A pentapeptide-derived peptide segment ys against skin aging and application thereof

Abstract

This invention provides a pentapeptide-derived peptide YS for anti-skin aging and its applications, relating to the field of biochemistry. The pentapeptide-derived peptide YS comprises KTTKS and an N-terminal modified peptide. The N-terminal modified peptide consists of basic amino acids and uncharged amino acids arranged alternately, with the number of basic amino acids not less than 50%. The uncharged amino acids are selected from neutral amino acids and / or polar neutral amino acids. The number of uncharged amino acids arranged consecutively does not exceed three. The N-terminal amino acid of the N-terminal modified peptide is tyrosine, and the C-terminus consists of three consecutive uncharged amino acids. This invention modifies the N-terminus of the pentapeptide KTTKS with a specific structure of amphiphilic peptide, unexpectedly obtaining a pentapeptide-derived peptide YS with good water solubility and strong skin penetration, exhibiting significant anti-skin aging effects without the need for additional chemical penetration enhancers, making it safer and more effective.

Description

TECHNICAL FIELD

[0001] The present application relates to the field of biochemical technology, and particularly relates to a skin anti-aging pentapeptide derivative YS and application thereof. BACKGROUND

[0002] Skin aging is a complex process, mainly due to endogenous and exogenous factors. Endogenous factors refer to natural physiological aging, with the growth of epidermal keratinocytes and dermal fibroblasts slowing down, the number of epidermal fibroblasts gradually decreasing, and the ability of collagen synthesis decreasing. At the same time, due to the increase of protease release, the degradation of collagen increases, and although the content of elastic fibers does not decrease, the elastic fiber network curls, relaxes, loses elasticity, and even disappears, causing the epidermis to relax and form fine wrinkles. At the same time, the thickening of the fiber bundle also increases the depth of the wrinkles. Ultraviolet radiation also causes the degradation of collagen fiber bundles, damages the elasticity of the skin, and thus increases the wrinkles, and ultraviolet radiation can also deform the elastic fibers, thicken, twist and fork the fibers, and accumulate over time to cause skin relaxation and wrinkles.

[0003] In the research of skin anti-aging, the main focus is on promoting cell division and proliferation, promoting the synthesis of collagen and elastic fibers, moisturizing and repairing skin barrier function, etc. Many anti-aging drugs and cosmetics on the market promote cell division and proliferation, accelerate the rate of epidermal keratinocyte shedding, stimulate basal cell division, and improve the appearance of the skin in the short term. However, due to the limitation of the life span and the number of cell divisions of normal skin cells, excessive acceleration of cell division will shorten the cell division cycle and thus shorten the cell life span and accelerate aging. Therefore, increasing the secretion of collagen in skin cells is an important and promising new direction for improving the appearance of the skin.

[0004] Collagen produces some small peptide fragments in the process of metabolism, some small peptide fragments such as KTTKS (pentapeptide) can stimulate fibroblasts to secrete collagen (A Pentapeptide from Type I Procollagen Promotes Extracellular Matrix Production, THE JOURNAL OF BIOLOGICAL CHEMISTRY, 1993, Vol. 268(14): 9941-9944). Many cosmetic companies are very interested in the application of these small molecule peptides in cosmetics. However, these small molecule peptides are hydrophilic, and their ability to penetrate the skin is very weak. Some researchers have used palmitoylation at the N-terminus of these small molecule peptides, and the results show that these palmitoylated small molecule peptides can effectively improve the properties of the skin (US2007 / 0099842A1). Even so, the efficiency of transdermal absorption is very limited, and often requires the addition of some penetration enhancers in cosmetics. In addition, the palmitoylated peptide molecules have poor water solubility, and organic solvents must be used when making cosmetics, which inevitably causes some irritation to the skin. SUMMARY

[0005] Since the skin penetration of the pentapeptide KTTKS is poor, and the transdermal absorption of the palmitoylated modified KTTKS (PAL-KTTKS) still needs to be improved, the present application modifies a specific structure of an amphiphilic peptide segment at the N segment of the pentapeptide KTTKS, and unexpectedly obtains a pentapeptide derivative peptide segment YS with good water solubility and strong skin penetration ability, which has a significant anti-aging effect on the skin, and does not require additional chemical penetration enhancers, and is more safe and effective.

[0006] In order to achieve the above-mentioned purposes of the application, the first aspect of the present application provides an anti-aging pentapeptide derivative peptide segment YS, which comprises KTTKS and an N-terminal modified peptide segment; the N-terminal modified peptide segment is arranged in intervals between basic amino acids and uncharged amino acids, and the number of basic amino acids is not less than 50%; the uncharged amino acids are selected from neutral amino acids and / or polar neutral amino acids; the uncharged amino acids are arranged continuously for not more than 3; the N-terminal amino acid of the N-terminal modified peptide segment is tyrosine, and the C-terminal is 3 consecutive uncharged amino acids.

[0007] Preferably, the N-terminal modified peptide segment at least comprises a structure as shown in formula (I):

[0008] (Xaa)m-X'aa-(Xaa)n (I)

[0009] Wherein, Xaa represents a basic amino acid, X'aa represents a neutral amino acid / polar neutral amino acid; m, n are independently selected from integers of 1-3.

[0010] Preferably, the structure shown in formula (I) is selected from KKSKK (SEQ ID NO.7), RRQRR (SEQ ID NO.8), KKTHK (SEQ ID NO.9) or KKQKK (SEQ ID NO.10).

[0011] Preferably, the structure of the N-terminal modified peptide is as shown in formula (II):

[0012] (X'aa)p-(Xaa)q-(X'aa)r-(Xaa)m-X'aa-(Xaa)n-X'aa-GG (II)

[0013] Where Xaa represents basic amino acids, and X'aa represents neutral amino acids / polar neutral amino acids;

[0014] p, q, and r are independently selected from integers between 0 and 3.

[0015] Preferably, the pentapeptide-derived peptide YS includes one or more of the following: YGRTS KKSKK SGGKT TKS (SEQ ID NO.1), YGRKKRRQRR MGGKT TKS (SEQ ID NO.2), YGHTS KKTHK SGGKT TKS (SEQ ID NO.3), YKKTS KKQKKSGGKT TKS (SEQ ID NO.4), and YGRTS RRQRR MGGKT TKS (SEQ ID NO.5).

[0016] Preferably, the uncharged amino acid is selected from one or more of threonine, serine, tyrosine, glycine, methionine, and glutamine.

[0017] A second aspect of the present invention provides the application of the pentapeptide-derived peptide YS described above in the preparation of anti-skin aging agents; preferably, the anti-skin aging includes one or more of promoting collagen I synthesis, increasing skin thickness, and reducing skin wrinkles. The anti-skin aging agents of the present invention can be pharmaceuticals or cosmetics.

[0018] A third aspect of the present invention provides an anti-skin aging composition comprising an active ingredient and excipients, wherein the active ingredient comprises the pentapeptide-derived peptide YS described in the above-described technical solution.

[0019] Preferably, the excipients in this invention include, but are not limited to, one or more of the following: diluents, excipients, fillers, binders, humectants, disintegrants, surfactants, adsorbents, lubricants, fragrances, and sweeteners acceptable for pharmaceuticals or cosmetics. The pentapeptide-derived peptide YS provided by this invention has excellent hydrophilicity and lipophilicity, and can be efficiently absorbed by the skin and exert its anti-skin aging effect without the need for penetration enhancers or other chemical components. Therefore, the anti-skin aging composition of this invention may not contain penetration enhancers, but the inclusion of penetration enhancers will further increase the skin permeability of the pentapeptide-derived peptide YS.

[0020] The anti-skin aging composition of this invention can be formulated into various dosage forms such as tablets, powders, granules, and ointments. All of these dosage forms can be prepared using conventional methods in the pharmaceutical field. Preferably, the anti-skin aging composition of this invention is a topical patch for local administration.

[0021] The active components in the anti-skin aging composition of the present invention may also include other effective ingredients that have skin care effects or enhance skin care effects and prolong metabolic time.

[0022] Compared with the prior art, the beneficial effects of the present invention are as follows:

[0023] Cell-penetrating peptides, possessing both hydrophilic and lipophilic properties, can carry peptides, DNA, and even larger particles into cells due to their unique molecular structure (Fawell S et al. (1994) Tat-mediated delivery of heterologous proteins into cells. Proc Natl Acad Sci USA 91:664–668). This invention unexpectedly discovered that modifying the N-terminus of the pentapeptide KTTKS with a structure of "(Xaa)m-X'aa-(Xaa)n-(X'aa)q-GG" (this modified peptide has an amphiphilic helical structure, with one side of the helical structure consisting of basic amino acids and the other side consisting of neutral or polar neutral amino acids (uncharged) interspersed), yields the pentapeptide-derived peptide YS as shown in formula (I). This peptide exhibits good hydrophilicity and high skin permeability; direct local application can significantly increase the expression of type I collagen, increase skin thickness, and reduce skin wrinkles, achieving a significant anti-aging effect.

[0024] Transdermal absorption assays in nude mice showed that the skin penetration ability of the pentapeptide-derived peptide YS (YS) provided by this invention can reach over 2%. In vitro and in vivo animal experiments showed that the pentapeptide-derived peptide YS provided by this invention has a stimulating effect on collagen secretion in HFL-1, and has the ability to penetrate the skin of nude mice, exhibiting significant improvements in skin properties such as increased skin thickness and reduced skin wrinkles in aged nude mice. It can be seen that the pentapeptide-derived peptide YS described in this invention can effectively deliver the pentapeptide KTTKS into the skin while maintaining its activity, and can effectively improve skin condition, showing promising application potential in the preparation of cosmetics and pharmaceuticals for improving skin condition. Attached Figure Description

[0025] Figure 1 This is a perspective view of the pentapeptide-derived peptide YS of the present invention (red markings indicate basic amino acids);

[0026] Figure 2 The figure shows the results of type I collagen mRNA expression detection after HLF-1 cells were treated with different peptides in Example 4; 1, 2, 3, and 4 in the figure are the NS group, YS2, YS1, and PAL group, respectively.

[0027] Figure 3 This is a graph showing the expression levels of type I collagen in HLF-1 cells after treatment with different peptides in Example 4; in the graph, 1, 2, 3, 4, and 5 represent YS2, NS, YS1, maker, and PAL, respectively.

[0028] Figure 4 This is a graph showing the in situ detection results of type I collagen expression in HLF-1 cells after treatment with different peptides in Example 5; in the figure, 1, 2, 3, and 4 represent NS, YS2, PAL, and YS1, respectively.

[0029] Figure 5 The figure shows the results of detecting collagen content in nude mouse skin using the MASSAN staining method in Example 6; in the figure, A, C, and E are YS2, YS1, and PAL preparations, respectively, and B, D, and F are NS controls. Detailed Implementation

[0030] In this invention, unless otherwise specified, the polypeptide is arranged from left to right from N-terminus to C-terminus.

[0031] In this invention, "basic amino acids" refer to positively charged amino acids whose R group is polar and dissociated, exhibiting basicity in neutral solutions, including lysine (K), arginine (R), and histidine (H). In this invention, "polar-neutral amino acids" refer to amino acids whose R group is polar but not dissociated or only weakly dissociated, including threonine (T), serine (S), cysteine ​​(C), tyrosine (Y), glutamine (Q), asparagine (N), and methionine (M). In this invention, "nonpolar amino acids" can be glycine (G).

[0032] The technical solutions provided by the present invention will be described in detail below with reference to the embodiments, but they should not be construed as limiting the scope of protection of the present invention. Experimental methods in the following embodiments without specific conditions are generally performed under conventional conditions or according to the manufacturer's recommendations. All raw materials without specified synthesis methods were purchased from manufacturers such as Sinopharm, Aladdin, and Sigma-Aldrich, and were of analytical grade.

[0033] Example 1: Synthesis of the pentapeptide-derived peptide YS (YS)

[0034] The following polypeptide fragments were synthesized using the method described below. All reagents were purchased from Applied Biosystems, Inc.

[0035] YS1(SEQ ID NO.1):YGRTS KKSKK SGGKT TKS

[0036] YS2(SEQ ID NO.2):YGRKK RRQRRMGGKT TKS

[0037] YS3(SEQ ID NO.3):YGHTS KKTHK SGGKT TKS

[0038] YS4(SEQ ID NO.4):YKKTS KKQKK SGGKT TKS

[0039] YS5(SEQ ID NO.5):YGRTS RRQRR MGGKT TKS

[0040] 1. Synthesis proceeds sequentially from the C-end to the N-end, and is automatically controlled by the synthesizer.

[0041] First, weigh an appropriate amount of resin (purchased from Applied Biosystems, USA) containing the first amino acid, Ser, pack it into a column, and then deprotect it with 20% piperidine dimethylformamide solution. After washing with dimethylformamide, dissolve the free amino acid protected by 9-fmoc in carbodiimide (DCC), hydroxybenzotriazole (HOBt) / diisopropylethylamine (DIPEA), and circulate the solution on the column for 30 minutes for coupling reaction. After washing with dimethylformamide, repeat the above deprotection and coupling reaction steps until the synthesis is complete (see the Pioneer Peptide Synthesizer Operation Guide for specific operating procedures).

[0042] 2. The synthesized polypeptide is cleaved through the following steps:

[0043] Remove the resin after reaction, add type B shearing fluid (88% trifluoroacetic acid, 5% phenol, 5% water, 2% triisopropylsilane), react at room temperature for 2 hours, filter, add 10 times the volume of pre-cooled anhydrous diethyl ether to the filtrate, centrifuge at 4000 rpm for 10 minutes, collect the precipitate and dry at room temperature.

[0044] 3. Purification of peptides

[0045] Weigh a certain amount of the dried polypeptide, dissolve it in 0.1% trifluoroacetic acid, and after sample processing, separate it by reverse column chromatography (elution buffer is 0.1% trifluoroacetic acid containing 80% acetic acid), and collect the elution peak.

[0046] Example 2

[0047] This experiment was used to verify the ability of the pentapeptide-derived peptide YS to penetrate the skin of nude mice.

[0048] 1. Sample to be tested

[0049] Experimental group 1: YS1 polypeptide (SEQ ID NO.1) prepared in Example 1.

[0050] Experimental group 2: YS2 polypeptide (SEQ ID NO.2) prepared in Example 1.

[0051] Experimental group 3: YS3 polypeptide (SEQ ID NO.3) prepared in Example 1.

[0052] Experimental group 4: YS4 polypeptide (SEQ ID NO.4) prepared in Example 1.

[0053] Experimental group 5: YS5 polypeptide (SEQ ID NO.5) prepared in Example 1.

[0054] Control group: Peptide NS prepared according to the method shown in Example 1, as shown in SEQ ID NO.6: NKKTSKKSKK SGGKT TKS.

[0055] 2. Experimental Methods

[0056] First, prepare the ex vivo mouse skin by taking a nude mouse about 8 weeks old, euthanizing it by pulling its neck, immediately peeling off the skin on its back, carefully removing the subcutaneous fat, washing it with physiological saline, and drying it for later use.

[0057] A vertical Franz diffusion cell was used. The skin was placed flat at the junction of the diffusion cells, with the stratum corneum facing the supply cell and the dermis facing the receiving cell. The temperature was maintained at 37°C, and water was used as the receiving medium. The skin was degassed by ultrasound before use. The sample to be tested was added to the supply cell until the concentration reached 10 mg / mL. The stir bar was rotated at 300 rpm. -1 After 1 hour, a sample was taken from the receiving pool and analyzed by HPLC (220 nm). The ratio of the peak area obtained to the peak area of ​​the 10 mg / mL peptide liquid is the skin penetration rate.

[0058] 3. Experimental Results

[0059] The skin penetration rates of each group of peptides in nude mice are shown in Table 1. It can be seen that, compared with the control group NS peptide, the skin penetration rate of the pentapeptide-derived peptide YS structure provided by the present invention is significantly improved. YS1 and YS2 in the experimental group both have good skin penetration ability, and YS2 has better skin penetration ability.

[0060] Table 1 Skin penetration rate of nude mice

[0061] Group Sample to be tested Polypeptide sequence Skin penetration rate of nude mice (%) Experimental group 1 YS1 YGRTSKKSKKSGGKTTKS 2.13 Experimental group 2 YS2 YGRKKRRQRRMGGKTTKS 6.44 Experimental group 3 YS3 YGHTSKKTHKSGGKTTKS 1.85 Experimental group 4 YS4 YKKTSKKQKKSGGKTTKS 0.53 Experimental group 5 YS5 YGRTSRRQRRMGGKTTKS 3.60 Control group NS NKKTSKKSKKSGGKTTKS 0.09

[0062] Example 3

[0063] This experiment was used to verify the hydrophilicity of the pentapeptide-derived peptide YS.

[0064] 1. Sample to be tested

[0065] Experimental group 1: YS1 polypeptide (SEQ ID NO.1) prepared in Example 1.

[0066] Experimental group 2: YS2 polypeptide (SEQ ID NO.2) prepared in Example 1.

[0067] Experimental group 3: YS3 polypeptide (SEQ ID NO.3) prepared in Example 1.

[0068] Experimental group 4: YS4 polypeptide (SEQ ID NO.4) prepared in Example 1.

[0069] Experimental group 5: YS5 polypeptide (SEQ ID NO.5) prepared in Example 1.

[0070] Control group 2: Commercially available N-terminal palmitoylated pentapeptide PAL-KTTKS (abbreviated as "PAL").

[0071] 2. Experimental Methods

[0072] The peptides from experimental groups 1-5 and control group 2 were directly dissolved in water, and their solubility in water was measured.

[0073] 3. Experimental Results

[0074] The results showed that the YS peptides in experimental groups 1-5 had a water solubility greater than 10 mg / mL, while the PAL peptides were poorly soluble in water and required the addition of the organic solvent DMSO to dissolve.

[0075] Example 4

[0076] This experiment was conducted to verify the ability of pentapeptide-derived peptides to promote type I collagen synthesis in human lung fibroblasts.

[0077] 1. Sample to be tested

[0078] Experimental group 1: YS1 polypeptide (SEQ ID NO.1) prepared in Example 1.

[0079] Experimental group 2: YS2 polypeptide (SEQ ID NO.2) prepared in Example 1.

[0080] Control group: Peptide NS prepared according to the method shown in Example 1, as shown in SEQ ID NO.6: NKKTSKKSKK SGGKT TKS.

[0081] Control group 2: Commercially available N-terminal palmitoylated pentapeptide PAL-KTTKS (abbreviated as "PAL").

[0082] 2. Experimental Methods

[0083] Human lung fibroblasts (HFL-1) were purchased from the Cell Bank of the Chinese Academy of Sciences Type Culture Collection Committee. HFL-1 cells were cultured in DMEM medium containing 10% bovine serum and incubated at 37°C with 7% CO2. 2 93% were cultured in air.

[0084] One dish (6Φ) of HFL-1 cells was digested with trypsin at a weight-to-volume ratio of 0.25% and collected. The cells were then passaged into 2.5 6Φ culture dishes. After culturing, the test sample was added to a final peptide concentration of 2 μg / mL (the peptide was first dissolved in PBS, then added to the cell culture medium at a volume ratio of 10%, ensuring the cells did not exceed 50-60% confluence at the time of drug addition). After culturing for another 24 hours, the mRNA expression level of type I collagen was detected by RT-PCR. The results are as follows: Figure 2As shown; the protein expression level of type I collagen in cells was detected by Western blot, and the results are as follows. Figure 3 As shown.

[0085] One dish (6Φ) of HLF-1 cells treated with the peptide was used. Total RNA was extracted from the cells using the Trizol kit (Invitrogen). 1 μg of RNA was used for reverse transcription, and 2 μL of cDNA was used as a template for PCR amplification. Agarose gel electrophoresis was used to detect the differences in type I collagen mRNA expression levels in cells treated with different concentrations of peptide, using GAPDH as a reference. The results are shown below. Figure 2 .

[0086] One dish (6Φ) of HLF-1 cells treated with peptides was used. Cells were lysed with lysis buffer (prepared as follows: Tris-HCl (pH 7.5), 150 mM NaCl, 1 mM EDTA, 2 mM DTT, 2 mM PMSF, and 1% Triton X-100). After centrifugation at 10,000 rpm, the supernatant was collected, and protein content was determined using the Bradford method. An equal volume of protein was added to each well, separated by 10% polyacrylamide gel electrophoresis, and then transferred to a PVDF membrane (see Sambrook et al., Molecular Cloning: A Laboratory Manual (New York: Cold Spring Harbor Laboratory Press, 1989) for electrotransfer methods). The PVDF membranes after electrotransfer were blocked with PBS containing 1% BSA and 1% sheep serum, and then detected with an anti-type I collagen antibody manufactured by Abcom. Results are shown below. Figure 3 .

[0087] 3. Experimental Results

[0088] like Figure 2 As shown, compared with the control group HLF-1 cells treated with NS, the mRNA and protein expression levels of type I collagen in HLF-1 cells treated with YS1, YS2, and PAL were significantly increased. Figures 1, 2, 3, and 4 represent the NS group, YS2 group, YS1 group, and PAL group, respectively.

[0089] like Figure 3 As shown, the type I collagen content in HLF-1 cells treated with YS1 and YS2 was similar, but higher than that in the PAL-treated group. Furthermore, the pentapeptide-derived peptide YS provided by this invention has superior water solubility, eliminating the need for organic solvents during formulation.

[0090] like Figure 3As shown, compared with the NS control group, the expression level of type I collagen in HLF-1 cells treated with YS1, YS2, and PAL was increased to some extent, and the expression level of type I collagen in HLF-1 cells treated with YS1 and YS2 was higher than that in the PAL treatment group. In the figure, 1, 2, 3, 4, and 5 represent YS2, PAL, YS1, Marker, and NS, respectively.

[0091] Example 5

[0092] This experiment used immunofluorescence assay to verify the effect of the pentapeptide-derived peptide YS on promoting the expression of type I collagen in human lung fibroblasts.

[0093] 1. Sample to be tested

[0094] Experimental group 1: YS1 polypeptide (SEQ ID NO.1) prepared in Example 1.

[0095] Experimental group 2: YS2 polypeptide (SEQ ID NO.2) prepared in Example 1.

[0096] Control group: Peptide NS prepared according to the method shown in Example 1, as shown in SEQ ID NO.6: NKKTSKKSKK SGGKT TKS.

[0097] Control group 2: Commercially available N-terminal palmitoylated pentapeptide PAL-KTTKS (abbreviated as "PAL").

[0098] 2. Experimental Methods

[0099] HLF-1 cells were cultured according to the method in Example 2. After the cells reached confluence, they were seeded onto coverslips at a ratio of 1:2.5. Each group of test samples (2 μg / mL) were added to the cultured cells. After 24 hours, the cells were fixed with 4% paraformaldehyde (paraformaldehyde was dissolved in PBS (pH 7.5) and fixed at room temperature for 15 minutes) and stored in a 4°C refrigerator for later use.

[0100] The experiment began with treatment with 0.2% Triton X100 for 10 minutes, followed by washing three times with PBS for 5 minutes each time. The mixture was then incubated in PBS containing 1% skim milk powder for 30 minutes, and subsequently incubated with anti-type I collagen antibody at 37°C for 2 hours. Finally, it was incubated with FITC-labeled secondary antibody at 37°C for 2 hours. The results were observed under a fluorescence microscope. See attached table. Figure 4 .

[0101] 3. Experimental Results

[0102] like Figure 4As shown, compared with the control group, the expression levels of type I collagen in HLF-1 cells treated with YS1, YS2, and PAL were significantly increased. Figures 1, 2, 3, and 4 represent NS, YS2, PAL, and YS1, respectively.

[0103] Example 6

[0104] This experiment was conducted to verify the anti-skin aging effect of the pentapeptide-derived peptide YS.

[0105] 1. Sample to be tested

[0106] Experimental group 1: YS1 polypeptide (SEQ ID NO.1) prepared in Example 1.

[0107] Experimental group 2: YS2 polypeptide (SEQ ID NO.2) prepared in Example 1.

[0108] Control group: The polypeptide NS shown in SEQ ID NO.3 was prepared according to the method shown in Example 1.

[0109] NS(SEQ ID NO.3):YGRKK RRQRR MGGKT TKS

[0110] Control group 2: Commercially available N-terminal palmitoylated pentapeptide PAL-KTTKS (abbreviated as "PAL").

[0111] Each group of test samples was prepared into a test sample solution with a concentration of 200 ug / mL using water as a solvent, and then set aside for later use.

[0112] 2. Experimental Methods

[0113] Nine 9-month-old nude mice were used. The test sample (200 μg / mL) was evenly applied to the skin on one side of the mouse's back, while the corresponding skin on the other side was treated with normal saline (NS) as a control group. Application was performed once daily for four weeks. After four weeks, skin samples from the treatment sites were collected, paraffin sections were prepared, and then stained with MASSAN to examine changes in skin condition after drug administration. Results are as follows: Figure 5 As shown.

[0114] 3. Experimental Results

[0115] like Figure 5 As shown, after applying samples of YS1, YS2, and PAL, the skin thickness of nude mice was significantly increased compared to the blank control group. The skin wrinkles treated with YS1 and YS2 were significantly fewer than those in the PAL-treated group, indicating that the anti-skin aging effect of the pentapeptide-derived peptide YS provided in this invention is better than that of PAL. In the figure, A, C, and E represent the YS2, YS1, and PAL preparations, respectively, while B, D, and F are the NS control.

[0116] The above description is only a preferred embodiment of the present invention. It should be noted that for those skilled in the art, several improvements and modifications can be made without departing from the principle of the present invention, and these improvements and modifications should also be considered within the scope of protection of the present invention.

[0117] sequence list

[0118]

[0119]

[0120]

[0121]

Claims

1. A pentapeptide-derived peptide YS for anti-skin aging, characterized in that, The pentapeptide-derived peptide YS is selected from one or more of the following: YGRTSKKSKK SGGKT TKS, YGHTS KKTHK SGGKT TKS, YKKTS KKQKK SGGKT TKS, and YGRTS RRQRRMGGKT TKS.

2. The use of the pentapeptide-derived peptide YS as described in claim 1 in the preparation of anti-skin aging agents.

3. The application according to claim 2, characterized in that, The anti-skin aging treatment includes one or more of the following: promoting collagen I synthesis, increasing skin thickness, and reducing skin wrinkles.

4. An anti-skin aging composition, characterized in that, It includes an active ingredient and excipients, wherein the active ingredient includes the pentapeptide-derived peptide YS as described in claim 1.

5. The anti-skin aging composition according to claim 4, characterized in that, The excipients mentioned do not include penetration enhancers.

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