Polypeptide composition as well as preparation method and application thereof

Abstract

The polypeptide composition is prepared from the following components in percentage by weight: 0.1 to 20 percent of carnosine, 0.01 to 10 percent of oligopeptide-1, 0.001 to 5 percent of blue copper peptide, 0.001 to 2 percent of DNA (deoxyribonucleic acid) sodium, 0.0001 to 1 percent of red scorpion four-membered cyclic peptide, 28.989 to 45 percent of betaine and 40 to 48.499 percent of sorbitol. Red scorpion four-membered cyclic peptide cooperates with the cell proliferation promoting function of tripeptide-1 copper and oligopeptide-1, the antioxidant effect of carnosine and the effect of DNA sodium activating mitochondrial metabolism to improve cell energy to achieve the synergistic anti-aging effect, betaine and sorbitol construct an ionic liquid synergistic permeation promoting system, and finally the instant-long-acting integrated anti-aging effect is achieved. The functional mechanism of each component is clear in action site, high in activity, high in acting speed, obvious in curative effect and high in safety, an ionic liquid technology and a penetration enhancing system cooperate to help transdermal absorption of polypeptide components, the active efficacy of the polypeptide components can be more easily exerted, the wrinkle condition of the skin can be improved, and the skin elasticity can be recovered.

Description

Technical Field

[0001] This invention belongs to the field of cosmetic technology, specifically relating to a polypeptide composition, its preparation method, and its application. Background Technology

[0002] Driven by factors such as changes in global demographics, a growing awareness of anti-aging, and more rational consumer decisions, consumers are increasingly demanding anti-aging cosmetics. The global anti-aging skincare market is projected to exceed $62 billion by 2025, with a compound annual growth rate of 7.0%. In terms of efficacy, consumers are shifting from "reducing surface wrinkles" to "structural anti-aging," with a significant increase in demand for combined effects that offer "immediate wrinkle reduction + long-lasting repair."

[0003] Cosmetic peptides are small molecular fragments composed of 2-50 amino acids, which have three major advantages: (1) strong targeting and clear anti-aging mechanism; (2) mild and hypoallergenic, suitable for a variety of skin types; and (3) wide adaptability of dosage forms and flexible use scenarios. Therefore, peptide ingredients have become popular core raw materials for high-end anti-aging products.

[0004] However, traditional skincare peptides still face three major industry challenges due to their structure and application technology: (1) Most peptides have a molecular weight exceeding 500 Daltons, making it difficult to penetrate the stratum corneum, resulting in poor transdermal absorption; (2) Traditional peptides are easily hydrolyzed by skin enzymes, and their activity retention rate is often below 60% at 45°C, leading to insufficient stability; (3) Traditional peptides often target a single aging site, resulting in relatively limited and singular efficacy. The market still needs to address the challenges of multi-target synergy, efficient penetration, and stable retention of peptide components, and to construct a complex peptide system. Summary of the Invention

[0005] The purpose of this invention is to address the deficiencies of the prior art by providing a polypeptide composition that can effectively improve skin wrinkles and restore skin elasticity.

[0006] To achieve the objectives of this invention, the following technical solution is adopted: A polypeptide composition comprising the following components in weight percentage: carnosine 0.1-20%, oligopeptide-1 0.01-10%, copper peptide 0.001-5%, sodium DNA 0.001-2%, red scorpion tetracyclic peptide 0.0001-1%, betaine 28.989-45%, and sorbitol 40-48.499%.

[0007] Preferably, the polypeptide composition comprises the following components in weight percentage: carnosine 10-20%, oligopeptide-1 0.01-5%, copper peptide 3-5%, sodium DNA 0.001-2%, red scorpion tetracyclic peptide 0.5-1%, betaine 30%, and sorbitol 45.989-47.5%.

[0008] Preferably, the polypeptide composition comprises the following components in weight percentage: carnosine 10-20%, oligopeptide-1 0.01-10%, blue copper peptide 0.001-5%, sodium DNA 0.001-2%, red scorpion tetracyclic peptide 0.01-1%, betaine 28.989-30%, and sorbitol 40-47.5%.

[0009] Preferably, the polypeptide composition comprises the following components in weight percentage: carnosine 0.1-10%, oligopeptide-1 5-10%, blue copper peptide 0.001-5%, sodium DNA 1-2%, red scorpion tetracyclic peptide 0.0001-0.5%, betaine 30-45%, and sorbitol 42.899-48.499%.

[0010] Secondly, the present invention provides a method for preparing the above-mentioned polypeptide composition, comprising: mixing and dissolving carnosine, oligopeptide-1, blue copper peptide, sodium DNA, red scorpion tetracyclic peptide, betaine, and sorbitol, homogenizing, and obtaining the polypeptide composition.

[0011] Thirdly, the present invention provides the application of the above-mentioned polypeptide composition in cosmetics.

[0012] Fourthly, the present invention provides a cosmetic product comprising the polypeptide composition described in the first aspect of the present invention.

[0013] Preferably, the polypeptide composition accounts for 0.1-10% of the cosmetic product by mass.

[0014] Preferably, the polypeptide composition accounts for 0.1-5% of the cosmetic by mass.

[0015] Preferably, the types of cosmetics include, but are not limited to, toners, serums, lotions, creams, masks, or gels.

[0016] In the composition of this invention, carnosine is a multifunctional anti-aging cosmetic ingredient with strong antioxidant capabilities. It can restore the activity of cellular superoxide dismutase (SOD), restore the activity of catalase (CAT), reduce the content of malondialdehyde (MDA) in cells, and affect the expression level of matrix metalloproteinase-1 (MMP-1) protein, thereby comprehensively preventing damage to cells from various environmental oxidative factors and significantly delaying cell aging and degeneration. Oligopeptide-1 promotes cell regeneration, makes the skin smooth and delicate, reduces wrinkles, strengthens the skin barrier, resists damage from external harmful substances, accelerates the repair process, increases the intercellular matrix, retains moisture, reduces water evaporation, promotes the proliferation of dermal fibroblasts, and increases skin elasticity. Blue copper peptide is a tripeptide that forms with copper ions. This is a polypeptide complex that naturally exists in the human body and has a high safety profile. It is an effective skin repair factor that can improve wound healing and quickly soothe skin trauma. Skin damage disrupts the body's protective barrier function, making it easier for harmful microorganisms such as bacteria and viruses to penetrate the skin barrier and cause infection and disease. Furthermore, it can significantly improve the migration ability of epidermal cells and inhibit the expression of inflammatory mediators, such as COX-2 protein, thereby promoting wound healing and alleviating inflammatory responses and reducing the chance of infection. In addition, it can promote the expression of type I collagen, making the skin structure younger and firmer. Sodium DNA (PDRN) activates adenosine A2A in human cells... The receptor (ADORA2A) enables multiple physiological regulation: inhibiting the release of inflammatory factors (such as TNF-α and IL-6), reducing skin redness and sensitivity, promoting fibroblast proliferation and collagen synthesis, accelerating tissue regeneration, stimulating angiogenesis, improving microcirculation, supplying oxygen and nutrients to damaged skin, providing purine / pyrimidine raw materials for cellular "rescue pathways," and assisting DNA repair, especially playing a key role in hypoxic or aging cells; Red Scorpion Tetracyclic Peptide is a biomimetic cyclic peptide with the chemical name "S-pyroglutamyl S-snail hexapeptide-1 (cycloglutamyl S-snail hexapeptide-2) S-snail nonapeptide-1 amide" (National Cosmetic Product Approval Number 20250044). It can effectively intervene in SNAP-25 protein, competitively inhibit the formation of SNARE complex, reduce neurotransmitter release, reduce muscle contraction frequency and improve expression lines, and promote fibroblast synthesis of collagen VII / XVII, strengthen the skin's supporting structure and improve skin elasticity.

[0017] This product combines four peptides—Oligopeptide-1, Carnosine, Tripeptide-1 Copper, and Red Scorpion Tetracyclic Peptide—with sodium DNA (PDRN) to exert anti-aging effects. Utilizing the four-membered ring structure of the Red Scorpion Tetracyclic Peptide as a "stabilizing core," it works synergistically with the cell proliferation-promoting functions of Tripeptide-1 Copper and Oligopeptide-1, the antioxidant effects of Carnosine, and the mitochondrial metabolism-activating and cellular energy-boosting effects of sodium DNA to achieve a synergistic anti-aging effect. Furthermore, a betaine and sorbitol are used to construct an ionic liquid synergistic penetration-enhancing system, resolving the contradiction between peptide transdermal penetration and stability, ultimately achieving an integrated "immediate-long-lasting" anti-aging effect. It improves skin wrinkles and restores skin elasticity.

[0018] Compared with existing technologies, the present invention has the following beneficial effects: the mechanism of action of each component is clear, the activity is strong, the effect is fast and the curative effect is obvious. Since it is synthesized by biotechnology, the purity is high, the quality is stable and no substances with side effects are introduced, and the safety is higher. The ionic liquid technology and the penetration-enhancing system help the peptide components to be absorbed through the skin, making it easier to exert their active effects. Therefore, it is a good choice to improve skin aging, and can improve skin wrinkles and restore skin elasticity. Detailed Implementation

[0019] To facilitate understanding of the present invention, a more complete description will be given below with reference to specific embodiments. Preferred embodiments of the invention are provided. However, the invention can be implemented in many different forms and is not limited to the embodiments described herein. Rather, these embodiments are provided to provide a thorough and complete understanding of the disclosure of the invention.

[0020] Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention pertains. The terminology used herein in the description of the invention is for the purpose of describing particular embodiments only and is not intended to be limiting of the invention.

[0021] Unless otherwise specified, the experimental methods used in the following examples and comparative examples are conventional methods, and the materials and reagents used are commercially available unless otherwise specified.

[0022] Example 1 A polypeptide composition comprising the polypeptide components listed in Table 1 below.

[0023] Table 1. Polypeptide component formulation

[0024] Preparation method: Carnosine, oligopeptide-1, blue copper peptide, sodium DNA, red scorpion tetracyclic peptide, betaine, and sorbitol were mixed and dissolved according to the mass fractions, and homogenized at 40℃ for 20 min using a high-pressure ultrasonic homogenizer to obtain a polypeptide composition.

[0025] Example 2 A polypeptide composition comprising the polypeptide components listed in Table 2 below.

[0026] Table 2. Polypeptide component formulation

[0027] The preparation method is the same as in Example 1.

[0028] Example 3 A polypeptide composition comprising the polypeptide components listed in Table 3 below.

[0029] Table 3. Polypeptide component formulation

[0030] The preparation method is the same as in Example 1.

[0031] Example 4 A polypeptide composition comprising the polypeptide components listed in Table 4 below.

[0032] Table 4. Polypeptide component formulation

[0033] The preparation method is the same as in Example 1.

[0034] Example 5 A polypeptide composition comprising the polypeptide components listed in Table 5 below.

[0035] Table 5. Polypeptide component formulation

[0036] The preparation method is the same as in Example 1.

[0037] Comparative Example 1 Compared with Example 5, Comparative Example 1 replaced oligopeptide-1 with an equal amount of water, and was otherwise the same as Example 5.

[0038] Comparative Example 2 Compared with Example 5, Comparative Example 2 replaced carnosine with water in equal amounts, and was otherwise the same as Example 5.

[0039] Comparative Example 3 Compared with Example 5, Comparative Example 3 replaced the copper peptide with water in equal amounts, and was otherwise the same as Example 5.

[0040] Comparative Example 4 Compared with Example 5, Comparative Example 4 replaced sodium DNA with water in equal amounts, otherwise it was the same as Example 5.

[0041] Comparative Example 5 Compared with Example 5, Comparative Example 5 replaced the red scorpion tetracyclic peptide with water in equal amounts, and was otherwise the same as Example 5.

[0042] Comparative Example 6 Compared with Example 5, Comparative Example 6 replaced betaine with water in equal amounts, and was otherwise the same as Example 5.

[0043] Comparative Example 7 Compared with Example 5, Comparative Example 7 replaced sorbitol with water in equal amounts, and was otherwise the same as Example 5.

[0044] Comparative Example 8 Compared with Example 5, Comparative Example 8 replaced oligopeptide-1, carnosine, blue copper peptide, sodium DNA, and red scorpion tetracyclic peptide with water in equal amounts, while the rest was the same as in Example 5.

[0045] Comparative Example 9 Compared with Example 5, Comparative Example 9 replaced oligopeptide-1, carnosine, blue copper peptide, sodium DNA, red scorpion tetracyclic peptide, and betaine with water in equal amounts, while the rest was the same as in Example 5.

[0046] Comparative Example 10 Compared with Example 5, Comparative Example 10 replaced oligopeptide-1, carnosine, blue copper peptide, sodium DNA, red scorpion tetracyclic peptide, and sorbitol with water in equal amounts, while the rest was the same as in Example 5.

[0047] Comparative Example 11 Compared with Example 5, Comparative Example 11 replaced oligopeptide-1 with palmitoyl tripeptide-1 in equal amounts, and was otherwise the same as Example 5.

[0048] Comparative Example 12 Compared with Example 5, Comparative Example 12 replaced carnosine with an equal amount of glutathione, and was otherwise the same as Example 5.

[0049] Comparative Example 13 Compared with Example 5, Comparative Example 13 replaced the copper peptide with palmitoyl tripeptide-5 in equal amounts, and was otherwise the same as Example 5.

[0050] Comparative Example 14 Compared to Example 5, Comparative Example 14 replaced sodium DNA with an equal amount of ceramide NP, otherwise it was the same as Example 5.

[0051] Comparative Example 15 Compared with Example 5, Comparative Example 15 replaced the red scorpion tetracyclic peptide with an equal amount of arginine / lysine polypeptide, and was otherwise the same as Example 5.

[0052] Comparative Example 16 Compared with Example 5, Comparative Example 16 replaced the red scorpion tetracyclic peptide with acetyl hexapeptide-8 in equal amounts, and was otherwise the same as Example 5.

[0053] Comparative Example 17 Compared with Example 5, Comparative Example 17 replaced betaine with sodium polyglutamate in equal amounts, and was otherwise the same as Example 5.

[0054] Comparative Example 18 Compared with Example 5, Comparative Example 18 replaced sorbitol with isopropanol in equal amounts, and was otherwise the same as Example 5.

[0055] Application Example 1 A firming and anti-wrinkle serum containing a polypeptide composition, the specific formula of which is shown in Table 6.

[0056] Table 6

[0057] The preparation method of this firming and anti-wrinkle serum includes the following steps: (1) Add phase A raw material to the emulsification pot and heat to 75-80℃, stirring until dissolved and homogeneous; (2) Dissolve the B phase raw material at 60-65℃ until it becomes transparent, and set aside for later use; (3) When the emulsifying pot cools down to 60-65℃, add the B phase raw material to the emulsifying pot and stir evenly; (4) After the emulsification pot cools down to below 40°C, add the C phase raw material, mix and stir until evenly dispersed; (5) After passing the inspection, filter the material through a 300-mesh filter.

[0058] Application Example 2 A firming and anti-wrinkle lotion containing a polypeptide composition, the specific formulation of which is shown in Table 7.

[0059] Table 7

[0060] The above-mentioned firming and anti-wrinkle emulsion is prepared by the following method: (1) Add phase A into the emulsifying pot, stir evenly, and heat and stir to 75~85℃; (2) Add phase B to the oil phase pot, stir evenly, and heat and stir to 75~85℃; (3) Pump the material in the oil phase pot into the emulsifying pot, stir evenly, then vacuum the emulsifying pot and homogenize for 10 minutes. (4) Keep warm for 15 minutes, then turn on the cooling water to cool to 40°C, add phase C, and stir evenly; (5) Cool down to 35℃ and discharge the material after passing inspection.

[0061] Application Example 3 Compared to Application Example 2, the polypeptide composition of Example 5 was replaced with the polypeptide composition of Example 1 in equal amounts, while all other aspects remained the same.

[0062] Application Example 4 Compared to Application Example 2, the polypeptide composition of Example 5 was replaced with the polypeptide composition of Example 2 in equal amounts, while all other aspects remained the same.

[0063] Application Example 5 Compared to Application Example 2, the polypeptide composition of Example 5 was replaced with the polypeptide composition of Example 3 in equal amounts, while all other aspects remained the same.

[0064] Application Example 6 Compared to Application Example 2, the polypeptide composition of Example 5 was replaced with the polypeptide composition of Example 4 in equal amounts, while all other aspects remained the same.

[0065] Comparative Application Example 1 Compared with Application Example 2, the polypeptide composition of Example 5 was replaced with the composition of Comparative Example 1 in equal amounts, and all other aspects were the same.

[0066] Comparative Application Example 2 Compared to Application Example 2, the polypeptide composition of Example 5 was replaced with the composition of Comparative Example 2 in equal amounts, while all other aspects remained the same.

[0067] Comparative Application Example 3 Compared to Application Example 2, the polypeptide composition of Example 5 was replaced with the composition of Comparative Example 3 in equal amounts, while all other aspects remained the same.

[0068] Comparative Application Example 4 Compared to Application Example 2, the polypeptide composition of Example 5 was replaced with an equal amount of the composition of Comparative Example 4, and everything else remained the same.

[0069] Comparative Application Example 5 Compared with Application Example 2, the polypeptide composition of Example 5 was replaced with the composition of Comparative Example 5 in equal amounts, and everything else was the same.

[0070] Comparative Application Example 6 Compared with Application Example 2, the polypeptide composition of Example 5 was replaced with the composition of Comparative Example 11 in equal amounts, and all other aspects were the same.

[0071] Comparative Application Example 7 Compared with Application Example 2, the polypeptide composition of Example 5 was replaced with the composition of Comparative Example 12 in equal amounts, and all other aspects were the same.

[0072] Comparative Application Example 8 Compared with Application Example 2, the polypeptide composition of Example 5 was replaced with the composition of Comparative Example 13 in equal amounts, and all other aspects were the same.

[0073] Comparative Application Example 9 Compared with Application Example 2, the polypeptide composition of Example 5 was replaced with the composition of Comparative Example 14 in equal amounts, and all other aspects were the same.

[0074] Comparative Application Example 10 Compared to Application Example 2, the polypeptide composition of Example 5 was replaced with an equal amount of the composition of Comparative Example 15, and all other aspects remained the same.

[0075] Comparative Application Example 11 Compared to Application Example 2, the polypeptide composition of Example 5 was replaced with an equal amount of the composition of Comparative Example 16, and all other aspects remained the same.

[0076] Comparative Application Example 12 Compared to Application Example 2, the polypeptide composition of Example 5 was replaced with an equal amount of the composition of Comparative Example 17, and all other aspects remained the same.

[0077] Comparative Application Example 13 Compared to Application Example 2, the polypeptide composition of Example 5 was replaced with an equal amount of the composition of Comparative Example 18, and all other aspects remained the same.

[0078] Experimental Example 1: Experiment on Promoting the Expression of Type XVII Collagen and Elastin in a Full-Thickness Skin Model Comparative Examples 6-7 showed insoluble substances, so no further tests were conducted. Removing either betaine or sorbitol did not achieve the target composition, indicating that betaine and sorbitol are indispensable for the realization of this composition.

[0079] Examples 1-5, Comparative Examples 1-5, and Comparative Examples 8-18 were prepared into sample solutions of the same concentration and the following experiments were conducted: T-Skin TM Ex vivo skin samples from the full-thickness skin model were pretreated. The skin samples were placed in culture dishes and treated with Examples 1-5, Comparative Examples 1-5, and Comparative Examples 8-18 respectively. They were then cultured in a constant temperature incubator at 35℃ for 6 days. After the culture, the samples were immunohistochemically stained, observed using an electron fluorescence microscope, and quantitatively analyzed using Image Pro Plus software to calculate the changes. The solvent group was used as a blank control. The results are shown in Table 8.

[0080] Table 8. Effects on the expression of type XVII collagen and elastin

[0081] Type XVII collagen effectively resists mechanical stress and prevents the separation of the epidermis and dermis by connecting keratinocytes to the basement membrane. It is the molecular basis for the skin's resistance to friction and tearing. Its expression declines with age, leading to thinning of the basement membrane and epidermis, and a decline in repair capacity. Exogenous supplementation or promotion of its expression can reverse these changes and improve skin elasticity, thickness, and barrier function. Elastin is a core component of the extracellular matrix in the dermis, accounting for 2-4% of the skin's dry weight. Together with collagen, it forms a "rigid scaffold-elastic spring" dual-track system, which is the direct molecular basis for maintaining skin firmness and preventing sagging.

[0082] As shown in Table 8, compared with the blank control, Examples 1-5, Comparative Examples 1-5, and Comparative Examples 11-18 all promoted the expression of type XVII collagen and elastin, indicating that betaine and sorbitol had no effect on promoting the expression of type XVII collagen and elastin. A comparison of the results of Example 5 with Comparative Examples 1-5 shows that replacing any polypeptide component in the composition with water did not achieve the effect of Example 5. A comparison of Example 5 with Comparative Examples 11-18 shows that replacing components of the composition with similar ingredients did not achieve the effect of the composition of the present invention, indicating that each component of the present invention is indispensable. Furthermore, Example 5 showed a superior sum of the simple promoting effects compared to Comparative Examples 1-5, indicating a synergistic effect among the components of the examples.

[0083] Experimental Example 2: Skin Permeability Test Transdermal tests were conducted on Examples 1-5 and Comparative Examples 17-18 to test their permeability. The test methods are as follows: (1) Prepare the sample into a 50 mg / ml aqueous solution and ensure that the sample is completely and evenly dissolved; (2) Process the pig skin sample into thin slices of uniform thickness and without damage, remove subcutaneous fat and connective tissue, rinse with physiological saline and set aside. (3) Fix the processed pig skin sample between the donor and recipient pools of the Franz diffusion cell, ensuring that the skin is in close contact with the diffusion cell and there are no air bubbles.

[0084] (4) Add an appropriate amount of PBS buffer to the receiver pool, turn on the thermostatic magnetic stirrer, and maintain the temperature at 32℃-37℃ to simulate human skin temperature. Continue stirring to ensure uniform drug concentration in the receiver medium. (5) At 24h and 48h, a certain amount of receiving solution was taken from the receiver pool, and an equal amount of fresh receiving medium was added. The concentration of peptides (oligopeptide-1, carnosine, copper peptide, sodium DNA, and red scorpion tetracyclic peptide) in the receiving solution was determined by analytical methods such as HPLC. The cumulative permeation amount and permeation rate of the peptides were calculated according to the formula. The results are shown in Table 9.

[0085] Table 9. Results of transdermal assay of polypeptide compositions

[0086] The experimental results show that the cumulative permeation amount and permeation rate of the polypeptides in Examples 1-5 are better than those in the comparative examples, indicating that the polypeptide compositions of the present invention have good skin permeability. The results of Examples 1-5 and Comparative Examples 17 and 18 show that the ionic liquid technology used in the present invention has a promoting effect on the permeation of polypeptides.

[0087] Experiment Example 3: Human Trial Evaluation 375 participants aged 25-55 years, selected for their noticeable wrinkles and decreased skin elasticity, were recruited as test subjects. The participants were evenly divided into 15 groups of 25 each, with an average of 50% male and 50% female. Each group used the following samples twice daily, morning and evening: Application Examples 1-2, Control Examples 1-13, and a blank sample on the left and right sides of the face respectively. No other products were used during the test. Follow-up tests were conducted on days 14 and 28. During the tests, participants washed their faces and sat quietly for at least 20 minutes in an environment of 22±1℃ and 50% relative humidity, maintaining a relaxed state. Facial images were taken using a Visia 2010 facial image analyzer to analyze wrinkle conditions and comprehensively evaluate the anti-wrinkle effect of the samples. Skin elasticity testers were used to measure the R2, R5, and R7 values ​​of facial skin elasticity before and after sample use, and the combined data were used to evaluate the skin-tightening effect of the samples. The results are shown in Tables 10 and 11.

[0088] Table 10. Changes in wrinkles after using the sample

[0089] Table 11. Changes in skin elasticity after sample use

[0090] As shown in Tables 10 and 11, after 28 days of human efficacy evaluation testing, the subjects using Application Examples 1-2 showed better average improvement in wrinkles and skin elasticity than those using Comparative Application Examples 1-13. Specifically, after 28 days of using Application Example 2, the subjects showed significantly better changes in the number of facial wrinkles, total wrinkle area, average wrinkle length, wrinkle depth, and skin elasticity-related indicators compared to Comparative Application Examples 1-13. This demonstrates that omitting any one of the following ingredients—Oligopeptide-1, Carnosine, Blue Copper Peptide, Sodium DNA, or Red Scorpion Tetracyclic Peptide—significantly reduces the firming and anti-wrinkle effect; replacing any one with a similar ingredient also reduces the firming and anti-wrinkle effect.

[0091] The preferred embodiments of the present invention have been described in detail above. These are the results of numerous experiments conducted by the inventors with considerable human, financial, and time investment. It should be understood that those skilled in the art can make many modifications and variations based on the concept of the present invention without creative effort. Therefore, all technical solutions that can be obtained by those skilled in the art based on the concept of the present invention through logical analysis, reasoning, or limited experimentation on the basis of existing technology should be within the scope of protection defined by these claims.

Claims

1. A polypeptide composition, characterized in that, It includes the following components by weight percentage: carnosine 0.1-20%, oligopeptide-1 0.01-10%, blue copper peptide 0.001-5%, sodium DNA 0.001-2%, red scorpion tetracyclic peptide 0.0001-1%, betaine 28.989-45%, and sorbitol 40-48.499%.

2. The polypeptide composition according to claim 1, characterized in that, The polypeptide composition comprises the following components in weight percentage: carnosine 10-20%, oligopeptide-1 0.01-5%, copper peptide 3-5%, sodium DNA 0.001-2%, red scorpion tetracyclic peptide 0.5-1%, betaine 30%, and sorbitol 45.989-47.5%.

3. The polypeptide composition according to claim 1, characterized in that, The polypeptide composition comprises the following components in weight percentage: carnosine 10-20%, oligopeptide-1 0.01-10%, copper peptide 0.001-5%, sodium DNA 0.001-2%, red scorpion tetracyclic peptide 0.01-1%, betaine 28.989-30%, and sorbitol 40-47.5%.

4. The polypeptide composition according to claim 1, characterized in that, The polypeptide composition comprises the following components in weight percentage: carnosine 0.1-10%, oligopeptide-1 5-10%, blue copper peptide 0.001-5%, sodium DNA 1-2%, red scorpion tetracyclic peptide 0.0001-0.5%, betaine 30-45%, and sorbitol 42.899-48.499%.

5. A method for preparing a polypeptide composition as described in any one of claims 1 to 4, characterized in that... The process includes the following steps: mixing and dissolving carnosine, oligopeptide-1, copper peptide, sodium DNA, red scorpion tetracyclic peptide, betaine, and sorbitol, then homogenizing to obtain a polypeptide composition.

6. The use of the polypeptide composition according to any one of claims 1 to 4 in cosmetics.

7. A cosmetic product, characterized in that, The cosmetic comprises a polypeptide composition as described in any one of claims 1 to 4.

8. The cosmetic product according to claim 7, characterized in that, The polypeptide composition accounts for 0.1-10% of the mass of the cosmetic product.

9. The cosmetic product according to claim 7, characterized in that, The polypeptide composition accounts for 0.1-5% of the cosmetic's mass.

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