KR101719355B1 - Peptides Having Activities of Skin Condition Improvement and Uses Thereof - Google Patents

Abstract

The peptide consisting of the sequence of SEQ ID No. 1 of the present invention, the sequence of SEQ ID No. 2, the sequence of SEQ ID No. 3 or the sequence of the 4th sequence of the present invention shows a skin condition improving activity. The peptide of the present invention exhibits antioxidative activity, inhibits skin cell death, increases collagen production, and has anti-inflammatory activity. The peptide of the present invention is very effective for improving skin conditions including wrinkle improvement, skin regeneration, skin elasticity improvement, skin aging inhibition, wound regeneration, skin regeneration, skin damage improvement by ultraviolet rays, and inflammatory skin disease alleviation. The present invention provides a composition for improving skin condition comprising the above-mentioned peptide.

Description

Peptides Having Activities of Skin Condition Improvement and Uses Thereof

The present invention relates to a peptide having a skin condition improving activity and a use thereof.

Human skin is constantly undergoing changes, the most representative of which is the decline in skin function and visual beauty due to aging. Skin aging is largely divided into internal aging according to genetic factors and external aging according to external environmental factors such as sunlight. Such external aging forms wrinkles in the skin, and representative wrinkle formation factors include reduced biosynthesis of free radicals, ultraviolet rays and collagen (Danielle, A study in the epidermiology of crow's feet., Ann. Intern. Med. , 75:873-880 (1971); Grove et al., Optical profilometry; an objective method for quantification of facial wrinkles., J. Am. Acad. Dermatol., 21:631-637 (1989)). In the case of internal aging of the skin, artificial control is not possible, but in the case of external aging, aging can be prevented, treated or delayed through the removal of active oxygen, proliferation of fibroblasts and promotion of collagen biosynthesis (Schwartz et al., Topical all -trans retinoic acid stimulates collagen synthesis in vivo., J. Invest. Dermatol., 96(6):975-978(1991)).

Throughout this specification, a number of papers and patent documents are referenced and citations are indicated. The disclosure contents of the cited papers and patent documents are incorporated by reference in this specification as a whole, and the level of the technical field to which the present invention belongs and the contents of the present invention are more clearly described.

As a result of the present inventors' efforts to develop excellent peptides having biologically effective activity, peptides having an amino acid sequence of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, or SEQ ID NO: 4 exhibit antioxidant activity. And suppresses skin cell death, increases collagen production, and suppresses inflammatory reactions, thereby completing the present invention.

Accordingly, an object of the present invention is to provide a peptide having an activity for improving skin conditions.

Another object of the present invention is to provide a composition for improving skin conditions.

Other objects and advantages of the present invention will become more apparent by the following detailed description, claims and drawings.

According to one aspect of the present invention, the present invention improves skin condition consisting of one amino acid sequence selected from the group consisting of Sequence Listing 1, Sequence Listing 2, Sequence Listing 3, and Sequence Listing 4 It provides a peptide having an activity.

As a result of the present inventors' efforts to develop excellent peptides having biologically effective activity, peptides having the amino acid sequence of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, or SEQ ID NO: 4 exhibit antioxidant activity. It was found that it has excellent physiological activity, such as inhibiting skin cell death, increasing collagen production, and inhibiting inflammatory reactions.

The peptide of the present invention includes an amino acid sequence of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, or SEQ ID NO: 4. Specifically, the peptide of the present invention consists essentially of the amino acid sequence of the first sequence of the sequence listing, the second sequence of the sequence listing, the third sequence of the sequence listing, or the fourth sequence of the sequence listing.

According to one embodiment of the present invention, the peptides of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, or SEQ ID NO: 4 exhibit antioxidant activity, inhibit the death of skin cells and inhibit collagen production. It increases and suppresses the inflammatory reaction, resulting in wrinkle improvement, skin regeneration, skin elasticity improvement, skin aging inhibition, wound regeneration, skin regeneration, improvement of skin damage caused by ultraviolet rays, and relief of inflammatory skin diseases.

According to another embodiment of the present invention, the anti-inflammatory activity of the peptide of the present invention is due to inhibition of the expression of inflammatory cytokines.

The term “peptide” as used herein refers to a linear molecule formed by bonding amino acid residues to each other by peptide bonds. The peptides of the present invention are chemically synthesized methods known in the art, in particular solid-phase synthesis techniques; Merrifield, J. Amer . Chem . Soc . 85:2149-54 (1963); Stewart, et al., Solid Phase Peptide Synthesis , 2nd.ed., Pierce Chem. Co.: Rockford, 111 (1984)) or liquid phase synthesis technology (US Patent No. 5,516,891).

According to an embodiment of the present invention, the N- or C-terminus of the peptide is an acetyl group, a fluorenyl methoxy carbonyl group, a formyl group, a palmitoyl group, a myristyl group, a stearyl group, and a polyethylene glycol (PEG). A protecting group selected from the group consisting of may be combined.

The above-described amino acid modification acts to greatly improve the stability of the peptide of the present invention. The term “stability” referred to in the present specification means not only “in vivo ” stability, but also storage stability (eg, room temperature storage stability). The above-described protecting group functions to protect the peptide of the present invention from attack by protein cleavage enzymes in vivo.

According to another aspect of the present invention, the present invention is a peptide consisting of one kind of amino acid sequence selected from the group consisting of the above-described sequence listing first sequence, sequence listing second sequence, sequence listing third sequence, and sequence listing fourth sequence. It provides a composition for improving skin conditions comprising as an active ingredient.

The composition of the present invention contains as an active ingredient a peptide consisting of the amino acid sequence of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or 4 of the present invention, as an active ingredient. In order to avoid excessive complexity of the present specification, the description is omitted.

As demonstrated in the following examples, the peptide consisting of the amino acid sequence of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3 or 4 of the present invention has antioxidant effect, and skin cells It includes anti-wrinkle, skin regeneration, skin elasticity improvement, skin aging inhibition, wound regeneration, skin regeneration, skin damage improvement due to ultraviolet rays, and relief of inflammatory skin diseases because it suppresses the death of blood, increases collagen production, and has anti-inflammatory activity. It is very effective in improving the skin condition.

According to certain embodiments of the present invention, the composition of the present invention comprises (a) a cosmetically effective amount of the peptide of the present invention described above; And (b) a cosmetically acceptable carrier.

As used herein, the term "cosmetically effective amount" means an amount sufficient to achieve the efficacy or activity of the above-described peptide.

The cosmetic composition of the present invention may be prepared in any formulation conventionally prepared in the art, for example, solution, suspension, emulsion, paste, gel, cream, lotion, powder, soap, surfactant-containing cleansing , Oil, powder foundation, emulsion foundation, wax foundation, and may be formulated as a spray, but is not limited thereto. In more detail, it may be prepared in the form of a flexible lotion, nutritional lotion, nutritional cream, massage cream, essence, eye cream, cleansing cream, cleansing foam, cleansing water, pack, spray or powder.

When the formulation of the present invention is a paste, cream or gel, animal oil, vegetable oil, wax, paraffin, starch, tracant, cellulose derivative, polyethylene glycol, silicone, bentonite, silica, talc, or zinc oxide may be used as a carrier component. I can.

When the formulation of the present invention is a powder or spray, lactose, talc, silica, aluminum hydroxide, calcium silicate, or polyamide powder may be used as a carrier component. In particular, in the case of a spray, additionally chlorofluorohydrocarbon, propane / May contain propellants such as butane or dimethyl ether.

When the formulation of the present invention is a solution or emulsion, a solvent, a solubilizing agent or an emulsifying agent is used as a carrier component, such as water, ethanol, isopropanol, ethyl carbonate, ethyl acetate, benzyl alcohol, benzyl benzoate, propylene glycol, 1 ,3-butylglycol oil, glycerol aliphatic ester, polyethylene glycol or fatty acid ester of sorbitan.

When the formulation of the present invention is a suspension, as a carrier component, a liquid diluent such as water, ethanol or propylene glycol, an ethoxylated isostearyl alcohol, a suspending agent such as polyoxyethylene sorbitol ester and polyoxyethylene sorbitan ester, and crystallites Sex cellulose, aluminum metahydroxide, bentonite, agar or tracanth, and the like can be used.

When the formulation of the present invention is a surfactant containing cleansing, as a carrier component, aliphatic alcohol sulfate, aliphatic alcohol ether sulfate, sulfosuccinic acid monoester, isethionate, imidazolinium derivative, methyltaurate, sarcosinate, fatty acid amide Ether sulfates, alkylamidobetaines, fatty alcohols, fatty acid glycerides, fatty acid diethanolamides, vegetable oils, lanolin derivatives or ethoxylated glycerol fatty acid esters may be used.

Ingredients included in the cosmetic composition of the present invention include ingredients commonly used in cosmetic compositions, in addition to peptides and carrier ingredients as active ingredients, such as antioxidants, stabilizers, solubilizers, vitamins, pigments, and perfumes. May contain adjuvants.

The features and advantages of the present invention are summarized as follows:

(i) The peptide consisting of the first sequence of the present invention, the second sequence of the sequence list, the third sequence of the sequence list, or the fourth sequence of the sequence list exhibits skin condition improvement activity.

(ii) The peptide of the present invention exhibits antioxidant activity, inhibits the death of skin cells, increases collagen production, and has anti-inflammatory activity.

(iii) The peptide of the present invention is very effective in improving skin conditions including wrinkle improvement, skin regeneration, skin elasticity improvement, skin aging inhibition, wound regeneration, skin regeneration, skin damage improvement due to ultraviolet rays, and inflammatory skin disease relief.

(iv) The present invention provides a composition for improving skin conditions comprising the above-described peptide.

1a-1d is a graph confirming the effect of inhibiting increase in ROS in skin cells by ultraviolet rays after treatment with the peptide of the present invention.
2A-2B are results of confirming the effect of inhibiting cell death by ultraviolet rays after treatment with the peptide of the present invention.
3A-D are results of measuring the expression level of p-p53 according to the peptide treatment of the present invention.
4A-4D are results of measuring the expression level of Bcl2 according to the peptide treatment of the present invention.
5A-5D are results of measuring the expression level of pERK according to the peptide treatment of the present invention.
6A-6B are results of measuring the expression level of an inflammatory cytokine gene according to the peptide treatment of the present invention by RT-PCR.
7A-7D are results of measuring the expression level of COX2 according to the peptide treatment of the present invention.
8A-8D are results of measuring the expression level of TNF-α according to the peptide treatment of the present invention.
9A-9D are results of measuring the expression level of MMP1 according to the peptide treatment of the present invention.
10A-10B are results of measuring changes in the amount of active oxygen in cells increased by ultraviolet rays after peptide treatment of the first and second sequences of the Sequence Listing of the present invention.
11 is a result of measuring the expression level of the pro-collagen gene according to the treatment of the peptide of SEQ ID NO: 2 of the present invention.

Hereinafter, the present invention will be described in more detail through examples. These examples are only for describing the present invention in more detail, and it will be apparent to those of ordinary skill in the art that the scope of the present invention is not limited by these examples according to the gist of the present invention. .

Example

Synthesis Example 1: Peptide Synthesis

700 mg of chloro trityl chloride resin (CTL resin, Nova biochem Cat No. 01-64-0021) was placed in a reaction vessel, and 10 ml of methylene chloride (MC) was added, followed by stirring for 3 minutes. The solution was removed, 10 ml of dimethylformamide (DMF) was added, stirred for 3 minutes, and the solvent was removed again. 10 ml of dichloromethane solution was added to the reactor, 200 mmole of Fmoc-Gly-OH (Bachem, Swiss) and 400 mmole of diisopropyl ethylamine (DIEA) were added, then stirred to dissolve well, and reacted with stirring for 1 hour. After the reaction was washed, methanol and DIEA (2:1) were dissolved in DCM (dichloromethane), reacted for 10 minutes, and washed with an excess of DCM/DMF (1:1). The solution was removed, 10 ml of dimethylformamide (DMF) was added, stirred for 3 minutes, and the solvent was removed again. 10 ml of a deprotection solution (20% piperidine/DMF) was added to the reaction vessel and stirred at room temperature for 10 minutes, and then the solution was removed. After the same amount of the deprotection solution was added and the reaction was maintained for another 10 minutes, the solution was removed and washed twice with DMF, once with MC, and once with DMF for 3 minutes each to prepare Gly-CTL resin. 10 ml of DMF solution was added to a new reactor, 200 mmole of Fmoc-Cys (Bachem, Swiss), 200 mmole of HoBt and 200 mmole of Bop were added, followed by stirring to dissolve well. After adding 400 mmole DIEA to the reactor twice as a fraction, the mixture was stirred for at least 5 minutes until all solids were dissolved. The dissolved amino acid mixture solution was placed in a reaction vessel with a deprotected resin and reacted with stirring at room temperature for 1 hour. The reaction solution was removed, and the mixture was stirred 3 times for 5 minutes with a DMF solution, and then removed. A small amount of reaction resin was taken and the degree of reaction was checked using a Kaiser test (Nihydrin Test). Cys-Gly-CTL resin was prepared by performing a deprotection reaction twice in the same manner as above with a deprotection solution. After sufficiently washing with DMF and MC, performing the Kaiser test again, the following amino acid adhesion experiment was performed in the same manner as above. Fmoc-Ile, Fmoc-Trp, Fmoc-Lys(Boc), Fmoc-Glu(OtBu), Fmoc-Ser(tBu), Fmoc-Ser(tBu) and Fmoc-Glu(OtBu) in order based on the selected amino acid sequence The chain reaction was carried out. The Fmoc-protecting group was reacted twice with a deprotection solution for 10 minutes each, and then washed well and removed. After performing acetylation for an hour by adding acetic anhydride, DIEA, and HoBt, the prepared peptidyl resin was washed 3 times with DMF, MC and methanol, respectively, and dried by slowly flowing nitrogen air, and then P ₂ O ₅ Decompression solution under vacuum and dry completely (Trifluroacetic acid 81.5%, distilled water 5%, thioanisole 5%, phenol (Phenol) 5%, EDT 2.5% and TIS 1%) ] After adding 30 ml, the reaction was maintained for 2 hours by occasionally shaking at room temperature. The resin was filtered by filtering, and the resin was washed with a small amount of TFA solution and then combined with the mother liquor. After distillation using reduced pressure so that the total volume remains about half, 50 ml of cold ether was added to induce precipitation, centrifuged to collect the precipitate, and washed with cold ether twice. The mother liquor was removed and sufficiently dried under nitrogen _{to synthesize 0.78 g of NH 2} -Glu-Ser-Ser-Glu-Lys-Trp-Ile-Cys-Gly-COOH peptide 1 (yield: 88.6%) before purification. 0.72 g of NH ₂ -Thr-Glu-Trp-Thr-Ala-Ser-Lys-Ser-Gly-COOH peptide 2 was synthesized (yield: 81.8%), NH ₂ -Glu-Gln-Leu-Glu-Arg-Ala 0.69 g of -Leu-Asn-Ser-Ser-COOH peptide 3 was synthesized (yield: 78.4%), _{and 0.75 g of NH 2} -Arg-Ala-Leu-Leu-Val-Asn-Ser-Ser-COOH peptide 4 was synthesized. (Yield: 85.2%). When measured using a molecular weight meter, the molecular weight of peptide 1 is 1038.0 (theoretical value: 1038.1), the molecular weight of peptide 2 is 965.9 (theoretical value: 966.0), the molecular weight of peptide 3 is 1146.3 (theoretical value: 1146.2), and the molecular weight of peptide 4 is 859.0 (theoretical value). Value: 858.9) was obtained.

Peptide Amino acid sequence Analysis value (mass spectrometer) Analysis value Theoretical value SEQ ID NO: 1 ESSEKWICG 1038.0 1038.1 SEQ ID NO: 2 TEWTASKSG 965.9 966.0 SEQ ID NO: 3 EQLERALNSS 1146.3 1146.2 SEQ ID NO: 4 RALLVNSS 859.0 858.9

Example 1: caused by ultraviolet rays Skin cell Intracellular ROS Increase inhibition experiment

Seed HaCaT (human keratinocyte line) in a 6-well plate at a cell density of 2×10 ^{5 cells/well.} After incubation for one night, the peptides of Sequence Listing 1 to 4 were treated by concentration (1-10 μg/ml) and incubated in an incubator at 37° C. for 30 minutes and then irradiated with UVB (25 mJ) at 37° C. Incubate for 48 hours in an incubator. The cells were treated with DCFH-DA (sigma) at a concentration of 10 μM and incubated in an incubator at 37° C. for 30 minutes to obtain cells. After centrifugation (6,000 rpm, 3 minutes) by adding 1 ml of PBS, 600 μl of PBS was added again to perform FACS analysis.

As a result of measuring the amount of increase in free radicals in keratinocytes generated during UVB irradiation through flow cytometry, the effective reduction ability of increased intracellular free radicals was confirmed in all of the peptides of SEQ ID NOs: 1 to 4 (Fig. 1a- 1d). This affects cytokines and apoptosis in inflammation induced by the initial intracellular ROS increase signal, and as a result, it is expected to have a preventive effect against skin aging caused by ultraviolet rays.

Example 2: Inhibition of skin cell death by ultraviolet rays (western blotting)

Seed NIH3T3 (epidermal cell line) in a 6-well plate at a cell density of 2×10 ^{5 cells/well.} After incubation for one night, the peptides of Sequence Listing 1 to 4 were treated at different concentrations (1-10 μg/ml) and incubated in an incubator at 37° C. for 30 minutes, followed by UVA (8 J) irradiation at 37° C. Incubate for 24 hours in an incubator. Protein is quantified after obtaining a lysate by treating the cell lysis buffer. Anti-pp53 antibody (Santa Cruz Biotechnology, USA) to confirm the expression of apoptosis factor, anti-pE antibody (Santa Cruz Biotechnology, USA) and anti-Bcl2 antibody (Santa Cruz Biotechnology) to confirm the expression of apoptosis inhibitors , USA) was used to perform Western blot.

During the apoptosis mechanism that occurs during UVA irradiation, the degree of bcl - 2 expression of pp53 and the function of inhibiting cell death was confirmed. In all treatment groups, it was confirmed that pp 53 inhibition, increased Bcl2, increased cell survival, and ERK phosphorylation, a protein involved in activity (Figs. 2a-2b, 3a-3d, 4a-4d, and 5a-5d), which is a sequence listing When the peptides of the first to fourth sequences are treated, apoptosis due to ultraviolet rays is suppressed and, on the contrary, cell activity is increased (p-p53→hospho-p53, pERK→hospho-ERK).

Example 3: Inhibition of expression of inflammatory cytokines in skin cells by ultraviolet rays (RT-PCR)

Seed NIH3T3 (epidermal cell line) in a 6-well plate at a cell density of 2×10 ^{5 cells/well.} After incubation for one night, the peptides of Sequence Listing 1 to 4 were treated at different concentrations (1-10 μg/ml) and incubated in an incubator at 37° C. for 30 minutes, followed by UVA (8 J) irradiation at 37° C. Incubate for 12 hours in an incubator. After recovering the cultured cells, RNA is prepared by processing an RNA extraction solution (Easy Blue, Intron), and cDNA is synthesized using RT premix (Intron). PCR was performed using primers for inflammation inducing factors (COX2, TNF-alpha) and cell structure degradation factor (MMP1) and a PCR premix (Intron). The target-specific primer sequence used for PCR of the inflammation inducing factor and the cytostructuring factor is as follows:

COX2 forward primer sequence, 5'-TTGGTCTACAAGACGCCACA-3' and COX2 reverse primer, 5'-CGGTTAATACGGGGTTGTTG-3' (annealing temperature, 60° C.);

TNF-alpha forward primer sequence, 5'-CGTCAGCCGATTTGCTATCT-3' and TNF-alpha reverse primer, 5'-CGGACTCCGCAAAGTCTAAG-3' (annealing temperature, 60° C.);

MMP1 forward primer sequence, 5'-ATTCTACTGATATCGGGGCTTTGA-3' and MMP1 reverse primer, 5'-ATGTCCTTGGGGTATCCGTGTAG-3' (annealing temperature, 60° C.).

After loading 5 μl of the PCR product on a 1% agarose gel each, check the band in Gel-Doc.

As a result of confirming the expression level of the inflammatory cytokine gene after treatment with the peptides of SEQ ID NOs: 1 to 4 of the Sequence Listing, all four types effectively reduced the increase in the expression of the inflammatory cytokine gene induced by UVA (Figs. 6a-6b, Figures 7a-7d and 8a-8d). In addition, inhibition of MMP1 expression, which is an ECM degrading enzyme, was also confirmed (Figs. 9a-9d).

Example 4: Experiment of inhibition of increase in intracellular ROS by ultraviolet rays in NIH3T3 (epidermal cell line)

Seed NIH3T3 (epidermal cell line) in a 6-well plate at a cell density of 2×10 ^{5 cells/well.} After incubating overnight, the peptides of the first and second sequences of the Sequence Listing were treated at different concentrations (1-10 μg/ml), incubated in an incubator at 37° C. for 30 minutes, and then irradiated with UVB (8 J). Incubate for 48 hours in an incubator at ℃. The cells were treated with DCFH-DA (sigma) at a concentration of 10 μM and incubated in an incubator at 37° C. for 30 minutes to obtain cells. After centrifugation (6,000 rpm, 3 minutes) by adding 1 ml of PBS, 600 μl of PBS was added again to perform FACS analysis.

As a result of measuring the amount of active oxygen increase in keratinocytes and epidermal cells (fibroblasts) caused by UVB irradiation through flow cytometry, the effective reduction ability of the increased intracellular free radicals was found in the peptides of the first and second sequences of the Sequence Listing. It was confirmed in (Figs. 10a-10b). This affects cytokines and apoptosis in inflammation induced by the initial intracellular ROS increase signal, and as a result, it is expected to have a preventive effect against skin aging caused by ultraviolet rays.

Example 5: Experiment to increase the expression of collagen type 1α chain in NIH3T3 (epidermal cell line)

Seed NIH3T3 (epidermal cell line) in a 6-well plate at a cell density of 2×10 ^{5 cells/well.} After incubation overnight, 10 μg/ml of the peptide of SEQ ID NO: 2 was treated and incubated in an incubator at 37° C. for 24 hours. After recovering the cultured cells, RNA is prepared by processing an RNA extraction solution (Easy Blue, Intron), and cDNA is synthesized using RT premix (Intron). PCR is performed using a primer for the extracellular construct (Collagen type 1 a chain) and a PCR premix (Intron). The target-specific primer sequence used for PCR of the extracellular construct is as follows:

Collagen type 1 a chain forward primer sequence, 5'-CTCGAGGTGGACACCACCCT-3' and Collagen type 1 a chain reverse primer sequence, 5'-CAGCTGGATGGCCACATCGG-3' (annealing temperature, 60°C).

After loading 5 μl of the PCR product on a 1% agarose gel each, check the band in Gel-Doc.

The expression level of the collagen type 1α chain is increased when the peptide of the second sequence in the sequence listing is treated (Fig. 11), which can be expected to prevent wrinkles by increasing collagen production along with the function of inhibiting the increase of collagen-degrading enzymes caused by ultraviolet rays. .

As described above, a specific part of the present invention has been described in detail, and it is clear to those of ordinary skill in the art that this specific technology is only an embodiment, and the scope of the present invention is not limited thereto. Therefore, it will be said that the practical scope of the present invention is defined by the appended claims and their equivalents.

<110> CAREGEN Co,. Ltd. <120> Peptides Having Activities of Skin Condition Improvement and Uses Thereof <130> PN130679D <160> 12 <170> KopatentIn 2.0 <210> 1 <211> 9 <212> PRT <213> Artificial Sequence <220> <223> Peptide 1 <400> 1 Glu Ser Ser Glu Lys Trp Ile Cys Gly 1 5 <210> 2 <211> 9 <212> PRT <213> Artificial Sequence <220> <223> Peptide 2 <400> 2 Thr Glu Trp Thr Ala Ser Lys Ser Gly 1 5 <210> 3 <211> 10 <212> PRT <213> Artificial Sequence <220> <223> Peptide 3 <400> 3 Glu Gln Leu Glu Arg Ala Leu Asn Ser Ser 1 5 10 <210> 4 <211> 8 <212> PRT <213> Artificial Sequence <220> <223> Peptide 4 <400> 4 Arg Ala Leu Leu Val Asn Ser Ser 1 5 <210> 5 <211> 20 <212> DNA <213> Artificial Sequence <220> <223> COX2 Forward Primer <400> 5 ttggtctaca agacgccaca 20 <210> 6 <211> 20 <212> DNA <213> Artificial Sequence <220> <223> COX2 Reverse Primer <400> 6 cggttaatac ggggttgttg 20 <210> 7 <211> 20 <212> DNA <213> Artificial Sequence <220> <223> TNF-alpha Forward Primer <400> 7 cgtcagccga tttgctatct 20 <210> 8 <211> 20 <212> DNA <213> Artificial Sequence <220> <223> TNF-alpha Reverse Primer <400> 8 cggactccgc aaagtctaag 20 <210> 9 <211> 24 <212> DNA <213> Artificial Sequence <220> <223> MMP1 Forward Primer <400> 9 attctactga tatcggggct ttga 24 <210> 10 <211> 23 <212> DNA <213> Artificial Sequence <220> <223> MMP1 Reverse Primer <400> 10 atgtccttgg ggtatccgtg tag 23 <210> 11 <211> 20 <212> DNA <213> Artificial Sequence <220> <223> Collagen type 1 a chain Forward Primer <400> 11 ctcgaggtgg acaccaccct 20 <210> 12 <211> 20 <212> DNA <213> Artificial Sequence <220> <223> Collagen type 1 a chain Reverse Primer <400> 12 cagctggatg gccacatcgg 20

Claims (7)

A peptide having a skin condition improving activity comprising an amino acid sequence selected from the group consisting of SEQ ID NO: 1, SEQ ID NO: 2 and SEQ ID NO: 4, wherein the skin condition is inhibited by skin aging, Lt; / RTI &gt; wherein the peptide is an amelioration of skin damage or an inflammatory skin disease. The peptide according to claim 1, wherein the peptide has an antioxidative activity. The peptide according to claim 1, wherein the peptide inhibits skin cell death. 2. The peptide of claim 1, wherein the peptide consisting of the amino acid sequence of the second sequence of sequence listing increases collagen production. The peptide according to claim 1, wherein the peptide has an anti-inflammatory activity. 6. The peptide of claim 5, wherein the inflammation-inhibiting activity is by inhibiting the expression of inflammatory cytokines. A composition for improving skin condition comprising the peptide according to any one of claims 1 to 6 as an active ingredient, wherein the skin condition is improved wrinkles or skin elasticity.

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