A polypeptide and its use in the preparation of anti-inflammatory and / or anti-aging products

Abstract

The application relates to the field of biological medicine, and provides a polypeptide and application of the polypeptide in preparation of anti-inflammatory and / or anti-aging products. The polypeptide is derived from bee venom, the amino acid sequence is shown as SEQ ID NO:1, the polypeptide has small molecular weight and good biocompatibility, exhibits excellent anti-inflammatory and anti-aging double biological activities, can effectively regulate key inflammation indexes, and plays a synergistic anti-aging role of inhibiting degradation and promoting synthesis through regulation of collagen metabolism balance. The application provides a new raw material selection for development of multifunctional and efficient anti-inflammatory and anti-aging products, and has wide application prospects in the fields of medicine, cosmetics, health products, medical biological materials and medical devices.

Description

Technical Field

[0001] This invention relates to the field of biomedical technology, and in particular to a polypeptide and its application in the preparation of anti-inflammatory and / or anti-aging products. Background Technology

[0002] Inflammation is a defensive response of the body's immune system to external stimuli or tissue damage, playing a crucial role in maintaining homeostasis. However, when the inflammatory response is excessive or persistent, it leads to abnormal expression of inflammatory mediators and inflammation-related cytokines (such as interleukin-6 (IL-6) and interleukin-8 (IL-8)), thereby causing tissue damage and being closely related to the development of various diseases. Currently, commonly used anti-inflammatory drugs mainly include nonsteroidal anti-inflammatory drugs (NSAIDs) and glucocorticoids. Although they can effectively relieve inflammatory symptoms, long-term or high-dose use is often accompanied by adverse reactions such as gastrointestinal damage, abnormal liver and kidney function, and immunosuppression. Furthermore, their ability to deeply regulate chronic inflammation and inflammation-related functional disorders is limited. Therefore, exploring novel anti-inflammatory substances that are naturally derived, highly safe, and possess clearly defined biological activities has significant research value and application prospects.

[0003] Aging is a gradual decline in physiological functions that occurs over time, and skin aging is one of the important external manifestations of aging. With increasing age and the cumulative effects of environmental factors (such as ultraviolet radiation), the structure of the dermis changes, collagen content decreases, and elastic fibers are damaged, leading to aging phenomena such as skin laxity and wrinkle formation. Studies have shown that type I collagen (Col-I) is an important component for maintaining skin structure and elasticity; reduced or degraded Col-I synthesis indicates accelerated skin aging. Matrix metalloproteinase-1 (MMP-1) plays a crucial role in collagen degradation; its overexpression accelerates collagen degradation and promotes skin aging. Currently, anti-aging active ingredients widely used in cosmetics and functional skincare products (such as vitamins, hyaluronic acid, and collagen) still face challenges in practical applications, including unclear bioactivity and limited efficacy. Therefore, developing novel functional ingredients with multiple bioactivities, stability, and suitability for skin health is a pressing issue in this field.

[0004] Polypeptides are small bioactive molecules formed by amino acids linked by peptide bonds. They are biocompatible, easily absorbed, and show potential for application in anti-inflammatory, antioxidant, and anti-aging activities. Bee venom is a natural complex rich in various bioactive components, possessing anti-inflammatory and immunomodulatory biological activities, but also exhibiting certain toxicity. Currently, research on peptides in bee venom is limited, and active peptides with anti-inflammatory and anti-aging effects remain to be discovered. Summary of the Invention

[0005] To address the aforementioned problems in the prior art, this invention provides a polypeptide and its application in the preparation of anti-inflammatory and / or anti-aging products, offering a new selection of active polypeptides for anti-inflammatory and anti-aging related products.

[0006] To achieve the above-mentioned objectives, the present invention provides the following technical solution:

[0007] In a first aspect, the present invention provides a polypeptide whose amino acid sequence is shown in SEQ ID NO:1, corresponding sequentially to polypeptide P1 described in the present invention. Polypeptide P1 is derived from Italian honeybees (…). Apis mellifera Bee venom sample.

[0008] Those skilled in the art should understand that homologous variants, conserved mutants, derivatives, and pharmaceutically acceptable salts of the polypeptide obtained by modifying it based on the amino acid sequence using conventional techniques should also be within the scope of protection of this invention.

[0009] Secondly, the present invention provides a nucleic acid molecule that encodes the aforementioned polypeptide.

[0010] Thirdly, the present invention provides a biomaterial containing the nucleic acid molecule, wherein the biomaterial is recombinant DNA, expression cassette, transposon, vector, microorganism or cell.

[0011] Fourthly, the present invention provides a conjugate comprising the polypeptide and a chemical moiety conjugated thereto.

[0012] According to a conjugate provided by the present invention, preferably, the composition further comprises an active ingredient having anti-inflammatory function.

[0013] According to a conjugate provided by the present invention, preferably, the composition further comprises an active ingredient having anti-aging function.

[0014] According to a conjugate provided by the present invention, preferably, the composition further comprises an active ingredient having anti-inflammatory and anti-aging functions.

[0015] Fifthly, the present invention provides a composition comprising the polypeptide.

[0016] The present invention also provides a product containing the polypeptide, or containing the nucleic acid molecule, or containing the biological material, or containing the conjugate, or containing the composition; the product is food, medicine, health product, cosmetic, medical biomaterial or medical device.

[0017] According to a product provided by the present invention, preferably, the effective concentration of the polypeptide in the product is 2μM to 50μM.

[0018] More preferably, the effective concentration of the polypeptide is 5 μM to 40 μM.

[0019] More preferably, the effective concentration of the polypeptide is 5 μM to 20 μM.

[0020] More preferably, the effective concentration of the polypeptide is 5 μM, 10 μM, 15 μM or 20 μM.

[0021] More preferably, the effective concentration of the polypeptide is 10 μM.

[0022] According to the present invention, the product is preferably a drug.

[0023] More preferably, the product further comprises a pharmaceutically acceptable carrier.

[0024] More preferably, the dosage form of the drug is a powder, tablet, granule, capsule, solution, emulsion or suspension.

[0025] According to the present invention, the product is preferably a cosmetic.

[0026] More preferably, the product further comprises a cosmetically acceptable carrier.

[0027] More preferably, the dosage form of the cosmetic is an aqueous solution, emulsion, ointment, essential oil, cream, powder, gel, mask, or spray.

[0028] More preferably, the cosmetic is a cleansing cosmetic, a skin care cosmetic, a beauty and makeup cosmetic, or a sunscreen cosmetic.

[0029] In a sixth aspect, the present invention provides the use of the polypeptide, the nucleic acid molecule, the biomaterial, the conjugate, or the composition in the preparation of anti-inflammatory and / or anti-aging products.

[0030] The use of the polypeptide, nucleic acid molecule, biomaterial, conjugate, or composition provided by the present invention in the preparation of anti-inflammatory and / or anti-aging products, preferably, the anti-inflammatory includes anti-skin inflammation.

[0031] The use of the polypeptide, nucleic acid molecule, biomaterial, conjugate, or composition provided by the present invention in the preparation of anti-inflammatory and / or anti-aging products, preferably, the anti-aging includes anti-skin aging.

[0032] According to the present invention, the application of the polypeptide, the nucleic acid molecule, the biomaterial, the conjugate or the composition in the preparation of anti-inflammatory and / or anti-aging products is preferably used to achieve one or more of the following objectives: (1) inhibiting the synthesis and / or secretion of inflammatory factors; (2) promoting the synthesis and / or secretion of collagen; (3) inhibiting the degradation of collagen.

[0033] More preferably, the inflammatory factors include IL-6 and / or IL-8.

[0034] More preferably, the collagen includes type I collagen.

[0035] More preferably, the inhibition of collagen degradation includes inhibiting the synthesis and / or secretion of matrix metalloproteinase-1.

[0036] According to the present invention, the use of the polypeptide, the nucleic acid molecule, the biomaterial, the conjugate, or the composition in the preparation of anti-inflammatory and / or anti-aging products, preferably, the effective concentration of the polypeptide in the product is 2 μM to 50 μM.

[0037] More preferably, the effective concentration of the polypeptide is 5 μM to 40 μM.

[0038] More preferably, the effective concentration of the polypeptide is 5 μM to 20 μM.

[0039] More preferably, the effective concentration of the polypeptide is 5 μM, 10 μM, 15 μM or 20 μM.

[0040] More preferably, the effective concentration of the polypeptide is 10 μM.

[0041] The application of the polypeptide, nucleic acid molecule, biomaterial, conjugate, or composition provided by the present invention in the preparation of anti-inflammatory and / or anti-aging products, preferably, the products are pharmaceuticals or cosmetics.

[0042] More preferably, the drug further comprises a pharmaceutically acceptable carrier.

[0043] More preferably, the dosage form of the drug is a powder, tablet, granule, capsule, solution, emulsion or suspension.

[0044] More preferably, the cosmetic product further comprises a cosmetically acceptable carrier.

[0045] More preferably, the dosage form of the cosmetic is an aqueous solution, emulsion, ointment, essential oil, cream, powder, gel, mask, or spray.

[0046] More preferably, the cosmetic is a cleansing cosmetic, a skin care cosmetic, a beauty and makeup cosmetic, or a sunscreen cosmetic.

[0047] Those skilled in the art should understand that the polypeptide described in this invention can be obtained by using any amino acid sequence of the polypeptide described in this invention through solid-phase synthesis, liquid-phase synthesis, recombinant expression, or equivalent techniques.

[0048] In a seventh aspect, the present invention provides a method for preparing the polypeptide, which is prepared by solid-phase synthesis according to the amino acid sequence shown in SEQ ID NO:1.

[0049] According to the method for preparing the polypeptide provided by the present invention, preferably, the product obtained by solid-phase synthesis is further purified by reversed-phase high-performance liquid chromatography.

[0050] The present invention has the following beneficial effects:

[0051] The polypeptide P1 derived from bee venom provided by this invention can effectively downregulate the expression levels of IL-6 and IL-8, inflammation-related factors, in endothelial cells induced by lipopolysaccharide, demonstrating excellent anti-inflammatory activity.

[0052] The polypeptide P1 derived from bee venom provided by this invention can effectively reduce the secretion level of matrix metalloproteinase-1 (MMP-1) in dermal cells and increase the content of type I collagen (Col-I), showing excellent anti-aging related biological activity.

[0053] The polypeptide P1 derived from bee venom provided by this invention has a clear origin, small molecular weight, and good biocompatibility. It exhibits excellent dual bioactivity of anti-inflammation and anti-aging, effectively regulating key inflammatory markers and exerting a synergistic anti-aging effect by inhibiting degradation and promoting synthesis through the regulation of collagen metabolism balance. This invention provides a new raw material option for developing multifunctional and highly effective anti-inflammatory and anti-aging products, and has broad application prospects in the fields of pharmaceuticals, cosmetics, health products, medical biomaterials, and medical devices. Attached Figure Description

[0054] To more clearly illustrate the technical solutions in this invention or the prior art, the drawings used in the description of the embodiments or the prior art will be briefly introduced below. Obviously, the drawings described below are some embodiments of this invention. For those skilled in the art, other drawings can be obtained from these drawings without creative effort.

[0055] Figure 1This is a graph showing the effect of polypeptide P1 provided in Example 2 of the present invention on the cytotoxicity of HUVEC cells; different lowercase letters indicate that the difference between groups is statistically significant (P < 0.05), and the same lowercase letter indicates that the difference between groups is not statistically significant (P > 0.05).

[0056] Figure 2 This is a graph showing the effect of polypeptide P1 provided in Example 2 of the present invention on the release of IL-6 in LPS-induced HUVEC cells; different lowercase letters indicate statistically significant differences between groups (P < 0.05), and the same lowercase letter indicates no statistically significant differences between groups (P > 0.05).

[0057] Figure 3 This is a graph showing the effect of polypeptide P1 provided in Example 2 of the present invention on the release of IL-8 in LPS-induced HUVEC cells; different lowercase letters indicate statistically significant differences between groups (P < 0.05), and the same lowercase letter indicates no statistically significant differences between groups (P > 0.05).

[0058] Figure 4 This is a graph showing the effect of polypeptide P1 provided in Example 3 of the present invention on the cytotoxicity of HDF cells; different lowercase letters indicate that the difference between groups is statistically significant (P < 0.05), and the same lowercase letter indicates that the difference between groups is not statistically significant (P > 0.05).

[0059] Figure 5 This is a graph showing the effect of polypeptide P1 provided in Example 3 of the present invention on the secretion of MMP-1 in HDF cells; different lowercase letters indicate that the difference between groups is statistically significant (P < 0.05), and the same lowercase letter indicates that the difference between groups is not statistically significant (P > 0.05).

[0060] Figure 6 This is a graph showing the effect of polypeptide P1 provided in Example 3 of the present invention on the secretion of Col-I in HDF cells; different lowercase letters indicate that the difference between groups is statistically significant (P < 0.05), and the same lowercase letter indicates that the difference between groups is not statistically significant (P > 0.05). Detailed Implementation

[0061] To make the objectives, technical solutions, and advantages of this invention clearer, the technical solutions of this invention will be clearly and completely described below with reference to the accompanying drawings. Obviously, the described embodiments are only some, not all, of the embodiments of this invention. All other embodiments obtained by those skilled in the art based on the embodiments of this invention without creative effort are within the scope of protection of this invention.

[0062] Unless otherwise specified, the experimental methods involved in the following embodiments are conventional methods in the art. For example, you can refer to the experimental manual in the art or follow the conditions recommended in the manufacturer's instructions.

[0063] Unless otherwise specified, all experimental materials and reagents used in the following examples are commercially available.

[0064] Example 1: Preparation of active peptides

[0065] 1. Determination of the active polypeptide sequence

[0066] Analysis of the polypeptide components of bee venom samples from Italian honeybees identified a potentially bioactive polypeptide P1 with the following amino acid sequence: GNGGGGLGSGGSLGLGHE (SEQ ID NO:1).

[0067] 2. Synthesis of bioactive peptides

[0068] The bee venom polypeptide P1 provided by this invention can be prepared through artificial synthesis, recombinant expression, and other methods. To facilitate subsequent bioactivity evaluation and application research, this embodiment uses a solid-phase polypeptide synthesis method for preparation. Details are as follows:

[0069] The polypeptide P1 was synthesized using a solid-phase polypeptide synthesis process with 9-fluorenemethoxycarbonyl (Fmoc) as the amino protecting group, and the polypeptide chain was assembled stepwise on 2-chlorotriphenylmethyl chloro resin.

[0070] During the synthesis, Fmoc-protected amino acid monomers were sequentially coupled to a resin support. This coupling reaction was carried out in an N,N-dimethylformamide (DMF) system, using diisopropylcarbodiimide (DIC) and Oxyma as coupling agents. After each amino acid coupling step, the coupling efficiency was monitored using ninhydrin (Kaiser) reagent. The Fmoc protecting groups were removed using a piperidine / DMF solution.

[0071] After the target amino acid sequence was assembled, each polypeptide was cleaved using a cleavage system containing trifluoroacetic acid (TFA) to detach it from the resin and remove the side chains. The resulting cleavage solution was then precipitated, centrifuged, and lyophilized to obtain the crude products of each polypeptide.

[0072] Subsequently, the crude products of each peptide were purified by preparative reversed-phase high-performance liquid chromatography (RP-HPLC), and necessary salt substitution treatment was performed to obtain purified peptide products.

[0073] The purity of each peptide was determined by analytical high-performance liquid chromatography (HPLC), and the molecular weight of peptide P1 was confirmed by electrospray ionization mass spectrometry (ESI-MS).

[0074] The test results showed that the purity of the prepared polypeptide P1 was not less than 95%, and its molecular weight was consistent with the theoretical calculation value, which could meet the requirements of subsequent bioactivity evaluation experiments.

[0075] It should be understood that the preparation method of the polypeptide P1 involved in this invention is not limited to the specific embodiments described above. It can also be obtained by other solid-phase synthesis methods, liquid-phase synthesis methods, recombinant expression methods or equivalent technical means. All polypeptide P1 prepared using the amino acid sequence described in this invention are within the protection scope of this invention.

[0076] Example 2 Evaluation of the anti-inflammatory effect of active peptides

[0077] 1. Experimental Methods

[0078] (1) Cell culture

[0079] Human umbilical vein endothelial cells (HUVECs) were cultured in complete endothelial cell culture medium (ECM basal medium containing 10% fetal bovine serum) and placed in a cell culture incubator at 37°C and 5% CO2. HUVECs were used for subsequent experiments when they adhered to the culture medium and reached approximately 85% confluence.

[0080] (2) Preparation of active polypeptide solution

[0081] The polypeptide P1 synthesized in Example 1 was fully dissolved in endothelial cell complete culture medium at working concentrations of 2 μM, 5 μM, 10 μM, 25 μM and 50 μM to obtain polypeptide P1 solutions of different concentrations.

[0082] (3) Determination of the effect of bioactive peptides on HUVEC cytotoxicity by MTT assay

[0083] HUVEC cells were adjusted to a density of 1×10⁶ cells using complete endothelial cell culture medium. 5 Cells / mL were seeded into 96-well plates, with 100 μL of HUVEC cell suspension added to each well.

[0084] After culturing for 24 hours, the culture medium was discarded, and different concentrations of peptide P1 solution from this embodiment were added as experimental groups, while an equal volume of complete endothelial cell culture medium without peptide P1 was added as the control group (i.e., the concentration of peptide P1 was 0 μM).

[0085] After culturing for another 24 hours, the culture medium was discarded, and the cells were washed twice with PBS. 100 μL of culture medium containing 0.5 g / L MTT was added to each well, and the cells were incubated in the dark for 4 hours. The supernatant was then discarded, and 150 μL of dimethyl sulfoxide (DMSO) was added to each well. The cells were shaken to fully dissolve the generated formazan crystals.

[0086] The absorbance (OD value) of each well was measured at a wavelength of 490 nm using an ELISA reader. Cell viability was calculated based on the OD value using the formula: Cell viability (%) = OD value of experimental group / OD value of control group × 100%.

[0087] (4) ELISA method was used to determine the effect of active peptides on LPS-induced secretion of inflammatory factors in HUVEC cells.

[0088] HUVEC cells in the logarithmic growth phase were harvested at a concentration of 1×10⁻⁶. 5 HUVEC cells were seeded at a density of 1 cell / mL in 24-well plates, with 1 mL of HUVEC cell suspension added to each well.

[0089] After culturing for 24 hours, the culture medium was discarded, and the peptide P1 solution of this embodiment was added to each group as the experimental group. An equal volume of complete endothelial cell culture medium without peptide P1 was added to each group as the model group and the control group, respectively.

[0090] After incubation for 2 hours, lipopolysaccharide (LPS) at a final concentration of 8 mg / L was added to each well of the experimental and model groups to induce inflammatory responses in the cells; an equal volume of complete endothelial cell culture medium without peptide P1 was added to the wells of the control group.

[0091] After culturing for another 24 hours, the culture supernatant of cells from each well was collected and centrifuged at 3000 rpm for 10 min to remove cell debris. The levels of IL-6 and IL-8 in the culture supernatant of cells from each well were detected using an enzyme-linked immunosorbent assay (ELISA) kit.

[0092] (5) Data processing

[0093] All experiments were performed in triplicate, and the results are expressed as mean ± standard deviation. Statistical methods were used to analyze the data between the experimental and control groups, with P < 0.05 indicating statistical significance.

[0094] 2. Experimental Results

[0095] (1) Effect of bioactive peptides on the survival rate of HUVEC cells

[0096] MTT test results are as follows Figure 1 As shown, within the concentration range of 2 μM to 50 μM, the survival rate of HUVEC cells treated with peptide P1 was higher than 86%, and no obvious cytotoxicity was observed.

[0097] MTT assay results show that, within the concentration range of 2 μM to 50 μM, the peptide P1 provided by this invention exhibits good biocompatibility and low toxicity in HUVEC cells, making it suitable for subsequent anti-inflammatory activity evaluation experiments.

[0098] (2) Effects of bioactive peptides on the secretion of inflammatory factors in HUVEC cells

[0099] like Figure 2 and Figure 3 As shown, compared with the control group, the HUVEC cells in the LPS-treated model group secreted significantly more inflammatory-related factors IL-6 and IL-8, indicating that the inflammatory cell model was successfully established. Compared with the model group, the secretion levels of IL-6 and IL-8 were significantly reduced after the addition of peptide P1, and showed a dose-dependent change trend in the concentration range of 2μM to 50μM. Among them, at the concentration of 50μM, peptide P1 had the most significant inhibitory effect on IL-6 and IL-8, with an inhibition rate of 56% for IL-6 secretion and 54% for IL-8 secretion.

[0100] ELISA results showed that the bee venom-derived polypeptide P1 provided by this invention could effectively inhibit the excessive secretion of LPS-induced inflammatory factors IL-6 and IL-8 in HUVEC cells within a concentration range of 2 μM to 50 μM, demonstrating excellent anti-inflammatory activity.

[0101] Example 3 Evaluation of the anti-aging effects of active peptides

[0102] 1. Experimental Methods

[0103] (1) Cell culture

[0104] Human dermal fibroblasts (HDF) were cultured in HDF cell culture medium (i.e., high-glucose DMEM medium containing 10% fetal bovine serum, 100 mg / L streptomycin, and 100 U / mL penicillin) and placed in a cell culture incubator at 37°C and 5% CO2. When the cells adhered and reached approximately 85% confluence, they were used for subsequent experiments.

[0105] (2) Preparation of active polypeptide solution

[0106] The polypeptide P1 synthesized in Example 1 was fully dissolved in HDF cell culture medium at working concentrations of 5 μM, 10 μM, 20 μM, 30 μM and 40 μM to obtain polypeptide P1 solutions of different concentrations.

[0107] (3) Determination of the effect of bioactive peptides on HDF cytotoxicity using the MTT assay

[0108] HDF cells in the logarithmic growth phase were digested with trypsin and counted. The density of HDF cells was then adjusted to 5 × 10⁶ cells / year using HDF cell culture medium. 4 Cells were seeded at a density of 100 μL / mL in 96-well plates, with 100 μL of HDF cell suspension added to each well.

[0109] After culturing for 48 hours, the culture medium was discarded, and different concentrations of peptide P1 solution from this embodiment were added as experimental groups, while an equal volume of HDF cell culture medium without peptide P1 was added as the control group (i.e., the concentration of peptide P1 was 0 μM).

[0110] After culturing for another 24 hours, the culture medium was discarded, and the cells were washed twice with PBS. 100 μL of HDF medium containing 0.5 g / L MTT was added to each well, and the cells were incubated in the dark for 4 hours. The supernatant was then discarded, and 150 μL of DMSO was added to each well. The cells were shaken to fully dissolve the generated formazan crystals.

[0111] The absorbance (OD value) of each well was measured at a wavelength of 490 nm using an ELISA reader. Cell viability was calculated based on the OD value using the formula: Cell viability (%) = OD value of experimental group / OD value of control group × 100%.

[0112] (4) ELISA method was used to determine the effect of active peptides on the secretion of MMP-1 and Col-I by HDF cells.

[0113] HDF cells in the logarithmic growth phase were harvested at a concentration of 5 × 10⁻⁶ cells / year. 4 The cells were seeded at a density of cells / mL in 96-well plates, with 100 μL of HDF cell suspension added to each well.

[0114] After culturing for 48 hours, the culture medium was discarded, and different concentrations of peptide P1 solution from this embodiment were added as experimental groups, while an equal volume of HDF cell culture medium without peptide P1 was added as a control group.

[0115] After culturing for 24 hours, the culture supernatant of cells from each well was collected and centrifuged at 4℃ and 3000 rpm for 20 min to remove cell debris. The contents of MMP-1 and Col-I in the culture supernatant of cells from each well were detected using an ELISA kit.

[0116] (5) Data processing

[0117] All experiments were performed in triplicate, and the results are expressed as mean ± standard deviation. Statistical methods were used to analyze the data between the experimental and control groups, with P < 0.05 indicating statistical significance.

[0118] 2. Experimental Results

[0119] (1) Effect of bioactive peptides on HDF cell survival

[0120] like Figure 4 As shown in the figure, within the concentration range of 5 μM to 40 μM, the survival rate of HDF cells treated with peptide P1 was higher than 89%, and no obvious cytotoxicity was observed.

[0121] MTT assay results show that, within the concentration range of 5 μM to 40 μM, the peptide P1 provided by this invention exhibits good biocompatibility and low toxicity to HDF cells, making it suitable for subsequent anti-aging-related activity evaluation experiments.

[0122] (2) Effects of bioactive peptides on the secretion of MMP-1 and Col-I by HDF cells

[0123] like Figure 5 As shown, within the concentration range of 5 μM to 40 μM, compared with the control group, the level of MMP-1 secreted by HDF cells generally decreased after treatment with peptide P1, with the most significant inhibitory effect at 10 μM, where the amount of MMP-1 secreted was reduced by about 28% compared with the control group.

[0124] like Figure 6 As shown, within the concentration range of 5 μM to 40 μM, compared with the control group, the content of Col-I secreted by HDF cells showed a trend of first increasing and then decreasing with the increase of peptide P1 concentration. Among them, when the peptide P1 concentration was 10 μM, the increase in MMP-1 secretion was the largest, which was 22% higher than that of the control group.

[0125] ELISA results show that the bee venom-derived polypeptide P1 provided by this invention can regulate the secretion levels of MMP-1 and Col-I, which are related to skin aging, in HDF cells, and has excellent anti-aging activity.

[0126] Finally, it should be noted that the above embodiments are only used to illustrate the technical solutions of the present invention, and not to limit them; although the present invention has been described in detail with reference to the foregoing embodiments, those skilled in the art should understand that modifications can still be made to the technical solutions described in the foregoing embodiments, or equivalent substitutions can be made to some of the technical features; and these modifications or substitutions do not cause the essence of the corresponding technical solutions to deviate from the spirit and scope of the technical solutions of the embodiments of the present invention.

Claims

1. A polypeptide, characterized in that, Its amino acid sequence is shown in SEQ ID NO:

1.

2. A nucleic acid molecule, characterized in that, It encodes the polypeptide described in claim 1.

3. A biomaterial, characterized in that, The biological material contains the nucleic acid molecule of claim 2, wherein the biological material is recombinant DNA, expression cassette, transposon, vector, microorganism or cell.

4. The use of the polypeptide of claim 1, the nucleic acid molecule of claim 2, or the biomaterial of claim 3 in the preparation of anti-inflammatory and / or anti-aging products.

5. The application according to claim 4, characterized in that, The product is used to achieve one or more of the following purposes: (1) Inhibit the synthesis and / or secretion of inflammatory factors; (2) Promotes collagen synthesis and / or secretion; (3) Inhibit collagen degradation.

6. The application according to claim 4, characterized in that, The product in question is a drug or cosmetic.

7. The application according to any one of claims 4 to 6, characterized in that, The effective concentration of the polypeptide is 2 μM to 50 μM.

8. The method for preparing the polypeptide according to claim 1, characterized in that, Prepared using solid-phase synthesis based on the amino acid sequence shown in SEQ ID NO:1.

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