Anti-aging polypeptide as well as synthesis method and application thereof

Abstract

The invention belongs to the technical field of cosmetics, and discloses a group of structures, a synthesis method and application of anti-aging active peptides. The sequences of the anti-aging active peptides provided by the invention are as follows: Pal-Lys-Met-Lys-OH, Ac-Ser-Pro-Ala-Gly-Gly-Pro-OH and Oct-Gly-Pro-OH, and the three polypeptides have excellent anti-aging performance under the concentration of 0.05%. The anti-aging polypeptide prepared by the invention has an excellent anti-aging effect when being applied to anti-aging essence or anti-aging face cream.

Description

Technical Field

[0001] The invention relates to a group of peptides and synthesis and application thereof, belonging to the technical field of cosmetics, and in particular to an anti-aging polypeptide with excellent performance and a synthesis method and application thereof. Background Art

[0002] The skin is the largest and outermost important organ of the human body, and its structure consists of the epidermis, dermis and subcutaneous tissue. Among them, the epidermis and dermis are the most important components of the skin and play an important role. Affected by internal and external factors, the number of dermal fibroblasts and extracellular matrix components in the skin decreases, reducing the ability to synthesize collagen and elastin in the ECM, ultimately leading to cell aging. Among them, external factors are an important factor in accelerating the natural aging of the skin. Long-term contact of UVB and atmospheric pollutants in the external environment with the skin will lead to excessive production of ROS reactive oxygen species. These substances will destroy the skin's antioxidant defense system, thereby causing oxidative stress. Oxidative stress leads to uncontrolled melanin synthesis in skin melanocytes, reduced hyaluronic acid formed by keratinocytes, and reduced ECM secreted by dermal fibroblasts, such as type I and III collagen and elastin, which in turn leads to macroscopic skin aging.

[0003] Although existing technologies have developed polypeptides with certain anti-aging functions, their amino acid sequences are long, their yields are low, and they are difficult to remove impurities, so their costs are high. In addition, the products have poor hydrolysis resistance due to their simple amino acid sequences, which is not conducive to their application in cosmetic products. Therefore, it is necessary to develop polypeptide raw materials with advantages in cost, efficacy, and stable application in cosmetic formulas to provide new solutions to skin aging problems. Summary of the invention

[0004] In order to overcome the deficiencies of the prior art, the present invention aims to provide an anti-aging polypeptide and a synthesis method and application thereof.

[0005] In order to achieve the above object, the technical solution of the present invention is:

[0006] In the first aspect, the present invention provides three anti-aging active polypeptides with excellent performance, wherein the anti-aging polypeptides are:

[0007] Anti-aging peptide-1: Pal-Lys-Met-Lys-OH

[0008] The structural formula of anti-aging polypeptide-1 is as shown in Formula Ⅰ:

[0009] Formula I

[0010] Anti-aging peptide-2: Ac-Ser-Pro-Ala-Gly-Gly-Pro-OH

[0011] The structural formula of anti-aging polypeptide-2 is as shown in Formula II:

[0012] Formula II

[0013] Anti-aging peptide-3: Oct-Gly-Pro-OH;

[0014] The structural formula of anti-aging polypeptide-3 is as follows:

[0015] Formula III

[0016] In a second aspect, the present invention provides a method for preparing an anti-aging polypeptide, the preparation steps of which include:

[0017] Step 1: Compound synthesis:

[0018] 2-Chlorotriphenylmethyl chloride (2-CTC resin, 1.58mmol / g loading, 4g) was weighed in a reaction tube and dichloromethane (DCM) was added to swell at room temperature for 1 hour. After the solvent was drained, the first amino acid monomer (1.5equiv) at the C-terminus and N,N-diisopropylethylamine (DIEA, 5equiv) in dichloromethane solution were added. After shaking at room temperature for 1 hour, the resin was washed with N,N-dimethylformamide (DMF) and DCM three times in sequence and drained. Subsequently, Fmoc protection was removed by adding 20% ​​piperidine / DMF solution for deprotection twice, each time for 10 minutes, and then the resin was washed with DCM and DMF three times in sequence. After drying, the second amino acid was coupled, and the activated second amino acid monomer DMF solution (including 5equiv of amino acid monomer, 4.75equiv of condensing agent HBTU and 5equiv of DIEA) was added. After shaking at room temperature for 1 hour, the resin was washed with DMF and DCM three times in sequence and drained. Repeat the above steps of Fmoc deprotection, washing, coupling, and washing until the last amino acid monomer. After all couplings are completed, perform Fmoc deprotection, wash, and drain. Then perform N-terminal modification, add palmitoyl chloride, acetyl chloride or octanoyl chloride (2 equiv), DIEA (2.5 equiv) in DCM solution to the resin, shake at room temperature for 2 h, wash the resin 3 times with DMF and DCM in turn, and drain.

[0019] Step 2: Compound cleavage:

[0020] Add the cleavage reagent to the resin connected with the anti-aging active peptide: trifluoroacetic acid (TFA) / triisopropylsilane (TIPS) / water = 95 / 2.5 / 2.5, and shake at room temperature for 2 hours. Collect the filtrate in a centrifuge tube, wash twice with DCM and acetonitrile, and combine the filtrate. After most of the solvent is blown dry by an air pump, add anhydrous ether to precipitate, mix thoroughly and centrifuge, pour the supernatant, wash 3 times in this way, and obtain a crude product.

[0021] Step 3: Compound purification:

[0022] The polypeptide is dissolved in a solvent such as acetonitrile, ethyl acetate, ethanol, etc., and the crude product is further purified by washing, beating or recrystallization.

[0023] In a third aspect, the present invention provides a method for using anti-aging polypeptides in cosmetics:

[0024] The application forms of the anti-aging polypeptide provided by the present invention in cosmetics include but are not limited to: anti-aging essence, anti-aging cream, anti-aging mask and other products. The application method of the anti-aging polypeptide in cosmetics is to disperse the anti-aging polypeptide in solvents such as glycerin, propylene glycol, butylene glycol and then add it to the cosmetic product.

[0025] In a fourth aspect, the present invention provides the use of anti-aging polypeptides in cosmetic anti-aging essences:

[0026] The anti-aging polypeptide anti-aging essence provided by the present invention comprises the following percentage components:

[0027] Phase A: water balance, EDTA-2Na 0.1%, carbomer 0.12%, xanthan gum 0.02%, hydroxyethyl cellulose 0.01%;

[0028] Phase B: phenoxyethanol 0.4%, hexylene glycol 0.8%, ethylhexylglycerin 0.1%;

[0029] Phase C: propylene glycol 2%, anti-aging polypeptide-1 and / or anti-aging polypeptide-2 and / or anti-aging polypeptide-3 0.001%-0.1%.

[0030] The steps of preparing the anti-aging essence are as follows:

[0031] Add phase A into the reaction vessel in sequence, stir and disperse, raise the temperature to 75°C and keep stirring for 15 to 30 minutes;

[0032] After phase A is completely dispersed, add phase B and stir to cool down to below 40°C;

[0033] Add the evenly mixed phase C and stir to disperse evenly to obtain the final anti-aging essence.

[0034] The technical effects and beneficial effects of the present invention are as follows:

[0035] 1) The present invention designs and develops a group of anti-aging peptides with excellent performance, including: anti-aging peptide-1 (Pal-Lys-Met-Lys-OH), anti-aging peptide-2 (Ac-Ser-Pro-Ala-Gly-Gly-Pro-OH) and anti-aging peptide-3 (Oct-Gly-Pro-OH);

[0036] 2) The present invention provides a method for preparing an anti-aging polypeptide, which can efficiently and massively prepare high-purity active polypeptides;

[0037] 3) The anti-aging polypeptide designed and developed by the present invention has an excellent effect of promoting collagen production and can reduce skin texture and facial wrinkles;

[0038] 4) The present invention provides an application form of anti-aging polypeptide in cosmetics, such as anti-aging essence. BRIEF DESCRIPTION OF THE DRAWINGS

[0039] Figure 1 This is the LCMS spectrum of anti-aging peptide-1;

[0040] Figure 2 This is the LCMS spectrum of anti-aging peptide-2;

[0041] Figure 3 This is the LCMS spectrum of anti-aging peptide-3;

[0042] Figure 4 The results of anti-aging activity test on HSF cells for three anti-aging peptides. DETAILED DESCRIPTION

[0043] In order to make the above-mentioned objects, features and advantages of the present invention more obvious and easy to understand, the specific embodiments of the present invention are described in detail below.

[0044] As used herein, the term "prepared from" is synonymous with "comprising." As used herein, the terms "comprising," "including," "having," "containing," or any other variation thereof, are intended to cover a non-exclusive inclusion. For example, a composition, process, method, article, or apparatus that comprises the listed elements is not necessarily limited to only those elements but may include other elements not expressly listed or inherent to such composition, process, method, article, or apparatus.

[0045] When amount, concentration or other value or parameter is expressed as range, preferred range or a series of upper preferred value and lower preferred value limit range, this should be understood as specifically disclosing all ranges formed by any pairing of any range upper limit or preferred value and any range lower limit or preferred value, regardless of whether the range is disclosed separately. For example, when disclosing range "1 to 5", described range should be interpreted as including range "1 to 4", "1 to 3", "1 to 2", "1 to 2 and 4 to 5", "1 to 3 and 5" etc. When numerical range is described in this article, unless otherwise stated, the range is intended to include its end value and all integers and fractions within the range.

[0046] Many specific details are set forth in the following description to facilitate a full understanding of the present invention. However, the present invention can be implemented in many other ways than those described herein, and those skilled in the art can make similar improvements without violating the connotation of the present invention, so the present invention is not limited to the specific embodiments disclosed below.

[0047] Examples 1 to 3

[0048] The present invention provides three anti-aging polypeptides, and the sequences and structures of the three anti-aging polypeptides are:

[0049] Anti-aging peptide-1:

[0050] The sequence of anti-aging peptide-1 is: Pal-Lys-Met-Lys-OH;

[0051] The structural formula of anti-aging polypeptide-1 is as shown in Formula Ⅰ:

[0052] Formula I The LCMS spectrum of anti-aging peptide-1 is as follows Figure 1 shown.

[0053] Anti-aging peptide-2:

[0054] The sequence of anti-aging peptide-2 is: Ac-Ser-Pro-Ala-Gly-Gly-Pro-OH;

[0055] The structural formula of anti-aging polypeptide-2 is as shown in Formula II:

[0056] Formula II The LCMS spectrum of anti-aging peptide-2 is as follows Figure 2 shown.

[0057] Anti-aging peptide-3:

[0058] The sequence of anti-aging peptide-3 is: Oct-Gly-Pro-OH;

[0059] The structural formula of anti-aging polypeptide-3 is as follows:

[0060] Formula III The LCMS spectrum of anti-aging peptide-3 is as follows Figure 3 shown.

[0061] The anti-aging polypeptide is prepared by the following steps:

[0062] Step 1: Compound synthesis:

[0063] 2-Chlorotriphenylmethyl chloride (2-CTC resin, 1.58mmol / g loading, 4g) was weighed in a reaction tube and dichloromethane (DCM) was added to swell at room temperature for 1 hour. After the solvent was drained, the first amino acid monomer (1.5equiv) at the C-terminus and N,N-diisopropylethylamine (DIEA, 5equiv) in dichloromethane solution were added. After shaking at room temperature for 1 hour, the resin was washed 3 times with N,N-dimethylformamide (DMF) and DCM in turn, and then drained. Subsequently, Fmoc protection was removed, and 20% piperidine / DMF solution was added for deprotection twice, each time for 10 minutes, and then the resin was washed 3 times with DCM and DMF in turn. After drying, the second amino acid was coupled, and the activated second amino acid monomer DMF solution (including 5equiv of amino acid monomer, 4.75equiv of condensing agent HBTU and 5equiv of DIEA) was added. After shaking at room temperature for 1 hour, the resin was washed 3 times with DMF and DCM in turn, and then drained. Repeat the above steps of Fmoc deprotection, washing, coupling, and washing until the last amino acid monomer. After all couplings are completed, perform Fmoc deprotection, wash, and drain. Then perform N-terminal modification, add palmitoyl chloride, acetyl chloride or octanoyl chloride (2 equiv), DIEA (2.5 equiv) in DCM solution to the resin, shake at room temperature for 2 h, wash the resin 3 times with DMF and DCM in turn, and drain.

[0064] Step 2: Compound cleavage:

[0065] Add the cleavage reagent to the resin connected with the anti-aging active peptide: trifluoroacetic acid (TFA) / triisopropylsilane (TIPS) / water = 95 / 2.5 / 2.5, and shake at room temperature for 2 hours. Collect the filtrate in a centrifuge tube, wash twice with DCM and acetonitrile, and combine the filtrate. After most of the solvent is blown dry by an air pump, add anhydrous ether to precipitate, mix thoroughly and centrifuge, pour the supernatant, wash 3 times in this way, and obtain a crude product.

[0066] Step 3: Compound purification:

[0067] The polypeptide is dissolved in a solvent such as acetonitrile, ethyl acetate, ethanol, etc., and the crude product is further purified by washing, beating or recrystallization.

[0068] The present invention provides a method for using anti-aging polypeptides in cosmetics:

[0069] The application forms of the anti-aging peptides provided by the present invention in cosmetics include but are not limited to: anti-aging essences, anti-aging creams, anti-aging masks and other products. The application method of the anti-aging peptides in cosmetics is to disperse the anti-aging peptides in solvents such as glycerin, propylene glycol, butylene glycol, etc. and then add them to the cosmetic products.

[0070] Application Examples 1 to 3 and Comparative Examples 1 to 3

[0071] The preparation method of the product containing the anti-aging polypeptide of the present invention is as follows:

[0072] Preparation of anti-aging essence containing anti-aging peptides:

[0073] The application examples 1 to 3 of the anti-aging essence and the comparative examples 1 to 3 were prepared according to the addition ratios in Table 1, and the preparation steps were as follows:

[0074] 1) Add phase A into the reaction vessel in sequence, stir and disperse, raise the temperature to 75°C and keep stirring for 15 to 30 minutes;

[0075] 2) After phase A is completely dispersed, add phase B and stir to cool down to below 40°C;

[0076] 3) Add the mixed phase C and stir to disperse evenly to obtain the final anti-aging essence.

[0077] Table 1 Anti-aging essence application examples 1 to 3 and comparative examples 1 to 3

[0078]

[0079] Effect Test Example 1

[0080] Zebrafish experiments

[0081] Test method for promoting the rate of type I collagen and elastin:

[0082] Thirty-six six-day-old zebrafish were divided into three groups and exposed to a 0.001% test concentration of the peptide sample solution. A blank control group was also set up. After 24 hours of exposure, RNA was extracted from the zebrafish, cDNA was synthesized, and real-time PCR amplification was performed. β-actin was used as the housekeeping gene and Ct was used as the amplification result. The relative expression levels of col1a1a, col1a1b and col1a2 were calculated and statistically analyzed. The results are shown in Table 2.

[0083] Thirty-six six-day-old zebrafish were divided into three groups and exposed to a 0.001% test concentration of the peptide sample solution. A blank control group was set up at the same time. After 24 hours of exposure, RNA was extracted from the zebrafish, cDNA was synthesized, and real-time PCR amplification was performed. β-actin was used as the housekeeping gene and Ct was used as the amplification result. The relative expression level of Elna was calculated and statistical analysis was performed. The results are shown in Table 3.

[0084] The results showed that the three anti-aging peptides can significantly promote the expression of zebrafish type I collagen gene, have the effect of promoting the regeneration of type I collagen, and have anti-wrinkle and firming effects.

[0085] The test structure and results of the type I collagen promotion rate are shown in Table 2.

[0086] Table 2 Promotion rate of zebrafish type I collagen

[0087] sample concentration(%) Col1a1a promotion rate (%) Col1a1b promotion rate (%) Col1a2 promotion rate (%) Anti-aging peptide-1 0.001 38 81 189 Anti-aging peptide-2 0.001 81 174 183 Anti-aging peptide-3 0.001 50 98 127 Hexapeptide-11 0.001 16 3 3 Tripeptide-1 Copper 0.001 57 42 55 blank - 0 0 0

[0088] Table 3 Zebrafish elastin promotion rate

[0089] sample concentration(%) Elna promotion rate (%) Anti-aging peptide-1 0.001 47 Anti-aging peptide-2 0.001 78 Anti-aging peptide-3 0.001 15 Hexapeptide-11 0.001 3 Tripeptide-1 Copper 0.001 42 blank - 0

[0090] It can be seen from Table 2 and Table 3 that under the condition of adding concentration of 0.001%, the anti-aging polypeptide of the present invention can significantly promote type I collagen and elastin, which shows that the anti-aging polypeptide of the present invention has excellent anti-wrinkle and anti-aging effects.

[0091] Effect Test Example 2

[0092] Human skin fibroblasts experiment

[0093] Test method for type I and III collagen and cell viability promotion rate:

[0094] Human skin fibroblasts HSF were cultured in DMEM complete medium. When the fusion rate reached 80%, the old medium was discarded, and medium containing 0.001% anti-aging polypeptide was added for cell culture. After 24 hours of culture, the supernatant was aspirated and centrifuged at 10000 rpm for 10 minutes to remove cell debris and exosomes. The supernatant of the centrifuged culture medium was taken for detection of type I and III collagen content. The remaining cells were added with CCK8 reagent and incubated at 337 degrees for 4 hours for cell viability test. After the results were obtained, the promotion rate of type I and III collagen concentrations was obtained using the calculation formula [(drug histone concentration-blank histone concentration) / blank histone concentration]. The processing method for the promotion results of cell viability was the same as the collagen results. The results are shown in Table 4.

[0095] Table 4. Table of tested samples and type I and III collagen and cell viability promotion rate

[0096]

[0097]

[0098] It can be seen from Table 4 that under the condition of an added concentration of 0.001%, the anti-aging polypeptide of the present invention can significantly promote the activity of human skin fibroblasts and the content of type I and III collagen, which shows that the anti-aging polypeptide of the present invention can significantly enhance the activity of skin cells, inhibit aging, and enhance the expression of skin ECM.

[0099] Effect Test Example 3

[0100] Human skin fibroblasts experiment

[0101] HSF cell senescence model test method:

[0102] The detection of aging-related β-galactosidase is a classic method for effectively detecting cell aging. X-Gal (5-bromo-4-chloro-3-indole-β-D-galactoside) is the substrate of β-galactosidase. X-Gal itself is colorless. After being hydrolyzed by β-galactosidase, it produces galactose and blue 5-bromo-4-chloro-indigo. Using this feature of X-Gal, the activity of β-galactosidase can be indirectly measured. The lysosomal contents in aging cells usually increase, which increases the activity of the lysosomal enzyme β-galactosidase. Therefore, X-Gal can be used as a substrate to detect cell aging. Senescent cells appear blue after staining, while non-senescent cells are colorless. By staining human skin fibroblasts cultured with different anti-aging peptides for β-galactosidase, their anti-aging activity can be determined. After the three anti-aging peptides were used to detect the anti-aging activity of HSF cells, the results are as follows. Figure 4 show.

[0103] The results showed that the three anti-aging peptides can significantly improve cell aging, indicating that the three peptides have excellent anti-aging capabilities.

[0104] Effect Test Example 4

[0105] Essence anti-aging effect test method:

[0106] 1) Volunteers aged between 18 and 40 were divided into 9 groups, with 10 people in each group (5 males and 5 females);

[0107] 2) Clean the subject's face with the same facial cleanser in a constant temperature and humidity environment;

[0108] 3) In groups 1 to 6, a blank control sample was applied on the left side of the face and forehead, and samples of application examples 1 to 3 and comparative examples 1 to 3 were applied on the right side of the face and forehead, respectively, with a sample amount of 2±0.2 g;

[0109] 4) Apply the samples of Comparative Examples 1 to 3 on the left side of the face and forehead of Groups 7 to 9, and apply the samples of Application Examples 1 to 3 on the right side of the face and forehead, respectively, with a sample amount of 2±0.2 g;

[0110] 5) Use VISA facial tester to measure facial wrinkles for 12 hours and 24 hours, measure three sets of data at each symmetrical part and calculate the average value;

[0111] 6) Evaluate the anti-aging effect of the essence based on the percentile score (percentile score describes the skin feature score of the tester compared with other people of the same age, gender, and skin type; the higher the score, the better) given by the VISA facial tester (score after improvement - score before improvement) as the calculation.

[0112] The test results of anti-aging essence are shown in Table 5:

[0113] Table 5 Test results of anti-aging essence (number of people)

[0114]

[0115] In Table 5, the texture improvement values ​​of most people in Group 1, Group 2, and Group 3 were greater than 10%, and more than half of the people had a texture improvement value greater than 20% at 24 hours. This shows that Application Example 1, Application Example 2, and Application Example 3 have excellent anti-aging effects. In Table 5, the texture improvement values ​​of most people in Group 4, Group 5, and Group 6 were less than 10%, which shows that the comparative examples also have certain anti-aging effects, but the anti-aging effects are relatively weak.

[0116] The population of Group 7, Group 8 and Group 9 mainly concentrated in the range of texture improvement value of 10-20%, which indicates that the anti-aging effect of the application example is much better than that of the comparative example.

[0117] The above description is only a preferred embodiment of the present invention and does not limit the present invention in any form. Therefore, any simple modification, equivalent change and modification made to the above embodiment according to the technical essence of the present invention without departing from the technical solution of the present invention still fall within the scope of the technical solution of the present invention.

Claims

1. An anti-aging polypeptide, characterized in that: The anti-aging polypeptide comprises: Anti-aging peptide-1: Pal-Lys-Met-Lys-OH; The structural formula of anti-aging polypeptide-1 is as shown in Formula Ⅰ: Formula I and / or, anti-aging peptide-2: Ac-Ser-Pro-Ala-Gly-Gly-Pro-OH; The structural formula of anti-aging polypeptide-2 is as shown in Formula II: Formula II and / or, anti-aging peptide-3: Oct-Gly-Pro-OH; The structural formula of anti-aging polypeptide-3 is as shown in Formula III: Formula III 2. The method for synthesizing the anti-aging polypeptide according to claim 1, characterized in that: The preparation steps include: Step 1: Compound synthesis: 2-Chlorotriphenylmethyl chloride was weighed in a reaction tube, and DCM was added to swell at room temperature for 1 hour. After the solvent was drained, the DCM solution of the first amino acid monomer at the C-terminus and DIEA was added. After shaking reaction at room temperature for 1 hour, the resin was washed 3 times with DMF and DCM in sequence, and then drained; Then, the Fmoc protection was removed by adding 20% ​​piperidine / DMF solution for 2 times, each time for 10 min, and then the resin was washed with DCM and DMF for 3 times; After drying, the second amino acid was coupled by adding the activated second amino acid monomer DMF solution, shaking and reacting at room temperature for 1 hour, and then washing the resin with DMF and DCM three times in sequence and drying; Repeat the above steps of removing Fmoc protection, washing, coupling, and washing until the last amino acid monomer is completed; after all couplings are completed, perform Fmoc deprotection, washing, and drying; Then, the N-terminal was modified by adding palmitoyl chloride, acetyl chloride or octanoyl chloride, and DIEA in DCM to the resin, shaking and reacting at room temperature for 2 h, and then washing the resin three times with DMF and DCM in sequence and draining it; Step 2: Compound cleavage: Add the cutting reagent: trifluoroacetic acid / triisopropylsilane / water to the resin connected with the anti-aging active peptide, and shake the reaction at room temperature for 2 hours; collect the filtrate in a centrifuge tube, wash twice with DCM and acetonitrile, and combine the filtrate; after most of the solvent is blown dry by an air pump, add anhydrous ether to precipitate, mix thoroughly and centrifuge, pour the supernatant, and wash 3 times to obtain a crude product; Step 3: Compound purification: The polypeptide is dissolved in a solvent, and the crude product is further purified by washing, beating or recrystallization.

3. The method for synthesizing the anti-aging polypeptide according to claim 2, characterized in that: In the step 1: In the DCM solution of the first amino acid monomer at the C-terminus and DIEA, the concentration of the first amino acid monomer is 1.5 equiv, and the concentration of DIEA is 5 equiv.

4. The method for synthesizing the anti-aging polypeptide according to claim 2, characterized in that: In the step 1: The second amino acid monomer DMF solution includes 5 equiv of amino acid monomer, 4.75 equiv of condensing agent HBTU and 5 equiv of DIEA.

5. The method for synthesizing the anti-aging polypeptide according to claim 2, characterized in that: In the step 2: The ratio of the cleavage reagent is: trifluoroacetic acid / triisopropylsilane / water=95 / 2.5 / 2.

5.

6. The method for synthesizing the anti-aging polypeptide according to claim 2, characterized in that: In the step three: The solvent is acetonitrile, ethyl acetate and ethanol.

7. The use of the anti-aging polypeptide according to any one of claims 1 to 6, characterized in that: The application forms include but are not limited to application in daily chemicals; the daily chemicals are selected from anti-aging essence, anti-aging cream, and anti-aging mask.

8. The use of the anti-aging polypeptide according to claim 7, characterized in that: The application method in daily chemicals is to disperse the anti-aging polypeptide in solvents such as glycerin, propylene glycol, butylene glycol, etc. and then add the resulting solvents into cosmetic products.

9. The use of the anti-aging polypeptide according to claim 7, characterized in that: The daily chemical product is an anti-aging essence; The anti-aging essence contains the following percentage components: Phase A: water balance, EDTA-2Na 0.1%, carbomer 0.12%, xanthan gum 0.02%, hydroxyethyl cellulose 0.01%; Phase B: phenoxyethanol 0.4%, hexylene glycol 0.8%, ethylhexylglycerin 0.1%; Phase C: propylene glycol 2%, anti-aging polypeptide-1 and / or anti-aging polypeptide-2 and / or anti-aging polypeptide-3 0.001%-0.1%.

10. The use of the anti-aging polypeptide according to claim 9, characterized in that: The steps of preparing the anti-aging essence are as follows: 1) Add phase A into the reaction vessel in sequence, stir and disperse, raise the temperature to 75°C and keep stirring for 15 to 30 minutes; 2) After phase A is completely dispersed, add phase B and stir to cool down to below 40°C; 3) Add the mixed phase C and stir to disperse evenly to obtain the final anti-aging essence.

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