivative may comprise an amino acid sequence having at least 50%, 60%, 70%, 80%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% sequence identity with the amino acid sequence of the above Chemical Formula I. Preferably, the above-mentioned peptide or its derivative may comprise an amino acid sequence having more than 80% sequence identity with the amino acid sequence of the above Chemical Formula I.

[0033] In one aspect of the present disclosure, the above-mentioned peptide or its derivative may comprise an amino acid sequence having at least 50%, 60%, 70%, 80%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% sequence identity with any one of the amino acid sequences of the above Sequence Numbers 1 to 13. Preferably, the above-mentioned peptide or its derivative may comprise an amino acid sequence having more than 80% sequence identity with any one of the amino acid sequences of the above Sequence Numbers 1 to 13.

[0034] In one aspect of the present disclosure, relative to the total weight of the composition, the content of the peptide or its derivative comprising the amino acid sequence of the above Chemical Formula I may be 0.0001 to 50% by weight, preferably 0.001 to 30% by weight, more preferably 0.001 to 1% by weight. When the content of the above-mentioned peptide or its derivative is within the above range, the skin condition improving effect may be more excellent.

[0035] In one aspect of the present disclosure, the peptide or its derivative comprising the amino acid sequence of the above Chemical Formula I can be used for improving skin condition, preferably for skin wrinkle, skin elasticity or skin sebum care.

[0036] In one aspect of the present disclosure, the term "peptide" may refer to all natural peptides and synthetic peptides containing 15 or fewer amino acids, including peptides found naturally or commercially available. The above-mentioned peptides include their derivatives, isomers or complexes with metal ions, etc.

[0037] In one aspect of the present disclosure, the peptide comprising the amino acid sequence of the above Chemical Formula I may be a pure peptide, or an L-isomer, D-isomer or a mixture thereof, preferably, it may be a naturally found L-isomer.

[0038] In one aspect of the present disclosure, the peptide comprising the amino acid sequence of the above Chemical Formula I may be in the form of a salt, preferably, it may be in the form of any salt commonly used in a cosmetic composition or a pharmaceutical composition, for example, it may be a hydrochloride salt or an acetate salt, etc.

[0039] In one aspect of the present disclosure, a derivative of a peptide containing the amino acid sequence of Formula I above refers to a peptide that has been modified or added with chemical functional groups but has no change in the carbon skeleton. The above derivatives include peptides in which the N-terminus, C-terminus, etc. of the peptide have been chemically modified, or peptides modified by the addition, substitution, or deletion of amino acids. The above peptide derivatives can be lipophilic derivatives. For example, they can be palmitoyl derivatives. In addition, the above peptide derivatives can be derivatives conjugated with dansyl groups. In addition, the above peptide derivatives can be derivatives conjugated with acetyl groups.

[0040] In one aspect of the present disclosure, even if the above peptide contains an amino acid sequence having a reverse sequence structure of the amino acids of Formula I, it can exhibit an effect of improving skin condition. Preferably, the amino acid sequence having the above reverse sequence structure can be any one of the amino acid sequences of SEQ ID NOs: 14 to 16 below.

[0041] - SEQ ID NO: 14: CDVFCSSRGK

[0042] - SEQ ID NO: 15: DVFCSSRGK

[0043] - SEQ ID NO: 16: FCSSRGK

[0044] In one aspect of the present disclosure, peptides containing the amino acid sequence of Formula I above include analogues having modifications and / or additions of chemical functional groups and additional changes in the carbon skeleton. In addition, the above peptides can include peptides having a sequence in which one or more amino acid residues are different from the wild-type amino acid sequence contained therein. Amino acid exchanges in proteins and polypeptides that do not change the molecular activity as a whole are well known in the technical field to which the present invention pertains. Commonly occurring exchanges can be exchanges between amino acid residues Ala / Ser, Val / Ile, Asp / Glu, Thr / Ser, Ala / Gly, Ala / Thr, Ser / Asn, Ala / Val, Ser / Gly, Thy / Phe, Ala / Pro, Lys / Arg, Asp / Asn, Leu / Ile, Leu / Val, Ala / Glu, or Asp / Gly. In addition, it can include peptides whose structural stability against heat, pH, etc. or activity is increased by mutations or modifications in the amino acid sequence.

[0045] The above-mentioned peptide can be prepared by conventional chemical peptide synthesis methods, or by PCR amplification of the gene encoding the above-mentioned peptide, or by cloning the synthesized product into an expression vector for expression by a known method. In addition, the above-mentioned peptide may include a complex with metal ions such as copper, zinc, manganese, and magnesium. In addition, when the above-mentioned peptide is synthesized by instrumental chemistry, it can be synthesized by an automatic peptide synthesizer through a liquid phase method (Convergent Solution Phase Synthesis) and a solid phase method (Solid Phase Peptide Synthesis).

[0046] In addition, the present disclosure provides a polynucleotide encoding a peptide or a derivative thereof comprising the amino acid sequence of Formula I above. The above-mentioned polynucleotide may be mutated by substitution, deletion, insertion, or a combination of more than one base. When preparing a nucleotide sequence by chemical synthesis, synthesis methods well-known in the art can be used. For example, the methods described in the literature (Engels and Uhlmann, Angew., Chem Int Ed Engl., 37:73-127, 1988) can be used, and methods such as triester, phosphite, phosphoramidite, and H-phosphate methods, PCR, and other autoprimer methods, oligonucleotide synthesis methods on solid supports, etc. can be used for synthesis.

[0047] The present disclosure provides polynucleotides of SEQ ID NOs: 17 to 19 encoding any one of the amino acid sequences of SEQ ID NOs: 1 to 3 above. The polynucleotide of SEQ ID NO: 17 encodes the amino acid sequence of SEQ ID NO: 1, the polynucleotide of SEQ ID NO: 18 encodes the amino acid sequence of SEQ ID NO: 2, and the polynucleotide of SEQ ID NO: 19 encodes the amino acid sequence of SEQ ID NO: 3.

[0048] - SEQ ID NO: 17: AAA GGC CGC AGC AGC TGC TTT GTG GAT TGC

[0049] - SEQ ID NO: 18: AAA GGC CGC AGC AGC TGC TTT GTG GAT

[0050] - SEQ ID NO: 19: AAA GGC CGC AGC AGC TGC TTT

[0051] In addition, the present disclosure provides an expression vector containing the above-mentioned polynucleotide and a transformant containing the above-mentioned expression vector. In addition, the present disclosure provides a method for producing the above-mentioned peptide for improving skin condition or a derivative thereof using the above-mentioned transformant.

[0052] In the present disclosure, an "expression vector" is a recombinant vector capable of expressing a target peptide in a host cell, and refers to a gene construct containing essential regulatory elements operably linked to express a gene insert. The above-mentioned expression vector includes expression regulatory elements such as a start codon, a stop codon, a promoter, and an operon. The above-mentioned start codon and stop codon are generally considered to be part of the nucleotide sequence encoding a polypeptide, and must function in an individual when the gene construct is administered, and must be in frame with the coding sequence. The above-mentioned promoter can be constitutive or inducible.

[0053] The above-mentioned expression vector may contain a signal sequence for excreting the polypeptide to facilitate the separation of the protein from the cell culture solution. To effectively translate the inserted nucleic acid sequence, specific initiation signals may be required. The signals include the ATG start codon and adjacent sequences. In some cases, exogenous translation regulatory signals that may include the ATG start codon need to be provided. These exogenous translation regulatory signals and start codons can be from a variety of natural and synthetic sources. The expression efficiency can be increased by introducing appropriate transcriptional or translational enhancer factors.

[0054] In addition, in order to easily detect the above-mentioned peptide or its derivative, the above-mentioned expression vector may additionally contain a protein tag that can be optionally removed using an endopeptidase. The above-mentioned "tag" refers to a molecule that exhibits a quantifiable activity or property, and can be a fluorescent molecule including a chemical fluorescent substance such as fluorescein, a polypeptide fluorescent substance such as a fluorescent protein (GFP) or a related protein; it can be an epitope tag such as a Myc tag, a Flag tag, a histidine tag, a leucine tag, an IgG tag, or a streptavidin tag. When using an epitope tag, the epitope tag can use a peptide tag preferably composed of more than 6 amino acid residues, more preferably composed of 8 to 50 amino acid residues.

[0055] In the present disclosure, the above-described expression vector may include a nucleotide sequence encoding the above-described peptide or its derivative. The above-described expression vector is not particularly limited as long as it can produce the above-described peptide or its derivative, but preferably plasmid DNA or phage DNA, etc. may be used, and more preferably commercially developed plasmids (pUC18, pBAD, pIDTSAMRT-AMP, etc.), plasmids derived from Escherichia coli (pYG601BR322, pBR325, pUC118, pUC119, etc.), plasmids derived from Bacillus subtilis (pUB110, pTP5, etc.), plasmids derived from yeast (YEp13, YEp24, YCp50, etc.), phage DNA (Charon4A, Charon21A, EMBL3, EMBL4, λgt10, λgt11, λZAP, etc.), animal virus vectors (retrovirus, adenovirus, vaccinia virus, etc.), insect virus vectors (baculovirus, etc.), etc. may be used. The above-described expression vector shows different protein expression levels, etc. depending on the host cell, and thus it is preferable to select and use the one most suitable for the target host cell.

[0056] In the present disclosure, the above-described transformant can be prepared by transforming the above-described expression vector into a host. The above-described transformant can express the polynucleotide contained in the expression vector for producing the above-described peptide for improving skin condition or its derivative. The above-described transformation can be carried out by various methods, and the CaCl2 precipitation method, the Hanahan method using a reducing substance DMSO in the CaCl2 precipitation method to improve efficiency, electroporation, calcium phosphate precipitation method, protoplast fusion method, agitation method using silicon carbide fibers, agrobacteria-mediated transformation method, transformation method using PEG, dextran sulfate, lipofectamine, and desiccation / inhibition-mediated transformation method, etc. may be used, but are not limited thereto. In addition, as the host used in the preparation of the above-described transformant, bacterial cells such as Escherichia coli (E. coli), Streptomyces, Salmonella typhimurium, etc.; yeast cells such as Saccharomyces cerevisiae, Schizosaccharomyces pombe, etc.; fungal cells such as Pichia pastoris, etc.; insect cells such as Drosophila, Sf9 cells of Spodoptera, etc.; animal cells such as CHO, COS, NSO, 293, bowe melanoma cells, etc.; or plant cells, etc. may be used, but are not limited thereto.

[0057] The above transformant can also be used in a method for producing the above peptide or its derivative. Specifically, the method for producing the peptide or its derivative of the present disclosure may include: (a) a step of obtaining a culture by culturing the above transformant; and (b) a step of recovering the peptide or its derivative of the present disclosure from the above culture.

[0058] In the present disclosure, "culturing" refers to a method of growing and developing microorganisms under appropriately artificially regulated environmental conditions. The method for culturing the above transformant can be carried out using methods well known in the art. Specifically, the above culturing can be continuous culturing in a batch process, a fed batch or a repeated fed batch process.

[0059] The culture medium used in the above culturing needs to be adjusted for temperature, pH, etc. under aerobic conditions in a conventional culture medium containing appropriate carbon sources, nitrogen sources, amino acids, vitamins, etc., while meeting the requirements of specific strains in an appropriate manner. As the carbon source that can be used, a mixed sugar of glucose and xylose is used as the main carbon source. In addition, it includes sugars and carbohydrates such as sucrose, lactose, fructose, maltose, starch or cellulose; oils and fats such as soybean oil, sunflower oil, castor oil or coconut oil; fatty acids such as palmitic acid, stearic acid, linoleic acid; glycerol; alcohols such as ethanol; and organic acids such as acetic acid. These substances can be used individually or as a mixture. As the nitrogen source that can be used, inorganic nitrogen sources such as ammonia, ammonium sulfate, ammonium chloride, ammonium acetate, ammonium phosphate, ammonium carbonate and ammonium nitrate can be used; amino acids such as glutamic acid, methionine, glutamine; and organic nitrogen sources such as peptone, NZ-amine, meat extract, yeast extract, malt extract, corn steep liquor, casein hydrolysate, fish or its decomposition products, defatted soybean cake or its decomposition products. These nitrogen sources can be used alone or in combination. The above culture medium may contain potassium dihydrogen phosphate, dipotassium hydrogen phosphate and the corresponding sodium salts as a phosphorus supply source. In addition, as inorganic compounds, sodium chloride, calcium chloride, ferric chloride, magnesium sulfate, ferric sulfate, manganese sulfate and calcium carbonate can be used. In addition, essential growth substances such as other amino acids and vitamins can be used.

[0060] In addition, precursors suitable for the culture medium can be used in the above-mentioned culture medium. The above-mentioned raw materials can be added to the culture in a batch, fed-batch or continuous manner by appropriate means during the culture process, but are not limited thereto. The pH of the culture can be adjusted by using an alkaline compound (such as sodium hydroxide, potassium hydroxide, ammonia, etc.) or an acid compound (such as phosphoric acid or sulfuric acid, etc.) by appropriate means. In addition, an antifoaming agent such as fatty acid polyethylene glycol ester can be used to inhibit the generation of bubbles. In order to maintain an aerobic state, oxygen or an oxygen-containing gas (such as air) is injected into the culture. The temperature of the culture is usually 27°C to 37°C, preferably 30°C to 35°C. The culture can be continuously carried out until the maximum production amount of the above-mentioned peptide or its derivative is obtained, and for this purpose, it can usually be cultured for 10 to 100 hours.

[0061] In addition, the step of recovering the above-mentioned peptide or its derivative from the culture can be carried out by methods well-known in the art. Specifically, the above-mentioned recovery methods can use centrifugation, filtration, extraction, spraying, drying, evaporation, precipitation, crystallization, electrophoresis, fractional dissolution (such as ammonium sulfate precipitation) or chromatography (such as ion exchange, affinity, hydrophobicity and size exclusion), etc., but are not limited thereto.

[0062] In one aspect of the present disclosure, the above-mentioned topical skin preparation refers to a solid, semi-solid or liquid topical preparation that can be easily applied to the skin by mixing an active ingredient in various bases such as oils, vaseline, lanolin or glycerin. There is no particular limitation on such topical dosage forms, but powder, gel, ointment, cream, liquid or aerosol dosage forms are preferred.

[0063] In one aspect of the present disclosure, in addition to the peptide or its derivative composed of the amino acid sequence of the above chemical formula I, the above-mentioned pharmaceutical composition can additionally contain a drug that is introduced into the body through the skin or delivered to an organ of the skin itself. The above-mentioned pharmaceutical composition can additionally contain appropriate carriers, excipients or diluents commonly used in the art.

[0064] The above pharmaceutical composition may have any dosage form selected from the group consisting of tablets, pills, powders, granules, capsules, suspensions, internal liquid preparations, emulsions, syrups, sterile aqueous solutions, non-aqueous solvents, suspensions, emulsions, lyophilized preparations, and suppositories, and may be various dosage forms for oral or non-oral administration. When formulating, it is formulated using diluents or excipients such as commonly used fillers, extenders, binders, wetting agents, disintegrants, or surfactants. Solid preparations for oral administration include tablets, pills, powders, granules, or capsules, etc., and such solid preparations are formulated by mixing one or more compounds with at least one excipient (for example, starch, calcium carbonate, sucrose, or lactose, or gelatin, etc.). In addition, lubricants such as magnesium stearate and talc are also used in addition to simple excipients. Liquid preparations for oral administration include suspensions, internal liquid preparations, emulsions, syrups, etc., and in addition to the commonly used simple diluents water and liquid paraffin, various excipients such as wetting agents, sweeteners, flavoring agents, preservatives, etc. may also be included. Preparations for non-oral administration include sterile aqueous solutions, non-aqueous solvents, suspensions, emulsions, lyophilized preparations, or suppositories, etc. As non-aqueous solvents and suspension solvents, propylene glycol, polyethylene glycol, vegetable oils such as olive oil, injectable esters such as ethyl oleate, etc. can be used.

[0065] In one aspect of the present disclosure, the above pharmaceutical composition can be administered in a pharmaceutically effective amount. The above "pharmaceutically effective amount" refers to an amount sufficient to treat a disease with a reasonable benefit / risk ratio applicable to medical treatment. The effective dosage level can be determined based on factors including the individual type and severity, age, gender, type of disease, activity of the drug, sensitivity to the drug, administration time, administration route and excretion rate, treatment period, drugs used simultaneously, and other factors well known in the medical field. The composition of the present disclosure can be administered as an individual therapeutic agent or in combination with other therapeutic agents, and can be administered sequentially or simultaneously with conventional therapeutic agents. In addition, it can be administered singly or multiply. Considering all of the above factors, it is important to administer an amount that can achieve the maximum effect with the minimum amount without side effects, and can be easily determined by those skilled in the art. The preferred dosage of the composition of the present disclosure varies depending on the patient's condition and body weight, degree of disease, drug form, administration route and period, and the appropriate total daily usage amount, within the scope of correct medical judgment, can be determined by the attending physician, but generally, an amount of 0.001 to 1000 mg / kg, preferably 0.05 to 200 mg / kg, more preferably 0.1 to 100 mg / kg can be administered once a day or divided into several times. There is no particular limitation on the individual to which the above composition is administered. For example, it can be applied to any individual, such as non-human animals such as monkeys, dogs, cats, rabbits, guinea pigs, rats, mice, cows, sheep, pigs, goats, etc. and humans, etc., and the administration method includes, without limitation, as long as it is a conventional method in the art. For example, a transdermal administration method such as by topical application can be used, but is not limited thereto.

[0066] In one aspect of the present disclosure, the above cosmetic composition can contain conventional auxiliaries, such as fatty substances, organic solvents, solubilizers, thickeners, gelling agents, softeners, antioxidants, suspending agents, stabilizers, foaming agents, fragrances, surfactants, water, ionic or non-ionic emulsifiers, fillers, sequestering agents, chelating agents, preservatives, vitamins, blockers, wetting agents, essential oils, dyes, pigments, hydrophilic or lipophilic active agents or lipid vesicles, and auxiliaries commonly used in the fields of cosmetics or dermatology.

[0067] In one aspect of the present disclosure, the above cosmetic composition may be a functional cosmetic. The above functional cosmetic is a product with professional functionality that incorporates the professional treatment functions of pharmaceuticals into cosmetics and emphasizes physiological active effects and results, including products that contribute to skin whitening, products that contribute to the improvement of skin wrinkles, cosmetics that contribute to even sun tanning of the skin or protect the skin from ultraviolet damage, etc. The above functional cosmetic can exhibit skin improvement effects through, for example, the effect of promoting the synthesis of functional substances such as collagen, elastin, laminin, or HAS2. Its dosage form is not particularly limited, but it can be prepared into, for example, solution, emulsion, suspension, paste, cream, lotion, gel, powder, spray, surfactant-containing cleanser, oil, soap, liquid cleanser, bath agent, foundation, makeup primer, essence, lotion, foam, mask, softener, sunscreen, or sunscreen oil, etc. Preferably, it can be prepared into the dosage form of a topical skin ointment, soft lotion, nutritious lotion, nutritious cream, massage cream, essence, mask, emulsion, or oil gel. At this time, the carrier used can be selectively used according to the dosage form of the cosmetic.

[0068] In one aspect of the present disclosure, there is provided a method for improving skin condition, which includes: the step of transdermally administering a composition containing an effective amount of a peptide or its derivative to a subject in need of improving skin condition, the peptide containing the amino acid sequence of the above Chemical Formula I. Preferably, the above improvement in skin condition may be improvement in skin wrinkles or improvement in skin lipid secretion.

[0069] In one aspect of the present disclosure, the above method for improving skin condition may include: the step of preparing a subject in need of improving skin wrinkles or skin lipid secretion; the step of transdermally administering 1 ml of the above composition for 4 weeks; and the step of improving the skin condition of the above subject. Preferably, the above improvement in skin condition may be improvement in skin wrinkles or improvement in skin lipid secretion.

[0070] In one aspect of the present disclosure, the above-described composition for improving skin condition may include a physiologically acceptable medium. Such a physiologically acceptable medium refers to an aqueous or hydro-alcoholic solution, a water-in-oil emulsion, an oil-in-water emulsion, a micro-emulsion, an aqueous gel, an anhydrous gel, a serum, a dispersant of vesicles, or a powder, but is not limited thereto. The above "physiologically acceptable" means that when the composition comes into contact with the mucous membranes, appendages (nails, hair), scalp, and skin of mammals, particularly humans, it is suitable for topical or transdermal use, and the above composition can be ingested or injected into the skin without toxicity, incompatibility, instability, allergic reactions, and other risks. Such a "physiologically acceptable medium" may be a conventional excipient of the composition.

[0071] In one aspect of the present disclosure, the above-described peptide or its derivative may optionally use a solubilizer according to the use to be dissolved in a lipophilic or hydrophilic matrix. In order to enhance and achieve the preferred effects described in the present disclosure, the above peptide may be combined with other active ingredients at an effective concentration that can act synergistically or additionally with the following preparations, etc.: anti-aging, anti-fine lines and wrinkles, whitening, pro-pigmenting, hydration, wetting, moisturizing, slimming, keratolytic, anti-acne, anti-flushing, anti-inflammatory, antioxidant / free radical scavenger, whitening effect of complexion, anti-glycation, plumpness, reconstruction, anti-carbonylation, skin relief, anti-hair regrowth, action in the stratum corneum, skin-epidermal junction, HSP protein production, firmness, elasticity, and skin tone, hair growth (eyelashes and eyebrows), eye contour (dark circles and eye bags), promotion of blood circulation, other peptides or vitamins, etc. These active ingredients may be obtained from traditional plant extracts or products of plant cell culture or fermentation, etc., of plant substances.

[0072] In one aspect of the present disclosure, the above composition may be in any conventional form or as a carrier, in the form of a solution, dispersion, emulsion, paste, or powder. Additionally, the above composition is applicable in a carrier (vehicle) or as a premix in a carrier (such as in the form of macro-, micro-, or nano-capsules; macro-, micro-, or nano-spheres; liposomes, oleosomes, or chylomicrons; macro-, micro-, or nano-particles; or macro-, micro-, or nano-sponges; or in the form of micro- or nano-emulsions), or may be adsorbed on organic polymer powders, talc, bentonite, spores or outer membranes, and other inorganic or organic supports.

[0073] In one aspect of the present disclosure, the above-mentioned composition can be used for skin protection or cosmetic purposes for the face, body, hair, body hair, etc. The above-mentioned peptide or its derivative can be locally delivered by contacting the skin through fabrics, natural or synthetic fibers, wool, clothing materials, handkerchiefs, etc.

[0074] In one aspect of the present disclosure, in addition to the above-mentioned peptide or its derivative, the above-mentioned composition may further contain additional active substances. These additional active substances may include a wide range of non-limiting cosmetic and pharmaceutical ingredients commonly used in the skin protection industry as described in CTFA (International Cosmetic Ingredient Dictionary & Handbook (15th Ed. 2014), published by the Personal Care Products council, ex-the Cosmetic, Toiletry, and Fragrance Association, Inc., Washington, D.C.). The above-mentioned additional active substances may be betaine, glycerol, Actimoist Bio 2 TM (active organic substance), AquaCacteen TM (Mibelle AG Cosmetics), Aquaphyline TM (Silab), Aquaregul K TM (Solabia), Carciline TM (Greentech), Codiavelane TM (Biotech Marine), Dermaflux TM (Arch Chemicals, Inc), Hydra'Flow TM (Sochibo), Hydromoist L TM (Symrise), RenovHyal TM (Soliance), Seamoss TM (Biotech Marine), Argireline TM (the commercial name of acetyl hexapeptide-3 of Lipotec), spilanthol or the known commercial name Gatuline Expression TM of Acmella oleracea, the known commercial name Boswellin TMExtracts of Boswellia serrata, Deepaline PVB TM (Seppic), Syn-AKE TM (Pentapharm), Ameliox TM , Bioxilift TM (Silab), PhytoCellTec TM Argan (Mibelle), Papilactyl D TM (Silab), Preventhelia TM (Lipotec), Subliskin TM (Sederma), Venuceane TM (Sederma), Moist 24 TM (Sederma), Vegesome Moist 24 TM (Sederma), Essenskin TM (Sederma), Juvinity TM (Sederma), Revidrat TM (Sederma), Resistem TM (Sederma), Chronodyn TM (Sederma), Kombuchka TM (Sederma), Chromocare TM (Sederma), Calmosensine TM (Sederma), Glycokin factor S TM (Sederma), Biobustyl TM (Sederma), Idealift TM (Sederma), Ceramide 2 TM Ceramide A TM and Ceramide HO3 TM (Sederma), Legance TM (Sederma), Intenslim TM (Sederma), Prodizia TM (Sederma), Beautifeye TM(Sederma), NG-shea butter unsaponifiables (natural grade) (Sederma), Zingersl TM (Sederma), Meiritage TM (Sederma), Senestem TM (Sederma), Sebuless TM (Sederma), Majestem TM (Sederma), Apiscalp TM (Sederma), Rubistem TM(Sederma) or its mixtures, etc. Additionally, as the above-mentioned additional active substances, Parthenocissus tricuspidata can be used, especially English ivy (Hedera Helix), Bupleurum chinense, Bupleurum falcatum, arnica (Arnica Montana L), rosemary (Rosmarinus officinalis N), marigold (Calendula officinalis), sage (Salvia officinalis L), ginseng (Panax ginseng), ginkgo biloba, St.-John's-Wort (Hyperycum Perforatum), butcher's broom (Ruscus aculeatus L), European meadowsweet (Filipendula ulmaria L), big-flowered Jarva tea (Orthosiphon Stamincus Benth), algae (Fucus Vesiculosus), birch (Betula alba), green tea, cola nut (Cola Nipida), horse-chestnut, bamboo, Centella asiatica, heather, fucus, willow, mouse-ear, escine, cangzhu, chrysanthellum indicum, Armeniacea genus plants, Atractylodis Platicodon, Sinnomenum, Pharbitidis, Flemingia, Coleus such as Coleus forskohlii (C. Forskohlii), Coleus blumei (C. blumei), Coleus esquirolii (C. esquirolii), Coleus scutellaroides (C. scutellaroides), Coleus xanthantus (C. xanthantus) and Coleus barbatus (C.Extracts of Coleus barbatus), for example, root extracts of Coleus barbatus, Ballote, Guioa, Davallia, Terminalia, Barringtonia, Trema, antirobia, Cecropia, Argania, Dioscoreae such as Dioscorea opposita or Mexican yam extracts, Ammi visnaga, Siegesbeckia, especially extracts of Siegesbeckia orientalis, Ericaceae vegetable extracts, especially bilberry extracts (Vaccinium angustifollium) or Arctostaphylos uva ursi, aloe vera, plants containing sterols (e.g., phytosterols), Manjistha (extracted from plants of the genus Rubia, especially Rubia cordifolia) and guggal (extracted from Commiphora, especially Commiphora Mukul), kola extract, chamomile, red clover extract, Piper methysticum extract (KavaKava from SEDERMA. TM ) extracts of Bacopa monieri (Bacocalmine from SEDERMA TM) and extracts of seawhip, Glycyrrhiza glabra, mulberry, melaleuca (tea tree), Larrea divaricata, Rabdosia rubescens, Euglena gracilis, Fibraurea recisa Hirudinea, extracts of Chaparral Sorghum, sunflower extract, Enantia chlorantha, Mitracarpe of Spermacocea, Buchu barosma, Lawsonia inermis L., Adiantium Capillus-Veneris L., Chelidonium majus, Luffa cylindrica, Japanese Mandarin (Citrus reticulate Blanco var.Plant extracts such as unshiu, Camellia sinensis, Imperata cylindrica, Glaucium Flavum, Cupressus Sempervirens, Polygonatum multiflorum, loveyly hemsleya, Sambucus Nigra, Phaseolus lunatus, Centaurium, Macrocystis Pyrifera, Turnera Diffusa, Anemarrhena asphodeloides, Portulaca pilosa, Humulus lupulus, Coffea Arabica, Ilex Paraguariensis, or Globularia Cordifolia, Albizzia julibrissin, Oxydendron arboretum, Zingimber Zerumbet Smith, Astragalus membranaceus, Atractylodes macrocephalae, Plantago lanceolata, Leontopodium alpinum, Mirabilis jalapa or Apium graveolens.

[0075] In one aspect of the present disclosure, the following components can be used as the above additional active substances.

[0076] - Vialox sold by Pentapharm TM (INCI name: pentapeptide-3 (synthetic peptide containing alanine, arginine, isoleucine, glycine and proline)), Syn-ake TM (β-Ala-Pro-Dab-NH-Bzl) or Syn-Coll TM (Pal-Lys-Val-Lys-OH);

[0077] - Argireline sold by Lipotec TM(Ac-Glu-Glu-Met-Gln-Arg-Arg-NH2) (INCI Name: Acetyl Hexapeptide-3), Leuphasyl TM (Tyr-D-Ala-Gly-Phe-Leu), Aldenine TM (Gly-His-Lys), Trylagen TM (INCI Name: Pseudoalteromonas Ferment Extract, Hydrolyzed Wheat Protein, Hydrolyzed Soy Protein, Tripeptide-10 Citrulline (Reaction Product of Citrulline and Tripeptide-10 (a Synthetic Peptide Composed of Aspartic Acid, Isoleucine and Lysine)), Tripeptide-1), Eyeseryl TM (Ac-β-Ala-His-Ser-His), Serilesine TM (Ser-Ile-Lys-Val-Ala-Val) or Decorinyl TM (INCI Name: Tripeptide-10 Citrulline = Reaction Product of Citrulline and Tripeptide-10 (a Synthetic Peptide Composed of Aspartic Acid, Isoleucine and Lysine));

[0078] - Collaxyl sold by Vincience TM (Gly-Pro-Gln-Gly-Pro-Gln) or Quintescine TM (Cys-Gly);

[0079] - Cytokinol sold by Les Laboratoires Serobiologiques / Cognis TM LS (Casein Hydrolysate);

[0080] - Kollaren sold by l'lnstitut Europeen de Biologie Cellulaire TM (Gly-His-Lys), IP2000 TM (Pal-Val-Tyr-Val) or Meliprene TM (INCI Name: Reaction Product of Monofluoroheptapeptide-1 and Acetic Acid and a Synthetic Peptide Containing Arginine, Glycine, Glutamic Acid, Histidine, Norleucine, p-Fluorophenylalanine and Tryptophan);

[0081] - Neutrazen sold by Innovations TM (Pal-His-D-Phe-Arg-NH2); or

[0082] - BONT-L-Peptide sold by lnfinitec Activos TM (INCI name: reaction product of palmitoyl hexapeptide-19, palmitic acid and hexapeptide-19 (synthetic peptide composed of asparagine, aspartic acid, lysine and methionine)), Timp-Peptide TM (INCI name: acetyl hexapeptide-20, reaction product obtained by acetylation of hexapeptide-20 (synthetic peptide composed of alanine, glycine, lysine, valine and proline)) or ECM Moduline TM (INCI name: palmitoyl tripeptide-28, reaction product of palmitic acid and tripeptide-28 (synthetic peptide composed of arginine, lysine and phenylalanine)).

[0083] In one aspect of the present disclosure, the above composition may contain at least one compound selected from compounds such as vitamin B3, compounds such as niacinamide or tocopherol, retinoid compounds such as retinol, hexamidine, α-lipoic acid, resveratrol or DHEA, or hyaluronic acid, etc. as an additional active substance.

[0084] The present disclosure provides the use of a peptide having the amino acid sequence of the above chemical formula I or a derivative thereof in the preparation of a composition for improving skin condition. The above peptide or its derivative can be used to induce the synthesis of at least one molecule in the skin matrix, thereby improving the condition of the skin and its appendages.

[0085] In one aspect of the present disclosure, the improvement of the above skin condition generally refers to the process or its effect of alleviating, relieving, treating skin damage induced by internal or external factors of the skin, etc. For example, the improvement of skin condition can refer to skin wrinkle improvement, skin moisturization, skin whitening, skin elasticity maintenance or enhancement, wound recovery, aging inhibition, lipid secretion improvement or dermatitis alleviation or improvement, etc. In addition, the improvement of skin condition can refer to overall anti-aging, anti-wrinkle and fine surface improvement (gently relieving the skin, wrinkle filling), improvement of the mechanical properties of the skin, i.e., firmness and elasticity, increase in skin density (skin reorganization effect), increase in skin volume (plumping effect), stretchmark improvement, anti-spot, skin uniformity, gloss improvement or skin pigment improvement, etc. Preferably, the above improvement of skin condition can refer to skin wrinkle improvement or sebum secretion improvement.

[0086] In one aspect of the present disclosure, the above composition may contain other peptides or peptide compounds in addition to the peptide or its derivative containing the amino acid sequence of Formula I. Relative to the total weight of the composition, the content of the above other peptides or peptide compounds in the composition may be 1x10 -7 % by weight to 20% by weight, preferably 1x10 -6 % by weight to 10% by weight, more preferably 1x10 -5 % by weight to 5% by weight.

[0087] All components described in the present disclosure, preferably, do not exceed the maximum use values specified in relevant regulations and specifications of Korea, China, the United States, Europe, Japan, etc. (e.g., relevant regulations such as cosmetic safety standards (Korea), Cosmetic Safety and Technology Specifications (China), Food Code (Korea), Food Additive Code (Korea), Health Functional Food Code (Korea), etc.). That is, preferably, the cosmetic composition, skin external preparation composition or pharmaceutical composition of the present disclosure contains the components of the present disclosure within the content limits permitted by the relevant regulations and specifications of each country.

[0088] Advantages of the Invention

[0089] The skin condition improving effect of the peptide or its derivative for improving skin condition of the present disclosure is significantly excellent. The above peptide or its derivative can be usefully used as an active ingredient of a functional cosmetic composition or a skin external preparation composition applicable to the skin. Detailed Description of the Invention

[0090] Hereinafter, in order to assist in understanding the present invention, examples and the like will be given for detailed description. However, the examples of the present invention can be modified into various other forms, and the scope of the present invention should not be construed as being limited to the following examples. The examples of the present invention are provided to more completely explain the present invention to those of ordinary skill in the art. The raw materials used in the present invention are purchased and used from sales enterprises commonly used for commercial purposes.

[0091] Synthesis Example: Peptide Synthesis Method of Formula I

[0092] The peptide of Formula I above can be synthesized by the following synthesis method.

[0093] By performing a process including the following steps, the peptide of Formula I of the present disclosure can be prepared:

[0094] Step 1: A step of combining a hydrazine derivative protected with a "9-fluorenylmethoxycarbonyl" (hereinafter simply referred to as "Fmoc") group with a carbonyl compound, reacting it with Link amide resin, and activating the N-terminus to prepare a semicarbazide type resin;

[0095] Step 2: A step of removing a protecting group by a deprotection reaction of treating a protecting group Fmoc group attached to the nitrogen terminus of Fmoc-azagly-Link amide resin (azagly: azaglycyl, -NH-NH-CO-) in the first step with a reaction solvent such as 20% piperidine / DMF (dimethyl formamide).

[0096] Step 3: After the second step, a step of reacting amino acid derivatives Fmoc-Lys, Fmoc-Gly, Fmoc-Arg, Fmoc-Ser, Fmoc-Ser, Fmoc-Cys, Fmoc-Phe, Fmoc-Val, Fmoc-Asp, Fmoc-Cys in which both the amine terminus and the side chain are protected by protecting groups in sequence.

[0097] Step 4: A step of obtaining a peptide resin by removing the Fmoc group of the above peptide by the deprotection reaction of the second step.

[0098] Step 5: A step of adding a weakly acidic cleavage solution such as 2% TFA (trifluoroacetic acid) / DCM (dichloromethane) to the peptide resin in the fourth step, separating the peptide from the resin, and then removing the resin; and

[0099] Step 6: A step of adding a hydrazine solution to the above-separated peptide, removing benzyl, nitro (NO2), and Cbz (benzyloxyl carbonyl) in the side chain protecting groups by a catalytic hydrogen transfer reaction using reagents such as pd / c (palladium / catalyst) and cyclohexadiene, purifying the obtained peptide with a reverse phase column, and purifying it with an ion exchange resin.

[0100] Preparation Example 1: Cosmetic composition for improving skin condition (skin lotion)

[0101] According to the formulation described in Table 1 below, a skin lotion composition was prepared by a conventional method.

[0102] [Table 1]

[0103]

[0104] Preparation Example 2: Cosmetic composition for improving skin condition (scalp lotion)

[0105] Prepare a scalp lotion composition according to the formulation described in Table 2 below by a conventional method.

[0106] [Table 2]

[0107] Ingredients Weight ratio (%) Cetearyl Alcohol 2 Stearyl Triethyl Ammonium Chloride 2 Hydroxyethyl Cellulose 0.5 One selected from the peptides of SEQ ID NOs: 1 to 3 1 Fragrance and pigment Appropriate amount Purified water Balance (total 100)

[0108] Experimental Example 1: Inhibition of Collagenase Activity According to Sequence Variation

[0109] The collagenase used was collagenase derived from mouse pancreas, and as the substrate for collagenase, the synthetic substrate N-(3-[2-Furyl]acryloyl)-Leu-Gly-Pro-Ala was used. The buffer solution used was a solution containing 50 mM of tris(hydroxymethyl)methylglycine (Tricine), 10 mM of CaCl2·H2O, and 400 mM of NaCl (pH 7.5). After the synthetic substrate was dissolved at a concentration of 10 mM in the buffer solution, it was finally diluted to 75 μM. The collagenase was dissolved at a concentration of 1 unit / ml in cold triple-distilled water at 4°C and finally diluted to 0.05 unit / ml with the buffer solution. The collagenase inhibitor candidates were tested at final concentrations of 25 and 50 ppm. As a positive control group, epigallocatechin gallate (EGCG), which is known to have a collagenase inhibitory effect, was set at a final concentration of 50 ppm. The reaction was carried out in a 96-well plate and reacted at room temperature for 10 minutes. Using a spectrophotometer, the absorbance at 345 nm was measured at 1-minute intervals to obtain the maximum slope of the absorbance versus time, thereby confirming the enzyme activity inhibition rate.

[0110] [Table 3]

[0111] Treatment group Chemical formula I structure Treatment concentration Inhibition rate of collagenase activity (%) Untreated - Positive control group 100 μM 14.90 SEQ ID NO: 1 KGRSSCFVDC 100 μg / ml 22.91 SEQ ID NO: 2 KGRSSCFVD 100 μg / ml 25.69 SEQ ID NO: 3 KGRSSCF 100 μg / ml 22.98 SEQ ID NO: 4 KGRSSCFV 100 μg / ml 22.62 SEQ ID NO: 5 RSSCFVDC 100 μg / ml 12.23 SEQ ID NO: 6 SSCFVDC 100 μg / ml 17.97 SEQ ID NO: 7 GRSSCFVD 100 μg / ml 18.11 SEQ ID NO: 8 RSSCFVD 100 μg / ml 9.50 SEQ ID NO: 9 SSCFVD 100 μg / ml 18.79 SEQ ID NO: 10 KGSSCFVDC 100 μg / ml 15.24 SEQ ID NO: 11 KGRSSCFDC 100 μg / ml 11.82 SEQ ID NO: 12 KGRSSCFVC 100 μg / ml 13.97 SEQ ID NO: 13 RSSCF 100 μg / ml 10.97

[0112] Experimental Example 2: Inhibition of Collagenase and Elastase Activities According to Sequence Order Variation

[0113] In order to confirm whether there is an effect according to the change in the peptide sequence order, the activity of collagenase was confirmed as in Experimental Example 1 after sequence variation. Elastase from human leukocyte cells was used, and as the substrate for elastase, the synthetic substrate MeOSuc-Ala-Ala-Pro-Val-pNA was used. A 100 mM Tris (pH 7.5) solution was used as the buffer solution. Elastase was used at a final concentration of 0.2 mU with the buffer solution. In addition, the synthetic substrate of elastase was made into a 100 mM solution with DMSO and then diluted with the buffer solution to a final concentration of 0.5 mM. At this time, the positive control group was set to add quercetin, which is known as an elastase inhibitor, at a concentration of 10 ppm. The elastase inhibition candidate was added to a final concentration of 10, 20 ppm. The reaction was carried out in a 96-well plate and reacted at room temperature for 20 minutes. Using a spectrophotometer, the absorbance at 405 nm was measured at 1-minute intervals, and the slope of the absorbance versus time was obtained to determine the enzyme activity.

[0114] The efficacy component was treated with a peptide sequence consisting of any one of SEQ ID NOs: 14 to 16 at 100 μg / ml. As the control peptide sequence, the peptide sequence RKSLFVD was used for the test. The collagenase activity inhibition rate (%) and the elastase activity inhibition rate (%) were calculated as the ratio of the relative enzyme activity to the control group, and the results are shown in Table 4 below.

[0115] [Table 4]

[0116] Treatment group Treatment concentration Inhibition rate of collagenase activity (%) Inhibition rate of elastase activity (%) Untreated group - - Positive control group 100 μM 14.4 63.8 Peptide of SEQ ID NO: 1 100 μg / ml 21.57 72.1 Peptide of SEQ ID NO: 14 100 μg / ml 24.77 68.5 Peptide of SEQ ID NO: 2 100 μg / ml 19.7 70.9 Peptide of SEQ ID NO: 15 100 μg / ml 27.7 65.5 Peptide of SEQ ID NO: 3 100 μg / ml 26.3 57.8 Peptide of SEQ ID NO: 16 100 μg / ml 21.3 51.5 Control group peptide sequence 100 μg / ml 0.7 5.2

[0117] From the results in Table 4 above, the peptides of SEQ ID NOs: 1 to 3 and their reverse sequences, i.e., the peptides of SEQ ID NOs: 14 to 16, all inhibited the activities of collagenase and elastase. Thus, it was confirmed that the composition containing the above peptides can be used for skin wrinkle improvement, elasticity enhancement, or moisturizing purposes.

[0118] Experimental Example 3: Inhibition of Collagenase and Elastase Activities According to N-Terminal or C-Terminal Variation of the Sequence

[0119] In order to confirm whether there is an effect according to the N-terminal or C-terminal variation of the peptide sequence, the activities of collagenase and elastase were confirmed as in Experimental Example 1 after sequence variation.

[0120] [Table 5]

[0121]

[0122] From the results in Table 5 above, even when the N-terminal or C-terminal of the peptide sequence of SEQ ID NO: 1 was substituted, the activities of collagenase and elastase were significantly inhibited.

[0123] Experimental Example 4: Effect of improving skin wrinkles

[0124] With 25 men and women as subjects, the effect of improving wrinkles of the composition for improving skin condition disclosed in the present invention was tested. The 25 men and women were divided into 5 groups, with 5 people in each group. The products of Comparative Example 1 and Examples 1 to 4 were used to test the efficacy of improving periorbital wrinkles and forehead wrinkles for a total of 4 weeks.

[0125] The order of efficacy measurement was carried out at before use, 1 week after use, 2 weeks after use, and 4 weeks after use. In addition, during the human application test, except for the test products, the use of all cosmetics containing active ingredients that may affect the test results (for example, functional cosmetics such as whitening and wrinkle improvement) was prohibited. During the 4-week period, the test was carried out based on using 1 ml twice a day, morning and evening.

[0126] For the measurement of periorbital and forehead wrinkles, the 3D skin imaging device Antera 3D CS (Miravex Ltd., Ireland) was used to photograph the same left forehead area of the test subjects before and after using the test product. The stored photos were converted to the Wrinkles Medium mode, and for the analysis of periorbital wrinkles, a circle with a diameter of 10.7 mm (Cricle) was used to specify the analysis range including this area. For the analysis of periorbital wrinkles, the Indentation index value representing the average roughness (Ra) of the wrinkles within the indicated range was analyzed, with the unit of A.U., and for the forehead wrinkles, the Depth value representing the average depth of the wrinkles within the indicated range was analyzed. The reduction rate of periorbital and forehead wrinkles was expressed as a percentage relative to the non-coated time point. The measurement results are shown in Table 6 below in terms of the reduction rate of wrinkle density.

[0127] [Table 6]

[0128]

[0129] From the results shown in Table 6 above, it was confirmed that in Examples 1 to 4 containing the peptides of SEQ ID NOs: 1 to 3 or 14, the wrinkle inhibitory effect was significantly excellent.

[0130] Experimental Example 5: Effect of improving skin lipid secretion

[0131] Using 50 men and women as subjects, the lipid secretion inhibitory effect of the composition for improving skin condition of the present disclosure was tested. The 50 men and women were divided into 5 groups of 10 people each, and Comparative Example 1 and Examples 1, 3, 5, and 6 were used. Based on Example 1 in Table 1, Examples 5 and 6 were prepared by only changing the type of peptide. After the face was cleansed and air-dried naturally for 15 minutes, 1 ml of Comparative Example 1 was applied to the left side and 1 ml of Example 1, 3, 5, or 6 was applied to the right side on the forehead and cheek areas. The lipid production amount was measured 1 hour later. The method for measuring the lipid production amount used a sebum meter (Sebumeter). Comparative Example was applied to one side of the cheeks and Example was applied to the other side, and the measurement was carried out as a relative value with respect to the Comparative Example, and the results are shown in Table 7.

[0132] [Table 7]

[0133]

[0134] From the above results, it can be seen that in Examples 1, 3, 5, or 6 containing the peptide sequences of SEQ ID NO: 1, 2, 5, or 6, a high lipid secretion inhibitory effect was shown. Thus, it was demonstrated that the composition for improving skin condition of the present disclosure containing the peptide sequences of SEQ ID NO: 1, 2, 5, or 6 can be very effectively used for inhibiting lipid secretion.

[0135] The above dosage form examples such as skin lotion are only examples of the composition for improving skin condition of the present disclosure, and it will be obvious to those of ordinary skill in the art that the scope of the composition of the present disclosure is not limited to these dosage forms.

Claims

1. A peptide, which comprises an amino acid sequence of the following Chemical Formula I, its derivative or its isomer: <Chemical Formula I> X1-X2-X3-(S-S-C-F)-Y1-Y2-Y3 In the above, X1 is K or not included; X2 is G or not included; X3 is R or not included; Y1 is V or not included; Y2 is D or not included; and Y3 is C or not included.

2. The peptide according to claim 1, wherein The above peptide is used for improving skin condition.

3. The peptide according to claim 2, wherein The above improvement of skin condition includes any one or more selected from the group consisting of improvement of skin wrinkles, improvement of skin elasticity, improvement of skin moisture retention, inhibition of skin aging, and improvement of skin lipid secretion.

4. A cosmetic composition, which comprises the peptide described in Claim 1 as an active ingredient.

5. The cosmetic composition according to claim 4, wherein, The above cosmetic composition is used for improving skin condition.

6. The peptide according to claim 1, wherein, The amino acid sequence of the above Chemical Formula I is any one selected from the group consisting of the amino acid sequences of SEQ ID NO: 1 to 13.

7. A peptide, which comprises any one amino acid sequence selected from the group consisting of the amino acid sequences of SEQ ID NO: 14 to 16, its derivative or its isomer.

8. The peptide according to claim 7, wherein The above peptide is used for improving skin condition.

9. The peptide according to claim 8, wherein, The above improvement of skin condition includes any one or more selected from the group consisting of improvement of skin wrinkles, improvement of skin elasticity, improvement of skin moisture retention, inhibition of skin aging, and improvement of skin lipid secretion.

10. A peptide, which has a sequence identity of more than 80% with the amino acid sequence of the following Chemical Formula I: <Chemical Formula I> X1-X2-X3-(S-S-C-F)-Y1-Y2-Y3 In the above, X1 is K or not included; X2 is G or not included; X3 is R or not included; Y1 is V or not included; Y2 is D or not included; and Y3 is C or not included.

Citation Information

Patent Citations

  • Method and apparatus for performing conditional handover

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