Pentapeptide and application thereof

Abstract

The invention provides a pentapeptide and application thereof. The pentapeptide with the amino acid sequence shown as SEQ ID NO: 1 has excellent melanin inhibition activity, antioxidant activity and tyrosinase inhibition activity, is not only suitable for preparing melanin inhibitors, antioxidant products and tyrosinase inhibitors, but also suitable for preparing products with the whitening effect, such as food, cosmetics or drugs with the whitening effect.

Description

Technical Field

[0001] The present invention belongs to the technical field of biological peptides and more specifically relates to a pentapeptide and its application. Background Art

[0002] Melanin is an amino acid derivative that exists in the cells of the basal layer of the skin and is secreted by pigment stem cells. The content of melanin determines the color of the skin. When the ability of melanocytes to synthesize melanin increases, the color of the skin will become darker, and the skin will become dull, yellow, or black.

[0003] Peptides are compounds formed by connecting multiple α-amino acids in a peptide chain. They have multiple biological activities and are safe and have no side effects. However, there are still few reports of peptides with melanin inhibitory activity. Summary of the invention

[0004] In view of the deficiencies in the prior art, the present invention aims to provide a pentapeptide having an amino acid sequence as shown in SEQ ID NO: 1, enriching the polypeptide resource library with melanin inhibitory activity and providing more raw material options for melanin inhibitors.

[0005] The primary object of the present invention is to provide a pentapeptide.

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

[0007] Another object of the present invention is to provide the use of the above pentapeptide or its related biological materials in the preparation of antioxidant products.

[0008] Another object of the present invention is to provide the use of the above pentapeptide or its related biological materials in the preparation of tyrosinase inhibitors.

[0009] Another object of the present invention is to provide the use of the above pentapeptide or its related biological materials in the preparation of whitening products

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

[0011] The above-mentioned purpose of the present invention is achieved through the following technical solutions:

[0012] The present invention provides a pentapeptide, the amino acid sequence of which is shown in SEQ ID NO: 1. SEQ ID NO: 1: VLSLY.

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

[0014] Therefore, the present invention also provides the use of the above pentapeptide or its related biological material 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 whitening products;

[0019] Wherein, the related 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 biological materials.

[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 food, cosmetic or medicine.

[0023] More preferably, it also contains excipients acceptable to food, cosmetics or medicines.

[0024] Further preferably, the food is nutritious and healthy food.

[0025] The present invention has the following beneficial effects:

[0026] The pentapeptide of the present invention, whose amino acid sequence is shown in SEQ ID NO: 1, has excellent melanin inhibitory activity, antioxidant activity, and tyrosinase inhibitory activity, and is not only suitable for preparing melanin inhibitors, antioxidant products and tyrosinase inhibitors, but also suitable for preparing products with whitening effects, such as foods, cosmetics or medicines with whitening effects. BRIEF DESCRIPTION OF THE DRAWINGS

[0027] Figure 1 The mass spectrometry identification results of the pentapeptide.

[0028] Figure 2This is the purity identification result of the pentapeptide.

[0029] Figure 3 It is a Lineweaver-Burk diagram.

[0030] Figure 4 This is the corresponding relationship between the slope of the straight line and the concentration of pentapeptide.

[0031] Figure 5 These are the safety test results of pentapeptide.

[0032] Figure 6 This is a graph showing the results of measuring tyrosinase activity after the action of pentapeptide.

[0033] Figure 7 This is a graph showing the results of determining the relative activity of ROS after the action of pentapeptide.

[0034] Figure 8 This is a graph showing the results of measuring SOD activity after the action of pentapeptide.

[0035] Fig. 9 This is the result of measuring the melanin content after the action of pentapeptide. DETAILED DESCRIPTION

[0036] The present invention is further described below in conjunction with the accompanying drawings and specific examples, but the examples do not limit the present invention in any form. Unless otherwise specified, the reagents, methods and equipment used in the present invention are conventional reagents, methods and equipment in the art.

[0037] Unless otherwise specified, the reagents and materials used in the following examples are commercially available.

[0038] All experiments in the embodiments of the present invention were set up in three groups of parallel experiments, and the final data were expressed as mean ± standard deviation. The statistical graphs were completed under Origin 2019 software, and the experimental results were analyzed by one-way analysis of variance on the means of each group using IBM SPSS Statistics 26 software. P < 0.05 indicates that the difference is statistically significant.

[0039] Example 1 Synthesis of pentapeptide

[0040] Shanghai Aminlian Biotechnology Co., Ltd. was commissioned to assist in the synthesis of the pentapeptide, whose amino acid sequence is shown in SEQ ID NO: 1: VLSLY.

[0041] Example 2 Identification of pentapeptides

[0042] (1) ESI-MS mass spectrometry was used to identify the molecular weight of the pentapeptide

[0043] Among them, the identification conditions of ESI-MS mass spectrum are:

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

[0045] Mobile phase B: acetonitrile (containing 0.1% (v / v) trifluoroacetic acid);

[0046] Flow rate: 2mL / min;

[0047] Running time: 4 minutes;

[0048] Operation mode: positive ion mode;

[0049] Scanning range: 0~2000Da.

[0050] The results of mass spectrometry identification are as follows Figure 1 As shown, it can be seen that the molecular ion peak m / z of the pentapeptide of this example is 594.64, with one charge, which is consistent with its theoretical molecular weight value, indicating that the pentapeptide synthesized in this example is the pentapeptide with an amino acid sequence as shown in SEQ ID NO: 1.

[0051] (2) HPLC was used to identify the purity of the pentapeptide

[0052] Among them, the identification conditions of high performance liquid chromatography are:

[0053] Chromatographic column: Inertsil ODS-SP (4.6×250 mm);

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

[0055] Mobile phase B: acetonitrile (containing 0.1% (v / v) trifluoroacetic acid);

[0056] Elution gradient: 0→25 min, 99% (v / v)→50% (v / v) A;

[0057] Flow rate: 1 mL / min;

[0058] Detection wavelength: 220nm;

[0059] Sample volume: 30 μL.

[0060] The results of purity identification are as follows Figure 2 As shown, it can be seen that the main peak in the pentapeptide of this example accounts for the majority, with only very few impurity peaks appearing, and the purity is as high as 97.31%.

[0061] Example 3 In vitro inhibitory effect of pentapeptide on tyrosinase activity

[0062] (1) Reagent preparation

[0063] Tyrosinase solution: Dissolve tyrosinase in phosphate buffer at pH 6.8 to a final concentration of 500 U / mL.

[0064] L-Tyrosine solution: L-Tyrosine was dissolved in phosphate buffer at pH 6.8 to a final concentration of 0.5 mg / mL.

[0065] Sample solution: The pentapeptide obtained in Example 1 was dissolved in a phosphate buffer at pH = 6.8 to a final concentration of 0.2, 0.4, 0.6, 0.8, and 1.0 mg / mL, respectively.

[0066] (2) Test method

[0067] Solvent blank wells: Add 110 μL of PBS solvent to the 96-well plate, incubate at 37°C for 15 min, then add 20 μL of tyrosinase solution to each well, incubate at 37°C for 10 min, and measure the absorbance value A1 at 475 nm.

[0068] 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, incubate at 37°C for 10 min, and measure the absorbance value A2 at 475 nm.

[0069] 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, incubate at 37°C for 10 min, and measure the absorbance value A3 at 475 nm.

[0070] 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°C for 15 min, then add 20 μL of tyrosinase solution to each well, incubate at 37°C for 10 min, and measure the absorbance value A4 at 475 nm.

[0071] The tyrosinase inhibition rate was calculated according to the formula "tyrosinase inhibition rate (%) = [1-(A4-A3) / (A2-A1)] x 100%".

[0072] (3) Test results

[0073] The results showed that the IC 50 The value is 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 preparing whitening products.

[0074] Example 4 Inhibition Types of Tyrosinase Activity by Pentapeptides

[0075] (1) Reagent preparation

[0076] Tyrosinase solution: Dissolve tyrosinase in phosphate buffer at pH 6.8 to a final concentration of 500 U / mL.

[0077] L-tyrosine solution: L-tyrosine was dissolved in phosphate buffer at pH 6.8 to a final concentration of 0.75, 1.00, 1.25, 2.00, and 3.00 mM, respectively.

[0078] Sample solution: The pentapeptide obtained in Example 1 was dissolved in a phosphate buffer at pH = 6.8 to a final concentration of 0, 0.25, 0.50, and 1.00 mM, respectively.

[0079] (2) Test method

[0080] In a 96-well plate, 40 μL of L-tyrosine solution, 40 μL of sample solution and 30 μL of phosphate buffer (pH = 6.8) were added, and incubated at 37°C for 10 min. Then, 20 μL of tyrosinase solution was added, and the plate was incubated at 37°C for another 10 min. The absorbance at 475 nm was measured at 0 and 10 min of the incubation. According to the formula "reaction rate (%) = (A 10 -A 0 ) / 10]×100%”(A 10 is the absorbance value at 10 min, A 0 The reaction rate between the pentapeptide and tyrosinase was calculated using the absorbance value at 0 min. A Lineweaver-Burk plot was made based on the calculation results. The results are shown in Figure 3 As shown, and according to Figure 3 The corresponding relationship between the slope of each straight line and the concentration of pentapeptide is shown in Figure 4 .

[0081] (3) Test results

[0082] Depend on Figure 3 It can be seen that the maximum reaction rate (Vmax, the reciprocal of the intercept on the y-axis) and the Michaelis constant (Km, the reciprocal of the intercept on the x-axis) in the coordinate graph change with the change of the pentapeptide concentration, 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 competition and non-competitiveness, that is, the inhibition type of tyrosinase by the pentapeptide of the present invention is mixed inhibition.

[0083] Depend on Figure 4 It can be seen that the slope of each straight line in the Lineweaver-Burk plot 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.

[0084] Example 5 Safety of Pentapeptides

[0085] (1) Reagent preparation

[0086] Kojic acid solution: In a clean bench, dissolve kojic acid in DMEM medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin-streptomycin double antibody to a final concentration of 300 μM, and then sterilize with a 0.22 μm syringe filter.

[0087] Sample solution: In a clean bench, the pentapeptide obtained in Example 1 was dissolved in DMEM medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin-streptomycin dual antibody to a final concentration of 100, 200, and 400 μM, respectively, and then sterilized with a 0.22 μm syringe filter.

[0088] (2) Test method

[0089] Blank wells: Add 100 μL of DMEM medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin-streptomycin double antibody to the 96-well plate, incubate in a 37°C incubator for 24 hours, discard the supernatant, add 100 μL of DMEM medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin-streptomycin double antibody, incubate in a 37°C incubator for 24 hours, discard the supernatant, add 110 μL of 10% (v / v) CCK-8 solution under light-proof conditions, incubate in a 37°C incubator for 30 minutes, and measure the absorbance value A of each well at 450 nm 空 .

[0090] Control wells: Melanoma cells (B16F10) in the logarithmic growth phase were inoculated in a 96-well plate at a density of 3000 cells / well, and the supernatant was discarded after adaptive culture in a 37°C incubator for 24 hours. 100 μL of DMEM medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin-streptomycin double antibody was added, and the supernatant was discarded after culture in a 37°C incubator for 24 hours. 110 μL of 10% (v / v) CCK-8 solution was added under light-proof conditions, and the cells were incubated in a 37°C incubator for 30 minutes. The absorbance value A of each well at 450 nm was measured. 0 .

[0091] Drug-added sample wells: Melanoma cells (B16F10) in the logarithmic growth phase were inoculated in a 96-well plate at a density of 3000 cells / well, and the supernatant was discarded after adaptive culture in a 37°C incubator for 24 hours. 100 μL of sample solution / kojic acid solution was added respectively, and the supernatant was discarded after culture in a 37°C incubator for 24 hours. 110 μL of 10% (v / v) CCK-8 solution was added under light-proof conditions, and the cells were incubated in a 37°C incubator for 30 minutes. The absorbance value A of each well at 450 nm was measured. 样 .

[0092] According to the formula "Cell viability (%) = [(A 样 -A 空 ) / (A 0 -A 空 )]×100%” to calculate the cell viability after the action of sample solution / kojic acid solution to evaluate the safety of the pentapeptide.

[0093] (3) Test results

[0094] 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 the pentapeptide was treated with 100-400 μM pentapeptide, indicating that the pentapeptide of the present invention has high safety.

[0095] Example 6 Inhibitory effect of pentapeptide on intracellular tyrosinase activity

[0096] (1) Reagent preparation

[0097] Sample solution: The pentapeptide obtained in Example 1 was dissolved in DMEM medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin-streptomycin dual antibody to a final concentration of 100 and 200 μM, respectively.

[0098] (2) Test method

[0099] Blank well (A 空 ): Melanoma cells (B16F10) in the logarithmic growth phase were cultured at 5×10 5 The cells were seeded at a density of 10 cells / well in a 6-well plate, and after adaptive culture in a 37°C incubator for 24 hours, the supernatant was discarded and washed twice with PBS solution (pH = 7.4), and 2 mL of DMEM culture medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin-streptomycin double antibody was added respectively. After culture in a 37°C incubator for 24 hours, 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 (the volume ratio of PMSF: RIPA was 1:100) was added respectively, and the cells were lysed at 4°C for 30 minutes. The supernatant was collected by centrifugation, the protein concentration of the supernatant was determined by BCA kit and normalized, 50 μL of protein solution was taken, mixed with 50 μL of PBS and 50 μL of L-DOPA (10 mM), reacted at 37°C for 30 minutes, and the absorbance value A was measured at 475 nm. 空 .

[0100] Drug-dosing sample well: Melanoma cells (B16F10) in the logarithmic growth phase were taken at 5×10 5The cells were inoculated at a density of 10 cells / well in a 6-well plate. After adaptive culture in a 37°C incubator for 24 hours, the supernatant was discarded and washed twice with PBS solution (pH = 7.4). 2 mL of sample solution was added to each well. After culture in a 37°C incubator for 24 hours, 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 (the volume ratio of PMSF: RIPA was 1:100) was added to each well. The cells were lysed at 4°C for 30 minutes. The supernatant was collected by centrifugation. The protein concentration of the supernatant was determined by a BCA kit and normalized. Then 50 μL of protein solution was taken and mixed with 50 μL of PBS and 50 μL of L-DOPA (10 mM). After reacting at 37°C for 30 minutes, the absorbance value A was measured at 475 nm. 样 .

[0101] According to the formula "Tyrosinase activity (%) = A 样 / A 空 × 100%” to calculate the tyrosinase activity after the sample solution was applied.

[0102] (3) Test results

[0103] The results are as follows Figure 6 As shown, compared with the blank wells, the tyrosinase activity of B16F10 cells was significantly reduced after the action of 100-200 μM pentapeptide, indicating that the pentapeptide of the present invention can significantly inhibit the activity of tyrosinase and is suitable for preparing whitening products.

[0104] Example 7 Antioxidant Effect of Pentapeptide

[0105] (1) Reagent preparation

[0106] Sample solution: In a clean bench, the pentapeptide obtained in Example 1 was dissolved in DMEM medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin-streptomycin dual antibody to a final concentration of 0, 100, and 200 μM, respectively, and then sterilized with a 0.22 μm syringe filter.

[0107] (2) Test method

[0108] ① ROS activity determination method

[0109] Blank wells: Melanoma cells (B16F10) in the logarithmic growth phase were inoculated in a 96-well plate at a density of 3000 cells / well. After adaptive culture in a 37°C incubator for 24 h, the supernatant was discarded and washed twice with PBS solution (pH = 7.4). 100 μL of DMEM medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin-streptomycin double antibody was added and incubated at 37°C, 5% CO 2After 24 hours of intervention in the incubator, the culture medium was discarded, 100 μL of DCFH-DA diluted to a concentration of 10 μM in DMEM culture medium was added, and the supernatant was discarded after incubation in a 37°C incubator for 30 minutes. The cells were washed with PBS solution (pH = 7.4) and the absorbance value A was measured with an enzyme marker. 空 (Set the excitation wavelength to 488 nm and the emission wavelength to 525 nm).

[0110] Drug-added sample wells: Melanoma cells (B16F10) in the logarithmic growth phase were inoculated in a 96-well plate at a density of 3000 cells / well. After adaptive culture in a 37°C incubator for 24 h, the supernatant was discarded and washed twice with PBS solution (pH = 7.4). 100 μL of sample solution was added and incubated at 37°C, 5% CO 2 After 24 hours of intervention in the incubator, the culture medium was discarded, 100 μL of DCFH-DA diluted to a concentration of 10 μM in DMEM culture medium was added, and the supernatant was discarded after incubation in a 37°C incubator for 30 minutes. The cells were washed with PBS solution (pH = 7.4) and the absorbance value A was measured with an enzyme marker. 样 (Set the excitation wavelength to 488 nm and the emission wavelength to 525 nm).

[0111] According to "ROS relative activity (%) = A 样 / A 空 × 100%” to calculate the relative activity of ROS.

[0112] ②SOD activity determination method

[0113] Melanoma cells (B16F10) in logarithmic growth phase were cultured at 5×10 5 Cells were inoculated in a 6-well plate at a density of 10 cells / well. After adaptive culture in a 37°C incubator for 24 hours, the supernatant was discarded and washed twice with PBS solution (pH = 7.4). 2 mL of sample solution was added. After culture in a 37°C incubator for 24 hours, the supernatant was discarded and washed twice with PBS solution (pH = 7.4) to remove non-adherent cells. Then 400 μL of lysis buffer (PMSF: RIPA volume ratio is 1: 100) was added respectively, and the cells were lysed at 4°C for 30 minutes. The supernatant was collected by centrifugation. The activity of SOD in the supernatant was determined according to the instructions of the SOD kit of Nanjing Jiancheng Bioengineering Institute.

[0114] (3) Test results

[0115] The results of ROS relative activity are as follows Figure 7 As shown, the SOD activity results are as follows Figure 8As shown, compared with the blank group, after the action of 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.

[0116] Example 6 Inhibitory effect of pentapeptide on melanin

[0117] (1) Reagent preparation

[0118] Sample solution: In a clean bench, the pentapeptide obtained in Example 1 was dissolved in DMEM medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin-streptomycin dual antibody to a final concentration of 100 and 200 μM, respectively, and then sterilized with a 0.22 μm syringe filter.

[0119] (2) Test method

[0120] Blank wells: Melanoma cells (B16F10) in logarithmic growth phase were collected and plated at 5×10 5 The cells were inoculated in a 6-well plate at a density of 10 cells / well. After adaptive culture in a 37°C incubator for 24 hours, the supernatant was discarded and washed twice with PBS solution (pH=7.4). 2 mL of DMEM culture medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin-streptomycin double antibody was added respectively. After culture in a 37°C incubator for 24 hours, the supernatant was discarded, and the cells were washed twice with PBS solution (pH=7.4) to remove non-adherent cells. Then, the cells were digested with trypsin, and the digestion products were collected and centrifuged at 1500 r / min for 10 minutes. 1 mL of NaOH solution (1 mol / L) containing 10% (v / v) DMSO was added to the precipitate obtained by centrifugation. After extraction in a water bath at 80°C for 1 hour, the absorbance value A of each well at 450 nm was measured. 空 .

[0121] Drug-dosing sample well: Melanoma cells (B16F10) in the logarithmic growth phase were taken at 5×10 5 The cells were inoculated in a 6-well plate at a density of 10 cells / well. After adaptive culture in a 37°C incubator for 24 hours, the supernatant was discarded and washed twice with PBS solution (pH = 7.4). 2 mL of sample solution was added to each well. After culture in a 37°C incubator for 24 hours, the supernatant was discarded and washed twice with PBS solution (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 minutes. 1 mL of NaOH solution (1 mol / L) containing 10% (v / v) DMSO was added to the precipitate obtained by centrifugation. After extraction in a water bath at 80°C for 1 hour, the absorbance value A of each well at 450 nm was measured. 样 .

[0122] According to the formula "Melanin content (%) = A 样 / A 空 × 100%” to calculate the melanin content after the sample solution was applied.

[0123] (3) Test results

[0124] The results are as follows Fig. 9 As shown, compared with the blank wells, the melanin content of B16F10 cells was significantly reduced after the action of 100-200 μM pentapeptide, indicating that the pentapeptide of the present invention can significantly inhibit the formation of melanin and is suitable for preparing whitening products.

[0125] The above embodiments are preferred implementation modes of the present invention, but the implementation modes of the present invention are not limited to the above embodiments. Any other changes, modifications, substitutions, combinations, and simplifications that do not deviate from the spirit and principles of the present invention should be equivalent replacement methods and are included in the protection scope of the present invention.

Claims

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

1.

2. Use of the pentapeptide according to claim 1 or its related biomaterials in the preparation of melanin inhibitors.

3. The application according to claim 2, characterized in that: The related 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.

4. Use of the pentapeptide or related biomaterials according to claim 1 in the preparation of antioxidant products.

5. The application according to claim 4, characterized in that: The related 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.

6. Use of the pentapeptide according to claim 1 or its related biomaterials in the preparation of tyrosinase inhibitors.

7. The use according to claim 6, characterized in that: The related 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.

8. Use of the pentapeptide or related biomaterials according to claim 1 in the preparation of whitening products.

9. The use according to claim 8, characterized in that: The related 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.

10. A product, characterized in that Comprising the pentapeptide according to claim 1 and / or its related biological materials.

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