A pentapeptide and its applications

Abstract

This invention provides a pentapeptide and its applications. The pentapeptide with the amino acid sequence shown in SEQ ID NO:1 exhibits excellent melanin-inhibiting activity, antioxidant activity, and tyrosinase-inhibiting activity. It is suitable not only for preparing melanin inhibitors, antioxidant products, and tyrosinase inhibitors, but also for preparing products with whitening effects, such as whitening foods, cosmetics, or pharmaceuticals.

Description

Technical Field

[0001] This invention belongs to the field of biopeptide technology. More specifically, it relates to a pentapeptide and its applications. Background Technology

[0002] Melanin is an amino acid derivative found in the cells of the basal layer of the skin and is secreted by melanocytes. The amount of melanin determines the skin color; when melanocytes increase their ability to synthesize melanin, the skin color will darken accordingly, resulting in dullness, yellowing, or darkening of the skin.

[0003] Peptides are compounds formed by multiple α-amino acids linked together by peptide chains. They possess a variety of biological activities and are safe with no side effects. However, there are still relatively few reported peptides with melanin-inhibiting activity. Summary of the Invention

[0004] To address the shortcomings of existing technologies, this invention aims to provide a pentapeptide with an amino acid sequence as shown in SEQ ID NO:1, thereby enriching the polypeptide resource library with melanin-inhibiting activity and providing more raw material options for melanin inhibitors.

[0005] The primary objective of this invention is to provide a pentapeptide.

[0006] Another object of the present invention is to provide the application of the above-mentioned pentapeptide or related biomaterials in the preparation of melanin inhibitors.

[0007] Another object of the present invention is to provide the application of the above-mentioned pentapeptide or related biomaterials in the preparation of antioxidant products.

[0008] Another object of the present invention is to provide the application of the above-mentioned pentapeptide or related biomaterials in the preparation of tyrosinase inhibitors.

[0009] Another object of the present invention is to provide the application of the above-mentioned pentapeptide or related biomaterials in the preparation of skin whitening products.

[0010] Another object of the present invention is to provide a product.

[0011] The above-mentioned objective of this invention is achieved through the following technical solution:

[0012] This invention provides a pentapeptide with the amino acid sequence shown in SEQ ID NO:1. SEQ ID NO:1: VLSLY.

[0013] The pentapeptide of the present invention, with an amino acid sequence as shown in SEQ ID NO:1, has excellent melanin inhibitory activity, antioxidant activity, and tyrosinase inhibitory activity. It is not only suitable for the preparation of melanin inhibitors, antioxidant products, and tyrosinase inhibitors, but also suitable for the preparation of products with whitening effects, such as foods, cosmetics, or pharmaceuticals with whitening effects.

[0014] Therefore, the present invention also provides the use of the above-mentioned pentapeptide or related biomaterials in any of the following:

[0015] (1) Application in the preparation of melanin inhibitors;

[0016] (2) Application in the preparation of antioxidant products;

[0017] (3) Application in the preparation of tyrosinase inhibitors;

[0018] (4) Application in the preparation of skin whitening products;

[0019] The relevant biological material is a nucleic acid molecule capable of expressing the pentapeptide, or a host cell, vector, transposon, expression cassette, or recombinant DNA containing the nucleic acid molecule.

[0020] Based on this, the present invention provides a product comprising the above-mentioned pentapeptide and / or its related biomaterials.

[0021] Preferably, the relevant biological material is a nucleic acid molecule capable of expressing the pentapeptide, or a host cell, vector, transposon, expression cassette, or recombinant DNA containing the nucleic acid molecule.

[0022] Preferably, the product is a cosmetic or a pharmaceutical.

[0023] More preferably, it also contains excipients acceptable for use in cosmetics or pharmaceuticals.

[0024] The present invention has the following beneficial effects:

[0025] The pentapeptide of the present invention, with an amino acid sequence as shown in SEQ ID NO:1, has excellent melanin inhibitory activity, antioxidant activity, and tyrosinase inhibitory activity. It is not only suitable for the preparation of melanin inhibitors, antioxidant products, and tyrosinase inhibitors, but also suitable for the preparation of products with whitening effects, such as foods, cosmetics, or pharmaceuticals with whitening effects. Attached Figure Description

[0026] Figure 1 This is the mass spectrometry identification result of the pentapeptide.

[0027] Figure 2 The results show the purity of the pentapeptide.

[0028] Figure 3This is a Lineweaver-Burk diagram.

[0029] Figure 4 This is a graph showing the relationship between the slope of the straight line and the concentration of the pentapeptide.

[0030] Figure 5 These are the safety test results for the pentapeptide.

[0031] Figure 6 The graph shows the results of tyrosinase activity assay after pentapeptide treatment.

[0032] Figure 7 The graph shows the results of the determination of the relative ROS activity after pentapeptide treatment.

[0033] Figure 8 The graph shows the results of SOD activity determination after pentapeptide treatment.

[0034] Figure 9 The graph shows the results of melanin content determination after pentapeptide treatment. Detailed Implementation

[0035] The present invention will be further described below with reference to the accompanying drawings and specific embodiments, but the embodiments do not limit the present invention in any way. Unless otherwise specified, the reagents, methods and equipment used in the present invention are conventional reagents, methods and equipment in this technical field.

[0036] Unless otherwise specified, all reagents and materials used in the following examples are commercially available.

[0037] All experiments in this embodiment of the invention consisted of three parallel groups, and the final data were expressed as mean ± standard deviation. Statistical graphs were generated using Origin 2019 software, and the experimental results were analyzed using IBM SPSS Statistics 26 software with one-way ANOVA of the group means. P < 0.05 indicated that the difference was statistically significant.

[0038] Example 1: Synthesis of Pentapeptides

[0039] The pentapeptide was synthesized with the assistance of Shanghai Aminolink Biotechnology Co., Ltd., and its amino acid sequence is shown in SEQ ID NO:1: VLSLY.

[0040] Example 2 Identification of pentapeptides

[0041] (1) The molecular weight of the pentapeptide was identified by ESI-MS mass spectrometry.

[0042] The identification conditions for ESI-MS mass spectrometry are as follows:

[0043] Mobile phase A: Water (containing 0.1% ( v / v (trifluoroacetic acid);

[0044] Mobile phase B: Acetonitrile (containing 0.1% ( v / v (trifluoroacetic acid);

[0045] Flow rate: 2 mL / min;

[0046] Running time: 4 min;

[0047] Operating mode: Positive ion mode;

[0048] Scan range: 0–2000 Da.

[0049] The results of mass spectrometry identification are as follows Figure 1 As shown, the molecular ion peak m / z of the pentapeptide in this embodiment is 594.64, carrying one charge, which is consistent with its theoretical molecular weight value, indicating that the pentapeptide synthesized in this embodiment is the pentapeptide with the amino acid sequence shown in SEQ ID NO:1.

[0050] (2) The purity of the pentapeptide was determined by high performance liquid chromatography.

[0051] The identification conditions for high-performance liquid chromatography (HPLC) are as follows:

[0052] Column: Inertsil ODS-SP (4.6×250 mm);

[0053] Mobile phase A: Water (containing 0.1% ( v / v (trifluoroacetic acid);

[0054] Mobile phase B: Acetonitrile (containing 0.1% ( v / v (trifluoroacetic acid);

[0055] Elution gradient: 0→25 min, 99% ( v / v ) → 50% v / v A;

[0056] Flow rate: 1 mL / min;

[0057] Detection wavelength: 220 nm;

[0058] Sample loading volume: 30 μL.

[0059] The results of purity testing are as follows Figure 2 As shown, the main peak in the pentapeptide of this embodiment accounts for the majority, with only a few impurity peaks appearing, and the purity is as high as 97.31%.

[0060] Example 3: In vitro inhibitory effect of pentapeptides on tyrosinase activity

[0061] (1) Reagent preparation

[0062] Tyrosinase solution: Dissolve tyrosinase in phosphate buffer at pH 6.8 to achieve a final concentration of 500 U / mL.

[0063] L-Tyrosine Solution: Dissolve L-tyrosine in phosphate buffer solution at pH 6.8 to achieve a final concentration of 0.5 mg / mL.

[0064] Sample solutions: The pentapeptide obtained in Example 1 was dissolved in phosphate buffer at pH 6.8 to achieve final concentrations of 0.2, 0.4, 0.6, 0.8, and 1.0 mg / mL.

[0065] (2) Test method

[0066] Solvent blank wells: Add 110 μL of PBS solvent to a 96-well plate, incubate at 37 °C for 15 min, then add 20 μL of tyrosinase solution to each well, and incubate at 37 °C for another 10 min. Measure the absorbance value A1 at 475 nm.

[0067] Solvent background wells: Add 40 μL of L-tyrosine solution and 70 μL of PBS solvent to a 96-well plate, incubate at 37 °C for 15 min, then add 20 μL of tyrosinase solution to each well, and incubate at 37 °C for another 10 min. Measure the absorbance value A2 at 475 nm.

[0068] Sample background wells: Add 40 μL of sample solution and 70 μL of PBS solvent to a 96-well plate, incubate at 37 °C for 15 min, then add 20 μL of tyrosinase solution to each well, and incubate at 37 °C for another 10 min. Measure the absorbance value A3 at 475 nm.

[0069] Sample reaction wells: Add 40 μL of L-tyrosine solution, 40 μL of sample solution and 30 μL of PBS solvent to a 96-well plate, incubate at 37 ℃ for 15 min, then add 20 μL of tyrosinase solution to each well, and incubate at 37 ℃ for another 10 min. Measure the absorbance value A4 at 475 nm.

[0070] The tyrosinase inhibition rate is calculated using the formula "Tyrosinase inhibition rate (%) = [1 - (A4 - A3) / (A2 - A1)] × 100%".

[0071] (3) Test results

[0072] The results showed that the IC50 of the pentapeptide was... 50 The value was 1.51 ± 0.10 mM, indicating that the pentapeptide of the present invention has a significant inhibitory effect on tyrosinase activity and is suitable for the preparation of skin whitening products.

[0073] Example 4: Types of inhibition of tyrosinase activity by pentapeptides

[0074] (1) Reagent preparation

[0075] Tyrosinase solution: Dissolve tyrosinase in phosphate buffer at pH 6.8 to achieve a final concentration of 500 U / mL.

[0076] L-Tyrosine Solution: L-tyrosine was dissolved in phosphate buffer solution at pH 6.8 to achieve final concentrations of 0.75, 1.00, 1.25, 2.00, and 3.00 mM.

[0077] Sample solutions: The pentapeptide obtained in Example 1 was dissolved in phosphate buffer at pH 6.8 to achieve final concentrations of 0, 0.25, 0.50, and 1.00 mM.

[0078] (2) Test method

[0079] In a 96-well plate, add 40 μL of L-tyrosine solution, 40 μL of sample solution, and 30 μL of phosphate buffer (pH=6.8). Incubate at 37 ℃ for 10 min, then add 20 μL of tyrosinase solution, and incubate again at 37 ℃ for 10 min. Measure the absorbance at 475 nm at 0 and 10 min of incubation. Calculate the absorbance using the formula: "Reaction rate (%) = (A... 10 -A0) / 10]×100%""A 10 The absorbance at min 10 and A0 at min 0 were used to calculate the reaction rate of the pentapeptide with tyrosinase. A Lineweaver-Burk plot was then plotted based on the calculation results, as shown below. Figure 3 As shown, and according to Figure 3 The relationship between the slope of each straight line and the concentration of the pentapeptide is plotted. Figure 4 .

[0080] (3) Test results

[0081] Depend on Figure 3 It can be seen that the maximum reaction rate (Vmax, the reciprocal of the y-intercept) and the Michaelis constant (Km, the reciprocal of the x-intercept) in the coordinate graph change with the concentration of the pentapeptide, and the four straight lines all intersect in the second quadrant of the coordinate axis, indicating that the inhibition of tyrosinase by the pentapeptide is a mixed result of competitive and non-competitive inhibition, that is: the inhibition type of tyrosinase by the pentapeptide of the present invention is a mixed inhibition.

[0082] Depend on Figure 4 As can be seen, the slope of each straight line in the Lineweaver-Burk diagram is linearly related to the concentration of the pentapeptide, indicating that the pentapeptide of the present invention can bind to a single site on tyrosinase.

[0083] Example 5 Safety of Pentapeptides

[0084] (1) Reagent preparation

[0085] Kojic acid solution: In a clean bench, dissolve kojic acid in a solution containing 10% ( v / v ) Fetal bovine serum + 1% ( v / v The penicillin-streptomycin bispecific antibody was prepared in DMEM medium to a final concentration of 300 μM, and then sterilized using a 0.22 μm syringe filter.

[0086] Sample solution: In a clean bench, the pentapeptide obtained in Example 1 was dissolved in a solution containing 10% ( v / v ) Fetal bovine serum + 1% ( v / v The penicillin-streptomycin bispecific antibody was prepared in DMEM medium to achieve final concentrations of 100, 200, and 400 μM, and then sterilized using a 0.22 μm needle filter.

[0087] (2) Test method

[0088] Blank well: Add 100 μL of a solution containing 10% ( ) to a 96-well plate. v / v ) Fetal bovine serum + 1% ( v / v The penicillin-streptomycin bispecific antibody was cultured in DMEM medium at 37 ℃ for 24 h, and the supernatant was discarded. Then, 100 μL of a solution containing 10% (…) was added. v / v ) Fetal bovine serum + 1% ( v / v The penicillin-streptomycin antibiotic was cultured in DMEM medium at 37 ℃ for 24 h, the supernatant was discarded, and 110 μL of 10% ( ) penicillin-streptomycin antibiotic solution was added under light-protected conditions. v / v After incubating the CCK-8 solution in a 37 °C incubator for 30 min, the absorbance value A at 450 nm was measured for each well. 空 .

[0089] Control wells: Logarithmic growth phase melanoma cells (B16F10) were seeded at a density of 3000 cells / well in 96-well plates and cultured at 37 ℃ for 24 h. The supernatant was discarded, and 100 μL of a solution containing 10% ( v / v ) Fetal bovine serum + 1% ( v / v The penicillin-streptomycin antibiotic was cultured in DMEM medium at 37 ℃ for 24 h, the supernatant was discarded, and 110 μL of 10% ( ) penicillin-streptomycin antibiotic solution was added under light-protected conditions. v / v After incubating the CCK-8 solution in a 37 ℃ incubator for 30 min, the absorbance value A0 of each well at 450 nm was measured.

[0090] Sample wells for drug addition: Logarithmic growth phase melanoma cells (B16F10) were seeded at a density of 3000 cells / well in 96-well plates. After acclimatization culture at 37 ℃ for 24 h, the supernatant was discarded. 100 μL of sample solution / kojic acid solution was added to each well, and the cells were cultured at 37 ℃ for 24 h. After discarding the supernatant, 110 μL of 10% ( ) kojic acid solution was added under light-protected conditions. v / v After incubating the CCK-8 solution in a 37 °C incubator for 30 min, the absorbance value A at 450 nm was measured for each well. 样 .

[0091] According to the formula "Cell viability (%) = [(A)", 样 -A 空 ) / (A0-A 空 The cell viability after treatment with the sample solution / kojic acid solution was calculated by multiplying the percentage by 100% to evaluate the safety of the pentapeptide.

[0092] (3) Test results

[0093] The results are as follows Figure 5 As shown, compared with the blank wells, there was no significant difference in the activity of B16F10 cells after treatment with 100–400 μM pentapeptide. This indicates that the pentapeptide of the present invention has high safety.

[0094] Example 6: Inhibitory effect of pentapeptides on intracellular tyrosinase activity

[0095] (1) Reagent preparation

[0096] Sample solution: Dissolve the pentapeptide obtained in Example 1 in a solution containing 10% ( v / v ) Fetal bovine serum + 1% ( v / v In DMEM medium containing penicillin and streptomycin, the final concentrations were 100 and 200 μM, respectively.

[0097] (2) Test method

[0098] Blank hole (A) 空 ): Take melanoma cells (B16F10) in logarithmic growth phase at 5 × 10⁻⁶ 5 Cells were seeded at a density of 100 cells / well in 6-well plates and cultured at 37 °C for 24 h. The supernatant was discarded, and the cells were washed twice with PBS solution (pH=7.4). 2 mL of PBS containing 10% (…) was added to each well. v / v ) Fetal bovine serum + 1% ( v / vCells were cultured in DMEM medium containing penicillin and streptomycin at 37 °C for 24 h. The supernatant was discarded, and the cells were washed twice with PBS solution (pH 7.4) to remove non-adherent cells. Then, 400 μL of lysis buffer (PMSF:RIPA volume ratio 1:100) was added, and lysis was performed at 4 °C for 30 min. The supernatant was collected by centrifugation, and the protein concentration was determined using a BCA kit and normalized. 50 μL of the protein solution was then mixed with 50 μL of PBS and 50 μL of L-DOPA (10 mM), and reacted at 37 °C for 30 min. The absorbance (A) was measured at 475 nm. 空 .

[0099] Sample wells for drug administration: Melanoma cells (B16F10) in logarithmic growth phase were collected at 5 × 10⁻⁶. 5 Cells were seeded at a density of 100 cells / well in 6-well plates and cultured at 37 °C for 24 h. After acclimatization, the supernatant was discarded, and the cells were washed twice with PBS (pH 7.4). 2 mL of sample solution was added to each well, and the cells were cultured at 37 °C for 24 h. The supernatant was discarded, and the cells were washed twice with PBS (pH 7.4) to remove non-adherent cells. 400 μL of lysis buffer (PMSF:RIPA, volume ratio 1:100) was added to each well, and lysis was performed at 4 °C for 30 min. The supernatant was collected by centrifugation, and the protein concentration was determined using a BCA kit and normalized. 50 μL of the protein solution was mixed with 50 μL of PBS and 50 μL of L-DOPA (10 mM), and reacted at 37 °C for 30 min. The absorbance (A) was measured at 475 nm. 样 .

[0100] According to the formula "Tyrosinase activity (%) = A 样 / A 空 The tyrosinase activity after the sample solution was reacted was calculated using the formula ×100%.

[0101] (3) Test results

[0102] The results are as follows Figure 6 As shown, compared with the blank well, the tyrosinase activity of B16F10 cells was significantly reduced after treatment with 100-200 μM pentapeptide, indicating that the pentapeptide of the present invention can significantly inhibit the activity of tyrosinase and is suitable for the preparation of whitening products.

[0103] Example 7 Antioxidant effect of pentapeptides

[0104] (1) Reagent preparation

[0105] Sample solution: In a clean bench, the pentapeptide obtained in Example 1 was dissolved in a solution containing 10% ( v / v ) Fetal bovine serum + 1% ( v / v The penicillin-streptomycin bispecific antibody was prepared in DMEM medium to achieve final concentrations of 0, 100, and 200 μM, and then sterilized using a 0.22 μm syringe filter.

[0106] (2) Test method

[0107] ① Methods for determining ROS activity

[0108] Blank wells: Logarithmic growth phase melanoma cells (B16F10) were seeded at a density of 3000 cells / well in 96-well plates and cultured at 37 ℃ for 24 h. The supernatant was discarded, and the cells were washed twice with PBS solution (pH=7.4). 100 μL of PBS containing 10% (…) was added to each well. v / v ) Fetal bovine serum + 1% ( v / v After incubating penicillin-streptomycin antibiotics in DMEM medium at 37 ℃ and 5% CO2 for 24 h, the medium was discarded. 100 μL of DCFH-DA diluted to 10 µM in DMEM medium was added, and the mixture was incubated at 37 ℃ for 30 min. The supernatant was discarded, and the mixture was washed with PBS solution (pH=7.4). The absorbance was measured using a microplate reader. 空 (Excitation wavelength set to 488 nm, emission wavelength set to 525 nm).

[0109] Sample wells for drug administration: Logarithmic growth phase melanoma cells (B16F10) were seeded at a density of 3000 cells / well in 96-well plates and cultured at 37 ℃ for 24 h. The supernatant was discarded, and the cells were washed twice with PBS (pH=7.4). 100 μL of sample solution was added, and the cells were incubated at 37 ℃ with 5% CO2 for 24 h. The culture medium was discarded, and 100 μL of DCFH-DA diluted to 10 µM with DMEM was added. The cells were incubated at 37 ℃ for 30 min, the supernatant was discarded, and the cells were washed with PBS (pH=7.4). The absorbance was measured using a microplate reader. 样 (Excitation wavelength set to 488 nm, emission wavelength set to 525 nm).

[0110] According to "ROS relative activity (%) = A 样 / A 空 The relative activity of ROS is calculated by multiplying by 100%.

[0111] ②SOD activity assay method

[0112] Melanoma cells (B16F10) in logarithmic growth phase were harvested at a concentration of 5 × 10⁻⁶. 5Cells were seeded at a density of 100 cells / well in 6-well plates and cultured at 37 °C for 24 h. The supernatant was discarded, and the cells were washed twice with PBS (pH 7.4). 2 mL of sample solution was added, and the cells were cultured at 37 °C for another 24 h. The supernatant was discarded, and the cells were washed twice with PBS (pH 7.4) to remove non-adherent cells. Then, 400 μL of lysis buffer (PMSF:RIPA ratio 1:100) was added, and the cells were lysed at 4 °C for 30 min. The supernatant was collected by centrifugation. The SOD activity in the supernatant was determined according to the instructions of the SOD kit from Nanjing Jiancheng Biotechnology Institute.

[0113] (3) Test results

[0114] ROS relative activity results are as follows Figure 7 As shown, the SOD activity results are as follows: Figure 8 As shown, compared with the blank group, after treatment with 100-200 μM pentapeptide, the relative ROS activity of B16F10 cells was significantly reduced and the SOD activity was significantly increased, indicating that the pentapeptide of the present invention has excellent antioxidant activity and is suitable for the preparation of whitening products.

[0115] Example 6: Inhibitory effect of pentapeptides on melanin

[0116] (1) Reagent preparation

[0117] Sample solution: In a clean bench, the pentapeptide obtained in Example 1 was dissolved in a solution containing 10% ( v / v ) Fetal bovine serum + 1% ( v / v The penicillin and streptomycin antibiotics were prepared in DMEM medium to achieve final concentrations of 100 and 200 μM, respectively, and then sterilized using a 0.22 μm needle filter.

[0118] (2) Test method

[0119] Blank wells: Melanoma cells (B16F10) in logarithmic growth phase were harvested at 5 × 10⁻⁶ cells / well. 5 Cells were seeded at a density of 100 cells / well in 6-well plates and cultured at 37 °C for 24 h. The supernatant was discarded, and the cells were washed twice with PBS solution (pH=7.4). 2 mL of PBS containing 10% (…) was added to each well. v / v ) Fetal bovine serum + 1% ( v / v Cells were cultured in DMEM medium containing penicillin and streptomycin at 37 °C for 24 h, then the supernatant was discarded. Cells were washed twice with PBS solution (pH=7.4) to remove non-adherent cells. Cells were then digested with trypsin, and the digestion products were collected and centrifuged at 1500 r / min for 10 min. 1 mL of a solution containing 10% (…) penicillin and streptomycin was added to the centrifuged precipitate. v / vAfter immersion in DMSO in NaOH solution (1 mol / L) at 80 °C for 1 h, the absorbance value A of each well at 450 nm was measured. 空 .

[0120] Sample wells for drug administration: Melanoma cells (B16F10) in logarithmic growth phase were collected at 5 × 10⁻⁶. 5 Cells were seeded at a density of 100 cells / well in 6-well plates and cultured at 37 °C for 24 h. The supernatant was discarded, and the cells were washed twice with PBS (pH=7.4). 2 mL of sample solution was added to each well, and the cells were cultured at 37 °C for 24 h. The supernatant was discarded, and the cells were washed twice with PBS (pH=7.4) to remove non-adherent cells. The cells were then digested with trypsin, and the digestion products were collected and centrifuged at 1500 r / min for 10 min. 1 mL of a solution containing 10% (…) was added to the precipitate. v / v After immersion in DMSO in NaOH solution (1 mol / L) at 80 °C for 1 h, the absorbance value A of each well at 450 nm was measured. 样 .

[0121] According to the formula "Melanin content (%) = A 样 / A 空 The melanin content after the sample solution was treated was calculated using the formula "×100%".

[0122] (3) Test results

[0123] The results are as follows Figure 9 As shown, compared with the blank well, the melanin content of B16F10 cells was significantly reduced after treatment with 100-200 μM pentapeptide, indicating that the pentapeptide of the present invention can significantly inhibit melanin production and is suitable for preparing whitening products.

[0124] The above embodiments are preferred embodiments of the present invention, but the embodiments of the present invention are not limited to the above embodiments. Any changes, modifications, substitutions, combinations, or simplifications made without departing from the spirit and principle of the present invention shall be considered equivalent substitutions and shall be included within the protection scope of the present invention.

Claims

1. A pentapeptide characterized in that, The amino acid sequence is shown as SEQ ID NO:

1.

2. Use of the pentapeptide or related biomaterials thereof according to claim 1 for the preparation of a melanin inhibitor, characterized in that, The related biological material is a nucleic acid molecule capable of encoding the pentapeptide, or a host cell, vector, transposon, expression cassette or recombinant DNA containing the nucleic acid molecule.

3. Use of the pentapeptide or related biomaterials thereof according to claim 1 for the preparation of an antioxidant product, characterized in that, The product is a cosmetic or pharmaceutical product; the related biological material is a nucleic acid molecule capable of encoding the pentapeptide, or a host cell, vector, transposon, expression cassette or recombinant DNA containing the nucleic acid molecule.

4. Use of the pentapeptide of claim 1 or a related biomaterial thereof in the preparation of a whitening product, characterized in that, The product is a cosmetic or pharmaceutical product; the related biological material is a nucleic acid molecule capable of encoding the pentapeptide, or a host cell, vector, transposon, expression cassette or recombinant DNA containing the nucleic acid molecule.

5. A product characterized by, The product is a cosmetic or pharmaceutical product; the related biological material is a nucleic acid molecule capable of encoding the pentapeptide, or a host cell, vector, transposon, expression cassette or recombinant DNA containing the nucleic acid molecule.

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