A repair polypeptide sc17-2 and its application in skin repair

Abstract

The application belongs to the technical field of polypeptides, and particularly relates to a repair polypeptide SC17-2 and application thereof in skin repair. The repair polypeptide SC17-2 comprises an amino acid sequence shown in SEQ ID NO:1. The repair polypeptide SC17-2 has multiple functions of skin wound repair, improvement of skin antioxidant activity and promotion of skin angiogenesis, thereby achieving more excellent skin repair function. Meanwhile, the repair polypeptide SC17-2 has good chemical stability, strong adaptability to different environmental conditions and is easy to be synthesized industrially.

Description

TECHNICAL FIELD

[0001] The application belongs to the technical field of polypeptides, and particularly relates to a repair polypeptide SC17-2 and application thereof in skin repair. BACKGROUND

[0002] Skin is an organ wrapped on the surface of the body, directly contacting with the external environment, and has the functions of protection, excretion, temperature regulation, and stimulation reception. It can resist the invasion of pathogenic bacteria on the skin surface and plays a very important protective role for human health. Once the skin is damaged, the skin barrier is destroyed, resulting in the loss of normal protective function of the skin, and the pathogenic bacteria on the skin surface can easily enter the inside of the skin through the damaged skin barrier, thereby further triggering a series of pathological reactions including skin inflammation.

[0003] For a long time, skin repair has been a problem that has been concerned in the field. The repair of the skin mainly includes the repair after skin trauma, the improvement of the antioxidant function of the skin, and the promotion of the generation of blood vessels, and there are some targeted repair schemes in the prior art. For the repair after skin trauma, there are some substances or methods for skin repair and related functions in the prior art, such as the use of growth factors in some studies. Growth factors bind to receptors on the surface of cells, trigger intracellular signal transduction pathways, and promote cell proliferation and migration to promote wound healing. However, these growth factors may have problems such as poor stability, high preparation cost, and possible immune response in actual application, and the process of repairing the skin by growth factors is relatively isolated and is not effectively integrated with other functions, for example, a large amount of free radicals generated during the wound healing process are not treated at the same time, which may affect the quality and speed of skin healing. For the antioxidant property after skin damage, natural antioxidants such as vitamin C, vitamin E and their derivatives, or some plant extracts are used in some studies to enhance the antioxidant activity of the skin. Although these antioxidants can neutralize free radicals to some extent, they lack active promotion of other physiological processes such as extracellular matrix reconstruction during the skin trauma repair process. For the promotion of angiogenesis after skin damage, substances such as vascular endothelial growth factor (VEGF) are used in some studies to promote angiogenesis, which mainly act on vascular endothelial cells, stimulate the proliferation and migration of vascular endothelial cells, and thereby promote the formation of blood vessels. However, when these substances are used alone to promote angiogenesis, the local microenvironment may change and affect their effect, and the problem of oxidative stress during neovascularization is not considered, nor is the cell proliferation during the skin trauma repair process effectively integrated.

[0004] It can be seen that the substances with skin repair function in the prior art mainly have single function, and there is a lack of substances that can achieve multifunctional synergy. SUMMARY

[0005] The present application aims to provide a repair polypeptide SC17-2 and its application in skin repair, which has multiple functions of skin wound repair, skin antioxidant activity improvement and skin angiogenesis promotion, thereby achieving more excellent skin repair function.

[0006] The present application provides a repair polypeptide SC17-2, which comprises an amino acid sequence shown in SEQ ID NO: 1.

[0007] Preferably, two cysteines in the amino acid sequence shown in SEQ ID NO: 1 are combined into a cyclic peptide by a disulfide bond.

[0008] The present application also provides an application of the repair polypeptide SC17-2 in the above technical solution in the preparation of a skin repair product.

[0009] Preferably, the skin repair product comprises a product having one or more functions of skin wound repair, skin antioxidant activity improvement and skin angiogenesis promotion.

[0010] Preferably, the product comprises a cosmetic and / or a drug.

[0011] Preferably, the drug comprises a drug having one or more functions of treating body surface wounds, treating body surface burns and treating skin ulcers.

[0012] Preferably, the cosmetic comprises a cosmetic having one or more functions of reducing scar formation, accelerating scar repair and antioxidant function.

[0013] The present application also provides a skin repair product, and an effective component of the skin repair product comprises the repair polypeptide SC17-2 in the above technical solution.

[0014] Preferably, the product comprises a cosmetic and / or a drug.

[0015] Preferably, the auxiliary materials in the cosmetic comprise one or more of sorbitol, butanediol, beeswax, mineral fat, tea tree oil, elastin, active peptide, herbal plant extract, cell active ingredient and vitamin.

[0016] Beneficial effects:

[0017] The application provides a repair polypeptide SC17-2, which comprises an amino acid sequence shown in SEQ ID NO: 1. The repair polypeptide SC17-2 has multiple functions of skin wound repair, improvement of skin antioxidant activity and promotion of skin angiogenesis, thereby achieving more excellent skin repair function.

[0018] The amino acid sequence shown in SEQ ID NO: 1 has a length of 17 amino acids and has two cysteines, and can form a cyclic peptide through a disulfide bond, thereby increasing the stability of the polypeptide. Compared with the length of the peptide chain of the known skin repair polypeptide, the length of the repair polypeptide SC17-2 is relatively shorter, the length is moderate, and the production cost is lower. Meanwhile, the proportion of hydrophobic amino acids in the repair polypeptide SC17-2 is 58.82%, which can balance the uniform dispersion characteristics in aqueous and lipid substances. In addition, the isoelectric point of the repair polypeptide SC17-2 is 8.64, which can maintain good stability in an acidic solvent, is conducive to the simplification of the preparation process, and is convenient for the preparation of more dosage forms of products. It can be seen that, based on the above sequence characteristics and physicochemical properties, the repair polypeptide SC17-2 has good chemical stability, strong adaptability to different environmental conditions and easy industrialized synthesis. BRIEF DESCRIPTION OF DRAWINGS

[0019] In order to more clearly illustrate the technical solutions in the embodiments of the application or the prior art, the drawings needed in the embodiments will be briefly introduced as follows.

[0020] Figure 1 Toxicity detection results of the repair polypeptide SC17-2 on HaCat cells in Example 2;

[0021] Figure 2 UV damage repair activity detection results of the repair polypeptide SC17-2 in Example 2;

[0022] Figure 3 Promotion of cell migration detection results of the repair polypeptide SC17-2 in Example 2, wherein A and B respectively represent the cell migration percentage of the wound after adding VEGF and the same volume of SC17-2 compared with the control group and the representative image graph in the cell scratch experiment;

[0023] Figure 4 Promotion of skin repair activity detection results of the repair polypeptide SC17-2 in the animal model in Example 2, wherein A, B and C respectively represent the wound healing area images of the control group, VEGF and SC17-2 mice, the area change graph of the representative image of the wound healing area of the mice in 11 days, and the change graph of the wound area of the mice with the change of days;

[0024] Figure 5For the effect of the repair polypeptide SC17-2 on angiogenesis in Example 2, the left image shows the restoration of the intersegmental vessels in zebrafish, and the right image shows the images of the intersegmental vessels under each treatment, wherein the control group is not treated.

[0025] Figure 6 For the effect of the repair polypeptide SC17-2 on the MAPK, TGF-β, and Smad2 / 3 signaling pathways in Example 2. DETAILED DESCRIPTION

[0026] The present application provides a repair polypeptide SC17-2, which comprises the amino acid sequence shown in SEQ ID NO: 1.

[0027] The amino acid sequence shown in SEQ ID NO: 1 of the present application is specifically SFMPLSIPIMCKMLSKC. As an embodiment, the cysteines at positions 11 and 17 in the amino acid sequence shown in SEQ ID NO: 1 form a pair of disulfide bonds to form a cyclic peptide, which can further increase the stability of the repair polypeptide SC17-2. The sequence of the repair polypeptide SC17-2 shown in SEQ ID NO: 1 of the present application is 17 amino acids in length, which is moderate, and the production cost is lower than that of a polypeptide that is too long.

[0028] The isoelectric point of the repair polypeptide SC17-2 of the present application is 8.64, which can maintain good stability in an acidic solvent, and is conducive to process simplification and preparation of more dosage forms during the preparation process, compared with a polypeptide with a lower isoelectric point.

[0029] The proportion of hydrophobic amino acids in the repair polypeptide SC17-2 of the present application is 58.82%, which can be uniformly dispersed in aqueous and lipid substances, ensuring the uniformity of the raw materials of the final product, compared with a polypeptide with a higher hydrophobicity.

[0030] As an embodiment, the synthesis method of the repair polypeptide SC17-2 of the present application is solid-phase synthesis or recombinant expression. The steps of the solid-phase synthesis or recombinant expression of the present application are not particularly limited, and the steps of conventional solid-phase synthesis or recombinant expression in the art can be used; for example, the steps of the recombinant expression can be: constructing an expression plasmid; expressing the expression plasmid through a bacterial or fungal expression system, and purifying the obtained crude polypeptide to obtain the repair polypeptide SC17-2.

[0031] The application also provides application of the repair polypeptide SC17-2 in the preparation of a skin repair product. As an embodiment, the skin repair product comprises a product having one or more of the functions of skin wound repair, improvement of skin antioxidant activity and promotion of skin angiogenesis; as another embodiment, the skin repair product comprises a product having the functions of skin wound repair, improvement of skin antioxidant activity and promotion of skin angiogenesis. As an embodiment, the product comprises a cosmetic and / or a drug; as another embodiment, the drug comprises a drug having one or more of the functions of treatment of a body surface wound, treatment of a body surface burn and treatment of skin ulcer; as another embodiment, the cosmetic comprises a cosmetic having one or more of the functions of reduction of scar generation, acceleration of scar repair and antioxidant function.

[0032] The application also provides a skin repair product, an effective component of the skin repair product comprising the repair polypeptide SC17-2. As an embodiment, the product comprises a cosmetic and / or a drug. As another embodiment, the auxiliary materials in the cosmetic comprise one or more of sorbitol, butanediol, beeswax, mineral fat, tea tree oil, elastin, active peptide, herbal plant extract, cell active component and vitamin.

[0033] In order to further illustrate the application, the technical solutions provided by the application are described in detail below in combination with the drawings and examples, but they should not be understood as limiting the protection scope of the application.

[0034] Example 1

[0035] The primary structure of the amino acid sequence of the repair polypeptide SC17-2 is SFMPLSIPIMCKMLSKC (SEQ ID NO: 1), which is a ring-shaped small peptide, and the amino acids at the 11th and 17th positions in the sequence are connected by a pair of disulfide bonds.

[0036] 2. The preparation method of the repair polypeptide SC17-2 is as follows:

[0037] According to the designed amino acid sequence, a crude polypeptide is synthesized by a solid-phase synthesis method, and the 11th and 17th cysteines are connected to form a pair of disulfide bonds, and the connection condition is that the crude polypeptide is reacted in hydrogen peroxide for 15 min;

[0038] The crude polypeptide is desalted and purified by HPLC reverse-phase column chromatography, and the purity is identified until the purity of the polypeptide is not less than 95%;

[0039] The HPLC purification and identification method is as follows: 0.1 mg of the sample to be tested is dissolved in 1 mL of ultrapure water containing 0.1% trifluoroacetic acid, and if there are insoluble impurities, the solution is filtered through a 0.45 μm filter; the mobile phase A is a water solution containing 0.1% trifluoroacetic acid, and the mobile phase B is a solution of acetonitrile containing 0.1% trifluoroacetic acid; after the baseline is stable, the sample is loaded, and the loading amount is 50 μL; the chromatographic column is a silica gel alkyl-bonded phase C18 column (4.6 mm x 300 mm, with a particle size of 5 μm and a pore size of 100 A); a binary mobile phase gradient elution system is used for gradient elution, i.e. the content of the mobile phase B in the eluent is increased from 0% to 80% in a linear relationship within 30 min, the flow rate is 1 mL / min, the detection wavelength is 215 nm, and the determination is performed at 25°C.

[0040] 3. Detection of the physicochemical properties of the repair polypeptide SC17-2

[0041] 1) The molecular weight of the repair polypeptide SC17-2 is determined to be 1925.95 Da by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF); the detection method is as follows: the purified repair polypeptide SC17-2 is dissolved in deionized water to prepare a 1 μmol / mL solution, 10 μL of the solution is mixed with an equal volume of saturated matrix solution (α-cyano-4-hydroxycinnamic acid is dissolved in a 50% acetonitrile solution containing 0.1% trifluoroacetic acid to prepare a saturated solution, which is centrifuged and the supernatant is taken), and then the mixture is measured.

[0042] 2) The isoelectric point of the purified repair polypeptide SC17-2 is determined to be 8.64 by isoelectric focusing electrophoresis, and the amino acid sequence structure of the purified polypeptide is determined to be Ser-Phe-Met-Pro-Leu-Ser-Ile-Pro-Ile-Met-Cys-Lys-Met-Leu-Ser-Lys-Cys (SFMPLSIPI MCKMLSKC) by an automatic amino acid sequencer after reducing disulfide bonds, and the correctness of the amino acid sequence is determined.

[0043] Example 2

[0044] Determination of the skin repair function of the repair polypeptide in Example 1

[0045] (I) Cytotoxicity determination experiment

[0046] The toxicity of the repair peptide SC17-2 in Example 1 to human immortalized keratinocytes (HaCat) was detected using the CCK8 assay. Human immortalized keratinocytes (HaCat) were purchased from the Kunming Cell Bank of the Chinese Academy of Sciences. Adult immortalized keratinocytes (HaCat) were cultured in DMEM / F12 medium containing 15% fetal bovine serum and double antibiotics (100 U / mL each of penicillin and streptomycin). After confluence, the cells were digested with 0.25% trypsin, washed twice with the above-mentioned medium, resuspended, and counted. 100 μL of the cell suspension was added to a 96-well cell culture plate to achieve a cell count of 10n per well. 5 indivual.

[0047] Eight experimental groups were set up: 20 μL of SC17-2 repair peptide solution at concentrations of 100.00 μg / mL, 50.00 μg / mL, 25.00 μg / mL, 12.50 μg / mL, 6.25 μg / mL, 3.13 μg / mL, 1.56 μg / mL, and 0.78 μg / mL were added to cell culture plates, respectively. The control group was added with the same volume of sterile ultrapure water, and the positive control group was added with vascular endothelial cell factor (VEGF) at a concentration of 20 ng / mL. All eight experimental groups, the control group, and the positive control group were incubated at 37°C in a 5% CO2 incubator for 24 h. After incubation, 10 μL of CCK8 solution was added to each well of a 96-well cell culture plate, and the cells were incubated for another 2–4 h. The absorbance was measured using a microplate reader at a wavelength of 450 nm. The average of three biological replicates from each treatment group was then divided by the average of three biological replicates from the control group, with the control group representing 100%. The results are as follows Figure 1 As shown, "*" and "**" indicate significant differences, P < 0.05 and P < 0.01, respectively.

[0048] Depend on Figure 1 It can be concluded that SC17-2, like VEGF, can promote the migration of HaCaT cells.

[0049] (II) Its role in promoting the repair of oxidative stress damage

[0050] HaCaT cells were used at a rate of 1×10 4Cells were seeded per well in 24-well plates and incubated for 24 h to ensure uniformity and quantity of cells per well. Before UV irradiation, cells were washed with phosphate-buffered saline (PBS) and covered with 300 mL of PBS. The blank control group was wrapped with aluminum foil to eliminate the influence of UV irradiation, and then irradiated with 5 J / cm. Immediately after irradiation, the PBS was replaced with culture medium and repair peptide SC17-2 was added to a final concentration of 20 μg / mL and 5 μg / mL, respectively, and incubated for 24 h. Then, 10 μL of CCK-8 was added to each well and incubated for 2 h. The absorbance of each well was measured at 450 nm. The average of three biological replicates of the same treatment group was then divided by the average of three biological replicates of the control group, with the control group as 100%.

[0051] The results are as follows Figure 2 As shown in the figure, "**" and "***" indicate significant differences (P < 0.01 and P < 0.001, respectively). It is evident that the repair peptide SC17-2 exhibits significant cellular UV damage repair activity at a concentration of 20 μg / mL. The above experiment demonstrates that the repair peptide SC17-2 can repair the cell viability of HaCaT cells after UV irradiation, thereby alleviating UV damage.

[0052] (III) Repairing the cell migration-promoting activity of peptide SC17-2.

[0053] The cell scratch assay was used for determination. HaCat cells in the logarithmic growth phase were digested with 0.25% trypsin, and a cell suspension was prepared using culture medium containing 10% fetal bovine serum. The suspension was then diluted at a concentration of 1×10⁻⁶ cells / mL. 6 Cells were seeded at a density of 1 cell / well in 6-well plates and incubated at 37°C in a 5% CO2 incubator until the cells completely filled the wells. The culture medium was then aspirated, and the cells were washed once with PBS. Using a sterile pipette tip, a line was drawn perpendicularly from top to bottom along the center of each well, applying as much pressure as possible to ensure a consistent width. The culture medium was carefully washed away, and the cells were rinsed several times with PBS to remove any cell clumps caused by the scratch, ensuring clean scratch edges. After carefully aspirating the PBS, serum-free fresh culture medium and an appropriate concentration of sample were added, and the cells were photographed under a microscope. The cells were then incubated in a cell culture incubator. During the incubation period, the cells were observed and photographed every 6 hours. To ensure that the same field of view was selected for each photograph, the bottom of each well was marked with a marker before seeding. The obtained image data were analyzed and processed using Image Pro Plus 6.0. After evenly selecting 30 points on each side of the scratch edge, the midline was taken to represent the scratch edge. The scratch spacing was measured, and the scratch repair rate was calculated using the following formula: Scratch repair rate = (0h scratch width - 16h scratch width) / 0h scratch width. The experiment was repeated three times.

[0054] The effect of the repair peptide SC17-2 at concentrations of 20 μg / mL and 5 μg / mL on the migration activity of HaCat cells was detected using the cell scratch assay. The results are as follows: Figure 3 As shown in the figure, "**" indicates a significant difference (P < 0.01). It is evident that SC17-2 showed a significant difference compared to the control group after 16 hours of treatment, indicating that SC17-2 promotes keratinocyte migration.

[0055] (IV) Experiment on the wound healing effect of repair peptide SC17-2 on mouse skin injury model

[0056] Randomly selected Kunming mice (6-8 weeks old, approximately 20g) were anesthetized by intraperitoneal injection of 1% sodium pentobarbital solution (100μL / 20g). The fur on their backs was trimmed as much as possible. After alcohol disinfection, an 8mm diameter incision was made on their backs using a punch. Physiological saline served as the blank control group; mouse-derived VEGF-A (mVEGF-A, 50μg / mL) served as the positive control; and the repair peptide SC17-2 (20μg / mL) served as the experimental group. Both VEGF-A and SC17-2 were prepared using physiological saline solution. The medication was administered once daily, 20μL each time, with the reagents from both the experimental and control groups applied to the surface of the wound. Wound changes were photographed every two days until the treated wound completely healed and scabs fell off. A ruler was used to measure the wound during photography. The results are as follows: Figure 4 As shown, in Figure 4 VEGF represents the positive control.

[0057] Depend on Figure 4 It can be concluded that, during the 11-day wound observation period, the SC17-2 repair peptide at a concentration of 20 μg / ml showed significantly better wound healing effects than the 50 μg / ml mouse-derived VEGF-A, demonstrating a significant improvement in wound repair capacity. Therefore, the SC17-2 repair peptide can be applied to the preparation of drugs for treating external wounds, burns, and skin ulcers, reducing scar formation, and accelerating scar repair.

[0058] (V) Effects of skin-repairing peptides on angiogenesis in zebrafish

[0059] First, healthy zebrafish embryos developed to 24 hours post-fertilization were selected and placed in clean water. They were cultured at 28.5℃ under alternating 14-hour light and 10-hour dark conditions until reaching 24 hpf. The 24 hpf embryos were then treated with 300 ng / mL of VEGFR tyrosine kinase inhibitor II (VRI) for 3 hours in a temperature-controlled environment to ensure uniform VRI distribution. After treatment, the embryos were carefully transferred to 24-well plates, 12 per well. After 24 hours of incubation, the repair peptide SC17-2 was slowly added to the 24-well plates in gradients of 5 μg / mL, 10 μg / mL, and 20 μg / mL, with gentle shaking to mix after each addition. The embryo morphological changes were then observed using a Leica fluorescence microscope, with microscope parameters adjusted to clearly visualize the vascular structure. The results are shown below. Figure 5 As shown ( Figure 5 The scale bar in the middle right figure is 500 μm. The results showed that the repair peptide SC17-2 at a concentration of 20 μg / mL significantly promoted angiogenesis in zebrafish compared with the control.

[0060] (VI) Effects of Repair Peptide SC17-2 on MAPK Signaling Pathway

[0061] HaCat cells were cultured in DMEM / F12 medium containing 10% fetal bovine serum to the logarithmic growth phase, and after trypsin digestion, were discharged at a cell density of 1×10⁶ cells / year. 6 Cells were seeded at a density of 10 cells / mL in 6-well cell culture plates. The plates were incubated at 37°C in a 5% CO2 incubator for 4-6 hours. After complete cell adhesion, the cells were washed 2-3 times with PBS and then starved for 16 hours with serum-free medium. 20 μL of different concentrations (10 μg / mL or 20 μg / mL) of sample were added to each well. A blank control was prepared with 20 μL of sterile Milli-Q water, and a positive control was prepared with 20 μL of VEGF. The samples were incubated for 16 hours.

[0062] Discard the culture medium and wash the cells twice with 1 mL of pre-chilled PBS. Add 250 μL of RIPA cell lysis buffer [50 mM Tris-HCl (pH 7.4), 1% Nonidet P-40, 0.25% sodium deoxycholate, 150 mM NaCl, 1 mM EDTA, 1 mM PMSF, 1 mM NaF, 1 mM Na3VO4, and 1 μg / mL each of aprotinin, leupeptin, and pepstatin] to each well. Lyse on ice for 30 min, centrifuge at 12,000 g for 20 min at 4 °C, carefully aspirate the supernatant, and aliquot it into new eppendorf tubes. Determine the protein concentration using the Bradford method with 2 μL of the supernatant, and aliquot the remainder into specific volumes and freeze rapidly at -20 °C.

[0063] Equal amount of cell lysate, 40 microgram of protein, was mixed with 6x SDS sample buffer, heated at 95-100°C for 5 min, and then loaded into each lane after cooling. Constant voltage electrophoresis: 90V for concentrated gel and 120V for separation gel. After electrophoresis, the gel was transferred to PVDF membrane by wet transfer method. After transfer, the membrane was washed with TBS for 5 min, and then blocked with 5 mL blocking solution (1x TBS, 0.1% Tween-20, 5% skim milk) for 1 h at room temperature. The membrane was washed with TBST for 5 min for three times. Then, the membrane was reacted with pre-diluted primary antibody (CST 4370T Phospho-p44 / 42 MAPK (Erkl / 2) (Thr202 / Tyr204) (D13.14.4E) XP, CST 4695T p44 / 42 MAPK (Erkl / 2) (137F5) purchased from Cell Signaling, USA) at 4°C overnight. The membrane was washed with TBST for 5 min for three times. Then, the membrane was reacted with pre-diluted secondary antibody (Goat Anti-Rabbit IgG (H+L) HRP purchased from Affinity Biosciences, OH. USA) for 1 h with gentle shaking. The membrane was washed with TBST for 5 min for three times. The ECL reaction substrate was prepared according to the manufacturer's instructions, and the membrane was exposed to color development in the dark room. The results are shown in Figure 6

[0064] Figure 6 The results in Table 1 show that the repair polypeptide SC17-2 activates the Smad2 / 3 pathway in a concentration-dependent manner. The increase in the p-MAPK / MAPK ratio in HaCat cells treated with the repair polypeptide SC17-2 may indicate that the MAPK pathway is activated, and the activated MAPK pathway may promote cell activity during wound healing. TGF-β plays a key role in the formation of granulation tissue and scar formation by promoting fibroblast proliferation and collagen synthesis, thereby promoting wound filling and scar tissue formation. Smad protein is a downstream molecule of the TGF-β signaling pathway. The increase in the phosphorylation level of Smad protein in HaCat cells after treatment with the repair polypeptide SC17-2 and VEGF may reflect the increase in TGF-β signal. The increase in TGF-β protein expression may be related to the fibrosis stage of wound healing.

[0065] From the above results, it can be concluded that the repair polypeptide SC17-2 can promote cell migration, promote the recruitment of macrophages and fibroblasts, promote angiogenesis, and act through the MAPK signaling pathway. Animal models show that the SC17-2 polypeptide has good wound repair function and no hemolytic activity and cytotoxicity.

[0066] ​The repair polypeptide SC17-2 described in the application consists of 17 amino acids, is a cyclic peptide with one pair of disulfide bonds, and has a mature synthesis process, low synthesis cost and high in-vivo stability. Therefore, the repair polypeptide SC17-2 can effectively promote skin repair, and is applied to the fields of preparing drugs for treating body surface wounds, burns and skin ulcers, reducing scar generation, accelerating scar repair and the like, and skin repair and regeneration cosmetic and skin care products.

[0067] Although the above embodiment has made a detailed description of the present application, it is only a part of the embodiments of the present application, but not all the embodiments, and other embodiments can be obtained according to the present embodiment without creativity, which all belong to the protection scope of the present application.

Claims

1. A repair polypeptide SC17-2, characterized in that, The amino acid sequence of the repair polypeptide SC17-2 is shown in SEQ ID NO:1; The two cysteine ​​residues in the amino acid sequence shown in SEQ ID NO:1 are linked together by disulfide bonds to form a cyclic peptide.

2. The application of the repair polypeptide SC17-2 according to claim 1 in the preparation of skin repair products.

3. The application according to claim 2, characterized in that, The skin repair product is a product that has one or more functions, such as repairing skin trauma, improving skin antioxidant activity, and promoting skin angiogenesis.

4. The application according to claim 2, characterized in that, The products mentioned are cosmetics and / or pharmaceuticals.

5. The application according to claim 4, characterized in that, The drug is a drug that has one or more functions of treating external trauma, treating external burns, and treating skin ulcers.

6. The application according to claim 4, characterized in that, The cosmetic product is a cosmetic product that has one or more functions such as reducing scar formation, accelerating scar repair, and anti-oxidation.

7. A skin repair product, characterized in that, The active ingredient in the skin repair product includes the repair polypeptide SC17-2 as described in claim 1.

8. The skin repair product according to claim 7, characterized in that, The products mentioned are cosmetics and / or pharmaceuticals.

9. The skin repair product according to claim 8, characterized in that, The excipients in the cosmetics include one or more of the following: sorbitol, butylene glycol, beeswax, mineral oil, tea tree oil, elastin, active peptides, herbal extracts, cell-active ingredients, and vitamins.

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