Spirulina phycocyanin polypeptide with moisturizing repair anti-aging effect and application thereof

Abstract

The present application relates to a kind of spirulina phycocyanin polypeptide with moisturizing repair anti-aging efficacy and its application, belong to active polypeptide technical field.The present application is screened from the enzymatic product of spirulina phycocyanin and has the active peptide with moisturizing, repair, anti-aging efficacy of specific sequence, and the active peptide is the polypeptide with amino acid sequence NSPL or GHP.The RXR alpha receptor binding agent of natural, safe and high efficiency is prepared in the present application, the application of small molecule polypeptide in the field of cosmetics is expanded, with good application prospect and excellent economic value.

Description

TECHNICAL FIELD

[0001] The present application relates to a spirulina phycocyanin polypeptide with moisturizing, repairing and anti-aging effects and application thereof, and belongs to the technical field of active polypeptides. BACKGROUND

[0002] Phycobiliprotein is a natural light-harvesting pigment protein existing in microalgae, cyanobacteria and some eukaryotic algae. Phycobiliprotein located on the thylakoid membrane of algae is stacked and assembled into phycobilisome according to certain structure. According to the type of color base contained and the difference of absorption spectrum, phycobiliprotein can be divided into four categories: phycocyanin (PC), phycoerythrin (PE), allophycocyanin (APC) and phycoerythrocyanin (PEC). Phycobiliprotein is water-soluble, non-toxic, presents bright color, can emit bright fluorescence, has multiple biological activities such as antioxidant, anti-radiation, anti-inflammatory, anti-virus, anti-tumor, immune regulation and nerve protection, and is widely used in food, cosmetics, medicine and other fields.

[0003] Phycocyanin active peptide has small molecular weight, easy absorption and clear action mechanism, so it can effectively penetrate into the deep layer of skin and play its biological effect, and can be used as an additive of high-end products in the field of cosmetics to improve the efficacy and competitiveness of products. However, due to the complex screening process and high cost, it is less used in the field of cosmetics. SUMMARY

[0004] The present application provides a spirulina phycocyanin polypeptide with moisturizing, repairing and anti-aging effects. The present application takes spirulina phycocyanin as parent protein, uses alkaline protease and papain complex enzyme to prepare a new type of phycocyanin source beauty peptide, and uses molecular docking technology and other bioinformatics methods to predict the physicochemical properties, toxicity, antioxidant activity and anti-aging activity of the obtained polypeptide, and screen ideal new phycobiliprotein source beauty peptide. The new beauty peptide is synthesized by chemical solid-phase synthesis method, and the moisturizing, repairing and anti-aging effects of the new beauty peptide are evaluated by in vitro experiment. The results show that the polypeptide screened by the present application has moisturizing, repairing and anti-aging effects, and can be used for research and development of cosmetics and the like.

[0005] The technical scheme of the present application is as follows:

[0006] A polypeptide, whose amino acid sequence is NSPL, i.e. Asn-Ser-Pro-Leu.

[0007] A polypeptide, whose amino acid sequence is GHP, i.e. Gly-His-Pro.

[0008] The two polypeptides NSPL and GHP are spirulina phycocyanin-derived bioactive peptides, and the polypeptides are obtained by optimizing enzymolysis conditions, screening enzymolysis products with high activity, separating and purifying the polypeptides by ultrafiltration and high performance liquid chromatography (HPLC), analyzing the structures of the phycocyanin-derived bioactive peptide components by LC-MS / MS, and screening bioactive polypeptides by predicting the physicochemical properties, potential biological activities, toxicity and the like of the polypeptides by bioinformatics methods.

[0009] A composition comprising the polypeptide with the amino acid sequence NSPL and the polypeptide with the amino acid sequence GHP.

[0010] Application of the polypeptide or the composition to preparation of a product with moisturizing efficacy.

[0011] Application of the polypeptide or the composition to preparation of a product with repairing efficacy.

[0012] Application of the polypeptide or the composition to preparation of a product with anti-aging efficacy.

[0013] According to the application, the polypeptide or the composition achieves the anti-aging effect by binding to RXRα receptor and / or promoting Collagen I expression.

[0014] In the application, the product with moisturizing, repairing or anti-aging efficacy includes any one or more of the following: a cosmetic product, a skin care product, a medical aesthetic product, and a pharmaceutical product. The skin care product includes any one or more of the following: a facial cleanser, a lotion, a toner, a moisturizing lotion, an eye serum, a moisturizing cream, an essence, a skin foundation, a sunscreen, and a facial mask. The cosmetic product includes any one or more of the following: a foundation and a sunscreen. The medical aesthetic product includes any one or more of the following: a medical aesthetic mask, a microneedle, and a water-light needle. The pharmaceutical product is in any one or more of the following dosage forms: an injection, a tablet, a capsule, a granule, an ointment, a controlled-release preparation, and an aerosol.

[0015] Application of the polypeptide or the composition to preparation of an RXRα receptor binding product.

[0016] A skin product comprising the polypeptide or the composition.

[0017] In the application, the skin product includes any one or more of the following: a cosmetic product, a skin care product, and a medical aesthetic product. The skin care product includes any one or more of the following: a facial cleanser, a lotion, a toner, a moisturizing lotion, an eye serum, a moisturizing cream, an essence, a skin foundation, a sunscreen, and a facial mask. The cosmetic product includes any one or more of the following: a foundation and a sunscreen. The medical aesthetic product includes any one or more of the following: a medical aesthetic mask, a microneedle, and a water-light needle.

[0018] The preparation method of the polypeptide or the composition is obtained by enzymolysis and separation from the spirulina phycocyanin or is obtained by chemical synthesis according to the amino acid sequence.

[0019] Beneficial effects:

[0020] The application screens the active peptide with the moisturizing, repairing and anti-aging effects from the enzymolysis product of the spirulina phycocyanin, and the active peptide is a polypeptide with the amino acid sequence of NSPL or GHP. The application prepares the natural, safe and efficient RXRα receptor binding agent, expands the application of the small molecule polypeptide in the cosmetic field, and has good application prospect and excellent economic value. BRIEF DESCRIPTION OF DRAWINGS

[0021] Figure 1 It is an HPLC spectrum of the polypeptide sample containing NSPL.

[0022] Figure 2 It is an MS spectrum of the polypeptide NSPL.

[0023] Figure 3 It is an HPLC spectrum of the polypeptide sample containing GHP.

[0024] Figure 4 It is an MS spectrum of the polypeptide GHP.

[0025] Figure 5 It is a simulated docking interaction diagram of the polypeptide NSPL and the RXRα receptor.

[0026] Figure 6 It is a simulated docking interaction diagram of the polypeptide GHP and the RXRα receptor. DETAILED DESCRIPTION

[0027] The technical scheme of the application will be further illustrated by combining specific embodiments. However, it should be understood that the embodiments described in the application are only exemplary and do not constitute any limitation on the scope of the application. The reagents and materials involved in the embodiments are all ordinary commercially available products if not otherwise specified. The biological materials involved in the embodiments can be obtained from the ordinary commercially available channels if not otherwise specified.

[0028] Example 1: Preparation of spirulina phycocyanin peptide

[0029] The preparation method of the spirulina phycocyanin peptide comprises the following steps:

[0030] 1) The spirulina phycocyanin powder is from Shanghai Kefan Chemical Co., Ltd., the spirulina phycocyanin powder is dissolved, and the pH of the spirulina phycocyanin solution is adjusted to 9, and then 2×10 5U / g of compound protease (alkaline protease, papain enzyme activity ratio 1:1) was added, mixed and placed in a shaker for enzymatic hydrolysis. The shaker speed was 150 rpm, the enzymatic hydrolysis time was 5 h, and the enzymatic hydrolysis temperature was 40 °C. After enzymatic hydrolysis, boiling water bath was used for 10 min to inactivate the enzyme and terminate the enzymatic hydrolysis.

[0031] 2) The enzymatic hydrolysate was centrifuged at 12000 rpm for 20 min at 4 °C, and the supernatant was collected and the precipitate was discarded. The supernatant was the spirulina phycocyanin peptide solution. Then, 3 kDa ultrafiltration membrane was selected for ultrafiltration to obtain a peptide solution with a peptide molecular weight of <3 kDa, which was freeze-dried to obtain spirulina phycocyanin peptide freeze-dried powder.

[0032] Example 2: Structure identification of spirulina phycocyanin peptide

[0033] The spirulina phycocyanin peptide freeze-dried powder obtained in Example 1 was re-dissolved with ultrapure water, filtered through a 0.22 μm water filter membrane, and the sample was collected according to the peak time by liquid chromatography for preliminary separation of the polypeptide sample. Then, the sequence structure of the spirulina phycocyanin peptide was analyzed and identified by ultra-high performance liquid chromatography tandem mass spectrometry. In the ultra-high performance liquid chromatography, the mobile phase A was 0.1% formic acid aqueous solution, the mobile phase B was 0.1% formic acid acetonitrile solution, the elution time was 60 min, the gradient elution conditions were shown in Table 1, the injection amount was 5 μL, and the flow rate was set to 300 μL / min. The tandem mass spectrometry was in positive ion mode, the secondary mass spectrometry analysis was performed with a resolution of 120000 for full MS scanning of 100-2000 m / z, and the specific mass spectrometry parameter settings were shown in Table 2.

[0034] Table 1. Ultra-high performance liquid chromatography elution conditions

[0035]

[0036] Table 2. Tandem mass spectrometry analysis conditions

[0037]

[0038] Mass spectrometry data analysis:

[0039] The mass spectrometry raw file was converted into MGF format file by MM File Conversion software, and then the protein data in uniport database was searched by MASCOT mass spectrometry data analysis platform, and the specific search parameters were shown in Table 3.

[0040] Table 3. Mascot search parameters

[0041]

[0042] Note: Search against database http: / / www.uniprot.org / taxonomy / 8139,

[0043] Search software http: / / www.matrixscience.com / .

[0044] Example 3: Bioinformatics prediction of Spirulina phycocyanin peptides

[0045] 1) Prediction of potential biological activity and toxicity of Spirulina phycocyanin peptides

[0046] The potential biological activity of the obtained polypeptide sequences was analyzed using the PeptideRanker online platform (http: / / distilldeep.ucd). The polypeptides were ranked according to the probability of biological activity prediction, and the default threshold of the PeptideRanker prediction model was 0.5. Any polypeptide with a threshold value exceeding 0.5 was marked as having biological activity. In this study, a threshold value > 0.8 was selected as the screening condition for polypeptides with biological activity.

[0047] Toxicity and allergenicity are also concerns in the development of polypeptides for use in the field of skincare. The ToxinPrep (https: / / webs.iiitd.edu.in / raghava / toxinpred / multi_submit.php) platform was used to predict the potential toxicity of the polypeptide sequences based on the SVM (Swiss-Port) algorithm.

[0048] 2) Prediction of antioxidant activity of Spirulina phycocyanin peptides

[0049] The polypeptide sequences selected for their lack of toxicity and potential biological activity (PeptideRanker > 0.8) were subjected to antioxidant activity prediction using the AnOxPePred (https: / / services.healthtech.dtu.dk / service.phpAnOxPePred-1.0) platform. The analysis model selected Peptide Mode, and the Minimum peptide length and Maximum peptide length were set to the length of the predicted polypeptide. In this study, a prediction result FRS score > 0.5 or CHEL score > 0.25 was selected as an indicator of the antioxidant activity of the polypeptide.

[0050] 3) Molecular docking test of Spirulina phycocyanin peptides with cell RXRa receptor

[0051] The polypeptide sequences screened for no toxicity and potential biological activity and antioxidant activity were used for docking with the cell RXRa receptor molecules. The polypeptide sequences were subjected to simulated molecular docking test and docking score calculation using pepsite 2.0 (http: / / pepsite2.russell lab.org / ), AutoDock 1.5.6 and RXRa receptor sequence from PDB database with accession number PDB ID: P19793, and the RXRa receptor target structure was docked with the polypeptide sequences using vina inside pyrx software (https: / / pyrx.sourceforge.io / ), and the Affinity value (kcal / mol) represented the binding ability of the two, and the lower the Affinity value, the more stable the binding of the ligand and the receptor.

[0052] Bioinformatics prediction results:

[0053] Through the above bioinformatics prediction experiment, two spirulina phycocyanin polypeptides were screened, which were NSPL (Asn-Ser-Pro-Leu) and GHP (Gly-His-Pro). Among them, the HPLC spectrum of the polypeptide sample containing NSPL is shown in Figure 1 , the MS spectrum of the polypeptide NSPL is shown in Figure 2 , the HPLC spectrum of the polypeptide sample containing GHP is shown in Figure 3 , and the MS spectrum of the polypeptide GHP is shown in Figure 4 .

[0054] The simulated docking interaction of polypeptide NSPL and RXRa receptor is shown in Figure 5 , and the simulated docking interaction of polypeptide GHP and RXRa receptor is shown in Figure 6As shown, the binding ability of polypeptides NSPL and GHP to RXRα receptor is shown in Table 4. From the above results, it can be seen that polypeptide NSPL forms hydrogen bond with ASP448, THE266, ASN262, THR445, PRO446 of RXRα receptor protein, and the binding is relatively tight; polypeptide GHP forms hydrogen bond with PRO446, THR445, THR266, VAL265, GLN443 of RXRα receptor protein, and the binding is relatively tight. Retinoic acid receptor (RARα) belongs to one of the nuclear receptor subfamily (RARα, RARβ and RARγ), after polypeptide binds to the related receptor (RXR, RAR), various dimers are formed, and under the help of activator (such as histone acetyltransferase), it binds to the corresponding retinoic acid response element, regulates and controls the activation and expression of messenger RNA in the nucleus, to regulate cell division and differentiation, stimulate keratinocyte proliferation, promote epidermal keratinocyte metabolism, reduce dermal collagen degradation, stimulate fibroblasts to produce more collagen and hyaluronic acid and other substances, so as to achieve the effect of anti-aging.

[0055] Table 4. Binding ability of polypeptide to RXRα receptor

[0056]

[0057] It is generally believed that an Affinity value less than -4.25 kcal / mol indicates certain binding activity between the two, less than -5.0 kcal / mol indicates better binding activity, and less than -7.0 kcal / mol indicates strong binding activity.

[0058] 4) Chemical synthesis of spirulina phycocyanin peptide

[0059] The above two polypeptide sequences are chemically synthesized by Fmoc amino acid solid-phase synthesis technology. The chemical synthesis is completed by Nanjing Peptide Valley Biotechnology Co., Ltd. The purity is ≥95%, and the purity and molecular weight of the synthesized phycocyanin-derived active polypeptide identified by RP-HPLC and MS meet the requirements.

[0060] Example 4: In vitro experiment of promoting type I collagen synthesis

[0061] The experiment uses human skin fibroblasts (HSF cells) (batch number: Fb220309, provided by Guangdong Boxi Biological Technology Co., Ltd.) as a model cell line for research, and the experimental steps are as follows:

[0062] 1) Cell inoculation: after recovering the cells, when the plating rate reaches about 60%, the cell suspension is obtained after digestion and resuspension, and the cell suspension is inoculated into a 6-well plate at an inoculation amount of 2 mL / well, and incubated in a CO2 incubator (37°C, 5% CO2) overnight;

[0063] 2) Liquid preparation: prepare the working solution of the test substance according to the test grouping (Table 5);

[0064] Table 5. Test grouping scheme

[0065]

[0066] 3) Dosing: according to the test grouping, when the plating rate of the cells in the 6-well plate reaches 40%-60%, dosing is performed in groups, with 3 replicates in each group; after discarding the old culture solution, 2 mL of culture solution is added to each well of the blank control group, 2 mL of culture solution containing the corresponding concentration of TGF-β1 is added to each well of the positive control group, and 2 mL of culture solution containing the corresponding concentration of the test sample is added to each well of the sample group; after dosing is completed, the 6-well plate is placed in a CO2 incubator (37°C, 5% CO2) for 24 h;

[0067] 4) Cell collection: after the culture is completed, the old solution is aspirated and discarded, and the cells are washed twice with PBS buffer; 1 mL of RNAisoPlus is added to each well, the cells are lysed by blowing, and the sample is collected;

[0068] 5) ELISA detection: collect the supernatant and detect the concentration of collagen I in the supernatant according to the operating instructions of the ELISA kit;

[0069] 6) Enhancement rate calculation: the enhancement rate of collagen I is calculated according to the following formula:

[0070]

[0071] 7) Statistical analysis of results: GraphPad Prism is used for plotting, and the results are expressed as Mean ± SD; the comparison between groups is performed using t -test statistical analysis; statistical analysis is two-tailed; P <0.05 is considered to be significantly different, P <0.01 is considered to be extremely significantly different; the results are shown in Table 6.

[0072] Table 6. Collagen I content detection results

[0073]

[0074] Note: when statistical analysis is performed using the t -test method, the significance compared with the BC group is represented by *, the P -value <0.05 is represented by *, the P -value <0.01 is represented by **.

[0075] As can be seen from Table 6, the Collagen I content of the PC group increased significantly compared with the BC group, indicating that the positive control of this test was effective; compared with the BC group, the Collagen I content of the polypeptides NSPL and GHP at a concentration of 2.5 mg / mL increased significantly, with an increase rate of 134.00% and 92.74%, respectively. Therefore, the above two polypeptides can significantly increase the Collagen I content and achieve the effect of tightening and anti-aging.

[0076] Example 5: In vitro experiment of promoting AQP3 synthesis

[0077] In the experiment, keratinocytes (batch number: Ep23082202, provided by Guangdong Boxi Biological Technology Co., Ltd.) were used as a model cell line for research, and the experimental steps were as follows:

[0078] 1) Cell inoculation: after recovering the cells, when the plating rate reached about 60%, the cells were digested and resuspended to obtain a cell suspension, which was inoculated into a 24-well plate at a volume of 1 mL / well. The cells were incubated in a CO2 incubator (37°C, 5% CO2) overnight.

[0079] 2) Liquid preparation: prepare the test sample working solution according to the test grouping (Table 7);

[0080] Table 7. Test grouping scheme

[0081]

[0082] 3) Dosing: according to the test grouping, when the plating rate of the cells in the 24-well plate reached 40%-60%, the cells were grouped and dosed, with 3 replicates in each group. After discarding the old culture medium, 1 mL of culture medium was added to each well of the blank control group, 1 mL of culture medium containing the corresponding concentration of CaCl2 was added to each well of the positive control group, and 1 mL of culture medium containing the corresponding concentration of the test sample was added to each well of the sample group. After dosing, the 24-well plate was placed in a CO2 incubator (37°C, 5% CO2) for 24 h;

[0083] 4) Immunofluorescence detection: after the culture was completed, the cells were fixed with 4% paraformaldehyde for 30 min, and then subjected to immunofluorescence detection. The cells were observed under a microscope, and the images were collected. The Ipwin32 image analysis software was used to analyze the target signal in the images, and the average value was calculated. Taking the blank control group as the reference, the relative IOD / cell number average value was calculated to represent the relative expression of AQP3 protein;

[0084] 5) Increase rate calculation: the AQP3 increase rate was calculated according to the following formula:

[0085]

[0086] 6) Result statistical analysis: GraphPad Prism was used for plotting, and the results were expressed as Mean ± SD; the comparison between groups was performed using t t-test statistical analysis; statistical analysis was two-tailed; P <0.05 was considered to be significantly different, P <0.01 was considered to be extremely significantly different; the results are shown in Table 8.

[0087] Table 8. AQP3 immunofluorescence analysis results

[0088]

[0089] Note: Integrated optical density (IOD), the value of which reflects the content of AQP3. The working solution of the test substance was prepared according to the test grouping (Table 9). t * when the t-test method was used for statistical analysis, compared with the BC group, P * when the t-test method was used for statistical analysis, compared with the BC group, P ** when the t-test method was used for statistical analysis, compared with the BC group.

[0090] Aquaporins (AQP) are a class of transport proteins related to water molecule permeability on the cell membrane. AQP generally selectively transports water molecules, but a few AQPs can also transport small molecules such as glycerol and urea. AQP3 is a transport protein that transports small molecules such as water, glycerol and urea across the cell membrane, and is the most expressed subtype of aquaporin in human skin. As can be seen from the AQP3 immunofluorescence analysis results in Table 8: compared with the BC group, the AQP3 content of the PC group increased significantly, indicating that the positive control was effective in this test; compared with the BC group, the AQP3 content of the polypeptides NSPL and GHP at a concentration of 2.5 mg / mL increased significantly, with an increase rate of 81.00% and 66.00%, respectively. Therefore, the above two polypeptides can significantly increase the content of AQP3 and achieve the moisturizing effect.

[0091] Example 6: In vitro experiment for promoting the synthesis of FLG and LOR

[0092] The experiment was conducted using keratinocytes as a model cell line, and the experimental steps were as follows:

[0093] 1) Cell inoculation: after recovering the cells, when the plating rate reached about 60%, the cells were digested and resuspended to obtain a cell suspension, which was inoculated into a 6-well plate at a volume of 2 mL / well. The cells were incubated in a CO2 incubator (37°C, 5% CO2) overnight;

[0094] 2) Liquid preparation: prepare the working solution of the test substance according to the test grouping (Table 9);

[0095] Table 9. Test grouping scheme

[0096]

[0097] 3) Drug administration: according to the test grouping, when the cell plating rate in the 6-well plate reaches 40%~60%, group administration is performed, and 3 replicate wells are set for each group; after the old culture solution is discarded, 2 mL of culture solution is added to each well of the blank control group, 2 mL of culture solution containing the corresponding concentration of WY14643 is added to each well of the PC group, and 2 mL of culture solution containing the corresponding concentration of the sample to be tested is added to each well of the sample group; after the drug administration is completed, the 6-well plate is placed in a CO2 incubator (37°C, 5% CO2) for 24 h of culture;

[0098] 4) Cell collection: after the culture is completed, the old solution is aspirated and discarded, and the PBS buffer is washed twice, 1 mL of RNAisoPlus is added to each well, the cells are lysed by blowing, and the sample is collected;

[0099] 5) Gene expression detection: after the RNA is extracted and reverse transcribed to cDNA, fluorescence quantitative PCR detection is performed, and 2 -△△CT method is used to calculate the mRNA expression of FLG and LOR;

[0100] 6) Up-regulation rate calculation: the mRNA expression up-regulation rate of FLG and LOR is calculated according to the following formula:

[0101]

[0102] 7) Result statistical analysis: GraphPad Prism is used for plotting, and the results are expressed as Mean±SD; the comparison between groups is analyzed by t -test statistical analysis; statistical analysis is two-tailed; P <0.05 is considered to be significantly different, P <0.01 is considered to be extremely significantly different; the results are shown in Tables 10 and 11.

[0103] Table 10. mRNA content detection results of FLG

[0104]

[0105] Note: 2- △△CT method is used for result calculation, and t -test method is used for statistical analysis, the mRNA content of the BC group is normalized, compared with the BC group, and the significance is represented by *, the P -value <0.05 is represented by *, and P -value <0.01 is represented by **.

[0106] Table 11. mRNA content detection results of LOR

[0107]

[0108] Note: 2- △△CT Method for calculating results, using t -test method for statistical analysis, mRNA content of BC group was normalized, compared with BC group, significance was represented as *, P -value <0.05 was represented as *, P -value <0.01 was represented as **.

[0109] Filaggrin (FLG) and Loricrin (LOR) are proteins closely related to skin barrier function. As can be seen from the gene detection results in Table 10 and Table 11, the mRNA content of FLG and LOR in PC group was significantly increased compared with BC group, indicating that the positive control test was effective; compared with BC group, the mRNA content of FLG of polypeptides NSPL and GHP at a concentration of 2.5 mg / mL was significantly increased, with an increase rate of 91.00% and 79.00% respectively, and the mRNA content of LOR was significantly increased, with an increase rate of 85.00% and 74.00% respectively. Therefore, it is indicated that the above two polypeptides at the concentration can increase the content of FLG and LOR, and have skin barrier repair efficacy.

Claims

1. A skin care polypeptide composition characterized in that, The polypeptide having an amino acid sequence of NSPL and the polypeptide having an amino acid sequence of GHP.

2. Use of the polypeptide composition of claim 1 or the polypeptide of any one of them in the preparation of a product having a moisturizing effect.

3. Use of the polypeptide composition of claim 1 or the polypeptide of any one of them in the preparation of a product having a skin barrier repair effect.

4. Use of the polypeptide composition of claim 1 or the polypeptide of any one of them in the preparation of a product having an anti-aging effect.

5. The use according to claim 4, wherein the compound is ###0002### The polypeptide composition or the polypeptide of any one of them achieves the anti-aging effect by promoting Collagen I expression.

6. Use according to any one of claims 2 to 4, wherein the compound is ###0002### The product includes any one or more of the following: a cosmetic product, a skin care product, a medical aesthetic product, and a pharmaceutical product.

7. Use according to claim 6, wherein The skin care product includes any one or more of the following: a facial cleanser, a lotion, a toner, a moisturizing cream, an essence, a serum, a sunscreen, and a mask.

8. Use according to claim 7, wherein the compound is ###0002### The lotion includes a moisturizing lotion, and the essence includes an eye essence.

9. The use according to claim 6, wherein The cosmetic product includes any one or more of the following: a foundation and a primer.

10. The use according to claim 6, wherein The medical aesthetic product includes any one or more of the following: a medical aesthetic mask, a microneedle, and a water-light needle.

11. Use according to claim 6, wherein The pharmaceutical product is in a dosage form selected from any one or more of the following: an injection, a tablet, a capsule, a granule, an ointment, a controlled-release preparation, and an aerosol.

12. A skin product comprising the polypeptide composition of claim 1.

13. The skin product of claim 12, wherein The skin product includes any one or more of the following: a cosmetic product, a skin care product, and a medical aesthetic product.

14. The skin product of claim 13, wherein The skin care product includes any one or more of the following: a facial cleanser, a lotion, a toner, a moisturizing cream, an essence, a serum, a sunscreen, and a mask.

15. The skin product of claim 14, wherein The lotion includes a moisturizing lotion, and the essence includes an eye essence.

16. The skin product of claim 13, wherein The cosmetic product includes any one or more of the following: a foundation and a primer.

17. The skin product of claim 13, wherein The medical aesthetic product includes any one or more of the following: a medical aesthetic mask, a microneedle, and a water-light needle.

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