CN116621925A - Pearl shell melanin inhibiting peptide with whitening effect and application thereof - Google Patents
Pearl shell melanin inhibiting peptide with whitening effect and application thereof Download PDFInfo
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- CN116621925A CN116621925A CN202211176479.5A CN202211176479A CN116621925A CN 116621925 A CN116621925 A CN 116621925A CN 202211176479 A CN202211176479 A CN 202211176479A CN 116621925 A CN116621925 A CN 116621925A
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- Prior art keywords
- melanin
- tyrosinase
- inhibiting peptide
- peptide
- melanin inhibiting
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- XUMBMVFBXHLACL-UHFFFAOYSA-N Melanin Chemical compound O=C1C(=O)C(C2=CNC3=C(C(C(=O)C4=C32)=O)C)=C2C4=CNC2=C1C XUMBMVFBXHLACL-UHFFFAOYSA-N 0.000 title claims abstract description 212
- 230000002401 inhibitory effect Effects 0.000 title claims abstract description 130
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 108
- 230000002087 whitening effect Effects 0.000 title claims abstract description 24
- 241000490567 Pinctada Species 0.000 claims abstract description 49
- 239000003814 drug Substances 0.000 claims abstract description 10
- 239000002537 cosmetic Substances 0.000 claims abstract description 9
- 235000013376 functional food Nutrition 0.000 claims abstract description 8
- 102000003425 Tyrosinase Human genes 0.000 claims description 81
- 108060008724 Tyrosinase Proteins 0.000 claims description 81
- 238000002360 preparation method Methods 0.000 claims description 12
- 239000003112 inhibitor Substances 0.000 claims description 10
- 125000000539 amino acid group Chemical group 0.000 claims description 9
- 108010058393 monophenolase Proteins 0.000 claims description 9
- 229910052739 hydrogen Inorganic materials 0.000 claims description 5
- 239000001257 hydrogen Substances 0.000 claims description 5
- 230000008099 melanin synthesis Effects 0.000 claims description 2
- 239000002773 nucleotide Substances 0.000 claims 1
- 125000003729 nucleotide group Chemical group 0.000 claims 1
- 229940079593 drug Drugs 0.000 abstract description 6
- 125000003275 alpha amino acid group Chemical group 0.000 abstract 1
- 241000252212 Danio rerio Species 0.000 description 29
- 230000000694 effects Effects 0.000 description 20
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 16
- 102000004196 processed proteins & peptides Human genes 0.000 description 14
- 238000003032 molecular docking Methods 0.000 description 13
- 238000002835 absorbance Methods 0.000 description 12
- 235000013372 meat Nutrition 0.000 description 10
- 102000007079 Peptide Fragments Human genes 0.000 description 9
- 108010033276 Peptide Fragments Proteins 0.000 description 9
- 235000013601 eggs Nutrition 0.000 description 9
- 230000036564 melanin content Effects 0.000 description 9
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 9
- 238000000338 in vitro Methods 0.000 description 8
- 229960003180 glutathione Drugs 0.000 description 7
- 239000007788 liquid Substances 0.000 description 7
- 239000013641 positive control Substances 0.000 description 7
- 230000005764 inhibitory process Effects 0.000 description 6
- 238000012800 visualization Methods 0.000 description 6
- 241000251468 Actinopterygii Species 0.000 description 5
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 5
- 238000002474 experimental method Methods 0.000 description 5
- 239000000523 sample Substances 0.000 description 5
- 238000012216 screening Methods 0.000 description 5
- 239000000758 substrate Substances 0.000 description 5
- 102000004190 Enzymes Human genes 0.000 description 4
- 108090000790 Enzymes Proteins 0.000 description 4
- WTDRDQBEARUVNC-LURJTMIESA-N L-DOPA Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C(O)=C1 WTDRDQBEARUVNC-LURJTMIESA-N 0.000 description 4
- WTDRDQBEARUVNC-UHFFFAOYSA-N L-Dopa Natural products OC(=O)C(N)CC1=CC=C(O)C(O)=C1 WTDRDQBEARUVNC-UHFFFAOYSA-N 0.000 description 4
- 238000000034 method Methods 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- 108090000145 Bacillolysin Proteins 0.000 description 3
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 3
- 102000035092 Neutral proteases Human genes 0.000 description 3
- 108091005507 Neutral proteases Proteins 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 150000001413 amino acids Chemical group 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 239000003963 antioxidant agent Substances 0.000 description 3
- 230000003078 antioxidant effect Effects 0.000 description 3
- 235000006708 antioxidants Nutrition 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 230000002255 enzymatic effect Effects 0.000 description 3
- 238000011156 evaluation Methods 0.000 description 3
- 230000002209 hydrophobic effect Effects 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 239000002244 precipitate Substances 0.000 description 3
- 102000004169 proteins and genes Human genes 0.000 description 3
- 108090000623 proteins and genes Proteins 0.000 description 3
- 239000012488 sample solution Substances 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 238000000108 ultra-filtration Methods 0.000 description 3
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 2
- 241000219173 Carica Species 0.000 description 2
- 235000009467 Carica papaya Nutrition 0.000 description 2
- QIGBRXMKCJKVMJ-UHFFFAOYSA-N Hydroquinone Chemical compound OC1=CC=C(O)C=C1 QIGBRXMKCJKVMJ-UHFFFAOYSA-N 0.000 description 2
- 208000003351 Melanosis Diseases 0.000 description 2
- 241001212699 Pinctada martensii Species 0.000 description 2
- 239000004480 active ingredient Substances 0.000 description 2
- 238000009395 breeding Methods 0.000 description 2
- 230000001488 breeding effect Effects 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 238000010586 diagram Methods 0.000 description 2
- 238000010828 elution Methods 0.000 description 2
- 230000004720 fertilization Effects 0.000 description 2
- 239000000413 hydrolysate Substances 0.000 description 2
- BJRNKVDFDLYUGJ-RMPHRYRLSA-N hydroquinone O-beta-D-glucopyranoside Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1OC1=CC=C(O)C=C1 BJRNKVDFDLYUGJ-RMPHRYRLSA-N 0.000 description 2
- 238000001294 liquid chromatography-tandem mass spectrometry Methods 0.000 description 2
- 238000004949 mass spectrometry Methods 0.000 description 2
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 2
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 239000007921 spray Substances 0.000 description 2
- 230000004083 survival effect Effects 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 230000001988 toxicity Effects 0.000 description 2
- 231100000419 toxicity Toxicity 0.000 description 2
- 229960004441 tyrosine Drugs 0.000 description 2
- 229910021642 ultra pure water Inorganic materials 0.000 description 2
- 239000012498 ultrapure water Substances 0.000 description 2
- 108700024526 zebrafish sox32 Proteins 0.000 description 2
- XKZQKPRCPNGNFR-UHFFFAOYSA-N 2-(3-hydroxyphenyl)phenol Chemical compound OC1=CC=CC(C=2C(=CC=CC=2)O)=C1 XKZQKPRCPNGNFR-UHFFFAOYSA-N 0.000 description 1
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 1
- 235000001674 Agaricus brunnescens Nutrition 0.000 description 1
- 208000037259 Amyloid Plaque Diseases 0.000 description 1
- 240000000425 Chaenomeles speciosa Species 0.000 description 1
- 235000005078 Chaenomeles speciosa Nutrition 0.000 description 1
- 206010008570 Chloasma Diseases 0.000 description 1
- 108010024636 Glutathione Proteins 0.000 description 1
- 206010027146 Melanoderma Diseases 0.000 description 1
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 1
- 108010009736 Protein Hydrolysates Proteins 0.000 description 1
- 235000017831 Pseudocydonia sinensis Nutrition 0.000 description 1
- XZKQVQKUZMAADP-IMJSIDKUSA-N Ser-Ser Chemical compound OC[C@H](N)C(=O)N[C@@H](CO)C(O)=O XZKQVQKUZMAADP-IMJSIDKUSA-N 0.000 description 1
- 208000031320 Teratogenesis Diseases 0.000 description 1
- 101710147108 Tyrosinase inhibitor Proteins 0.000 description 1
- 210000001015 abdomen Anatomy 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 230000003064 anti-oxidating effect Effects 0.000 description 1
- 229960000271 arbutin Drugs 0.000 description 1
- 235000010323 ascorbic acid Nutrition 0.000 description 1
- 229960005070 ascorbic acid Drugs 0.000 description 1
- 239000011668 ascorbic acid Substances 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 239000007844 bleaching agent Substances 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 230000018044 dehydration Effects 0.000 description 1
- 238000006297 dehydration reaction Methods 0.000 description 1
- 238000010612 desalination reaction Methods 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 238000003028 enzyme activity measurement method Methods 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 235000019253 formic acid Nutrition 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 238000005984 hydrogenation reaction Methods 0.000 description 1
- 229960004337 hydroquinone Drugs 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000037427 ion transport Effects 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- BEJNERDRQOWKJM-UHFFFAOYSA-N kojic acid Chemical compound OCC1=CC(=O)C(O)=CO1 BEJNERDRQOWKJM-UHFFFAOYSA-N 0.000 description 1
- 229960004705 kojic acid Drugs 0.000 description 1
- WZNJWVWKTVETCG-UHFFFAOYSA-N kojic acid Natural products OC(=O)C(N)CN1C=CC(=O)C(O)=C1 WZNJWVWKTVETCG-UHFFFAOYSA-N 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 238000005360 mashing Methods 0.000 description 1
- 230000003061 melanogenesis Effects 0.000 description 1
- 201000001441 melanoma Diseases 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 230000009456 molecular mechanism Effects 0.000 description 1
- BJRNKVDFDLYUGJ-UHFFFAOYSA-N p-hydroxyphenyl beta-D-alloside Natural products OC1C(O)C(O)C(CO)OC1OC1=CC=C(O)C=C1 BJRNKVDFDLYUGJ-UHFFFAOYSA-N 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 239000008055 phosphate buffer solution Substances 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- REQCZEXYDRLIBE-UHFFFAOYSA-N procainamide Chemical compound CCN(CC)CCNC(=O)C1=CC=C(N)C=C1 REQCZEXYDRLIBE-UHFFFAOYSA-N 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 238000004725 rapid separation liquid chromatography Methods 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 238000004366 reverse phase liquid chromatography Methods 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 230000005808 skin problem Effects 0.000 description 1
- 238000010532 solid phase synthesis reaction Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 238000004885 tandem mass spectrometry Methods 0.000 description 1
- 238000012795 verification Methods 0.000 description 1
- 229910052724 xenon Inorganic materials 0.000 description 1
- FHNFHKCVQCLJFQ-UHFFFAOYSA-N xenon atom Chemical compound [Xe] FHNFHKCVQCLJFQ-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
- A23L33/18—Peptides; Protein hydrolysates
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
- A61Q19/02—Preparations for care of the skin for chemically bleaching or whitening the skin
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K2800/00—Properties of cosmetic compositions or active ingredients thereof or formulation aids used therein and process related aspects
- A61K2800/74—Biological properties of particular ingredients
- A61K2800/78—Enzyme modulators, e.g. Enzyme agonists
- A61K2800/782—Enzyme inhibitors; Enzyme antagonists
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A40/00—Adaptation technologies in agriculture, forestry, livestock or agroalimentary production
- Y02A40/80—Adaptation technologies in agriculture, forestry, livestock or agroalimentary production in fisheries management
- Y02A40/81—Aquaculture, e.g. of fish
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Organic Chemistry (AREA)
- Veterinary Medicine (AREA)
- Dermatology (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Engineering & Computer Science (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Biochemistry (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Birds (AREA)
- Epidemiology (AREA)
- Mycology (AREA)
- Nutrition Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Cosmetics (AREA)
- Peptides Or Proteins (AREA)
Abstract
The invention relates to a pearl shell melanin inhibiting peptide with a whitening effect and application thereof. The pearl oyster melanin inhibiting peptide has the amino acid sequence shown in SEQ ID NO:1, specifically: SPSSS (Ser-Pro-Ser-Ser-Ser). The inventor of the invention discovers that the pearl oyster melanin inhibiting peptide can inhibit melanin generation, has good whitening activity and good safety, and can be widely applied to the fields of medicines, functional foods, cosmetics and the like.
Description
Technical Field
The invention relates to the technical field of active peptides, in particular to a pearl shell melanin inhibiting peptide with a whitening effect and application thereof.
Background
Melanin can reduce damage to skin caused by Ultraviolet (UV) radiation, but excessive melanin generation can cause skin problems such as chloasma, freckle and senile plaque, and even cause related diseases such as melanoma. Substances such as ascorbic acid, kojic acid, hydroquinone and arbutin are often used as effective active ingredients for skin antioxidation and whitening, but have limited application due to the problems of poor stability or strong toxicity, etc. Because of the wide demand for whitening agents in the fields of foods, medicines and cosmetics, a safe and stable natural active substance capable of inhibiting melanin generation is sought, for example, a group of small peptides capable of inhibiting melanin generation are provided by Chinese patent named antioxidant small peptides capable of inhibiting melanin generation, a preparation method and application of the antioxidant small peptides. However, there is still little research on natural peptides that inhibit melanogenesis. Therefore, the search for natural peptides for inhibiting melanin production has important practical significance and application prospect.
Disclosure of Invention
The primary purpose of the invention is to overcome the problem that the prior natural peptide for inhibiting melanin generation lacks, and provide the pearl shell melanin inhibiting peptide with whitening effect. The pearl oyster melanin inhibiting peptide can inhibit melanin generation, has good whitening activity and good safety, and can be widely applied to the fields of medicines, functional foods, cosmetics and the like. In addition, the pearl oyster melanin inhibiting peptide also has tyrosinase inhibiting activity.
The invention further aims to provide application of the pearl oyster melanin inhibiting peptide in preparing whitening medicines.
It is a further object of the present invention to provide the use of the above-mentioned pearl oyster melanin inhibiting peptide in the preparation of cosmetics.
A further object of the present invention is to provide the use of the above-mentioned pearl oyster melanin inhibiting peptide in the preparation of functional foods.
A further object of the present invention is to provide the use of the above-mentioned nacre melanin inhibiting peptide in the preparation of tyrosinase inhibitors.
A nacre melanin inhibiting peptide with whitening efficacy, said nacre melanin inhibiting peptide having the amino acid sequence as set forth in seq id no: 1.
The pearl shell melanin inhibiting peptide disclosed by the invention has the amino acid sequence shown in SEQ ID NO:1, specifically: SPSSS (Ser-Pro-Ser-Ser-Ser). The inventor of the invention discovers that the pearl oyster melanin inhibiting peptide can inhibit melanin generation, has good whitening activity and good safety, and can be widely applied to the fields of medicines, functional foods, cosmetics and the like.
The application of the pearl shell melanin inhibiting peptide in preparing the whitening medicine is also in the protection scope of the invention.
Preferably, the application of the pearl shell melanin inhibiting peptide in preparing a whitening medicine for inhibiting melanin generation.
The application of the pearl shell melanin inhibiting peptide in preparing cosmetics is also within the protection scope of the invention.
The application of the pearl shell melanin inhibiting peptide in preparing functional foods is also within the protection scope of the invention.
The application of the pearl shell melanin inhibiting peptide in preparing tyrosinase inhibitors is also in the protection scope of the invention.
The inventors of the present invention have also found that the pearl oyster melanin inhibiting peptide can form 11 hydrogen bonds with amino acid residues LYS379, ASP312, LYS376, GLN351, ASP353 and GLU356 of tyrosinase, so as to stably combine with the active center of tyrosinase, inhibit the activity of tyrosinase, and thus inhibit the generation of melanin.
Preferably, the use of the nacre melanin inhibiting peptide in the preparation of a tyrosinase inhibitor that hydrogen bonds with amino acid residues LYS379, ASP312, LYS376, GLN351, ASP353 and GLU356 of tyrosinase.
Preferably, the application of the pearl shell melanin inhibiting peptide in preparing an inhibitor with tyrosinase monophenolase inhibiting activity and/or tyrosinase diphenolase inhibiting activity.
More preferably, the pearl oyster melanin inhibiting peptide is applied to the preparation of an inhibitor with tyrosinase monophenolase inhibiting activity.
More preferably, the use of the nacre melanin inhibiting peptide in the preparation of an inhibitor having tyrosinase diphenolase inhibitory activity.
Compared with the prior art, the invention has the beneficial effects that:
the pearl shell melanin inhibiting peptide can inhibit melanin generation, has good whitening activity and good safety, and can be widely applied to the fields of medicines, functional foods, cosmetics and the like. In addition, the pearl oyster melanin inhibiting peptide also has tyrosinase inhibiting activity.
Drawings
FIG. 1 is a graph showing the results of evaluation of tyrosinase inhibitory activity in vitro of the enzymatic hydrolysate and active ingredient of example 1.
Fig. 2 is a 3D and 2D visualization of the interface of the nacreous layer melanin inhibiting peptide and tyrosinase, wherein fig. 2A is a 3D visualization of the interface of the nacreous layer melanin inhibiting peptide and tyrosinase (2 y9 x), and fig. 2B is a 2D visualization of the interface of the nacreous layer melanin inhibiting peptide and tyrosinase (2 y9 x).
FIG. 3 is a graph showing the results of evaluating tyrosinase inhibitory activity in vitro of the pearl oyster melanin inhibiting peptide of example 3.
FIG. 4 is a graph showing the experimental results of the effect of the pearl shell melanin inhibiting peptide of example 4 on the survival rate of zebra fish.
FIG. 5 is a graph showing the experimental results of the effect of the pearl oyster melanin inhibiting peptide of example 4 on the melanin content of zebra fish.
FIG. 6 is a graph showing the experimental results of the effect of the pearl oyster melanin inhibiting peptide of example 4 on the tyrosinase activity of zebra fish.
Detailed Description
The present invention will be described in further detail with reference to the following specific examples for the purpose of illustration and not limitation, and various modifications may be made within the scope of the present invention as defined by the appended claims.
The main reagents and raw material sources of the embodiments of the invention are as follows:
pearl oyster meat (Pinctada martensii meat): north sea black pearl Marine biotechnology Co.Ltd (Guangxi, china).
Neutral protease (10 kU/g): nanning Pang Bo bioengineering Co., ltd (Nanjing, china).
L-tyrosine, L-dopa, tyrosinase (BR, mushroom, 500U/mg,25 kU): shanghai Yuan Yes biotechnology Co., ltd (Nanjing, china).
Other reagents are all analytically pure, and ultrapure water is self-made in a laboratory.
EXAMPLE 1 preparation of enzymatic hydrolysate and active Components
The invention adopts neutral protease to carry out enzymolysis treatment on pearl oyster meat and ultrafiltration separation treatment to obtain active components with different molecular weights, and the specific process is as follows:
and (3) enzymolysis treatment: mashing pearl oyster meat into meat paste, adding ultrapure water (feed liquid ratio 1:1, w/w) and adjusting pH to 7.25, adding neutral protease (enzyme bottom ratio 0.4%, w/w), performing enzymolysis at 50deg.C for 3h, immediately inactivating enzyme at 90deg.C for 15min after enzymolysis, cooling at room temperature, centrifuging at 4000r/min for 15min to obtain pearl oyster meat enzymolysis liquid, and storing at-20deg.C for further analysis.
Ultrafiltration separation: separating the pearl oyster meat enzymolysis liquid by an ultrafiltration membrane (3 kDa) according to the molecular weight at room temperature to obtain two active components of which the molecular weight is more than or equal to 3kDa and less than 3kDa, collecting sample liquid separately, and freeze-drying and preserving the sample liquid for subsequent activity research.
And respectively taking the pearl oyster meat enzymolysis liquid, the components with the molecular weight of more than or equal to 3kDa and the components with the molecular weight of less than 3kDa as sample liquids, and evaluating the in-vitro tyrosinase inhibitory activity.
The specific process of the in vitro tyrosinase inhibitory activity experiment is as follows:
l-tyrosine and L-dopa were used as a monophenol substrate and a diphenol substrate, respectively, 40. Mu. L L-tyrosine solution (0.5 mM) or L-dopa solution (0.5 mM) was added, 40. Mu.L of the sample solution and 80. Mu.L of the phosphate buffer solution (0.05M, pH 6.8) were added, the reaction was started by adding 40. Mu.L of the tyrosinase solution (250U/mL) after 10min incubation at 37℃and absorbance values were measured at 475nm by an enzyme-labeled instrument (Enspire Xenon Light Module,200Perkin-Elmer, beaconsfield, U.K.), respectively. Tyrosinase inhibition rates (including monophenolase inhibition rate of tyrosinase and diphenolase inhibition rate of tyrosinase) were calculated according to formula (1).
Tyrosinase inhibition rate/% = [1- (Δa) 1 -ΔA 2 )/(ΔA 3 -ΔA 4 )]×100％ (1)
Wherein: a is that 1 The absorbance values of the substrate, the sample solution, tyrosinase and PBS system; a is that 2 The absorbance values are the absorbance values of the sample solution, tyrosinase and PBS system; a is that 3 Absorbance values for substrate, tyrosinase and PBS systems; a is that 4 Is the absorbance of tyrosinase and PBS systems.
The in vitro tyrosinase inhibitory activity evaluation results of the pearl oyster meat enzymatic hydrolysate, the components with the molecular weight of more than or equal to 3kDa and the components with the molecular weight of less than 3kDa are shown in the figure 1, wherein the figure 1A is a graph of tyrosinase monophenolase inhibitory activity, and the figure 1B is a graph of tyrosinase diphenolase inhibitory activity. As can be seen from FIG. 1, the pearl oyster meat zymolyte, the 3kDa fraction or more and the 3kDa fraction have tyrosinase monophenolase inhibitory activity and tyrosinase diphenolase inhibitory activity; the < 3kDa fraction was better active than the substrate and the.gtoreq.3 kDa fraction at 0.5mg/mL and 1mg/mL, with significance (p < 0.05) at 0.5mg/mL, indicating that the more active peptide fraction was concentrated mainly in the < 3kDa fraction. The diphenolase inhibitory activity of the < 3kDa fraction was 15.96% at 1mg/mL, slightly higher than that of the < 1kDa fraction (about 15%) and the 1-3kDa fraction (about 5%) of the papaya seed active peptide (data of the papaya seed active peptide are derived from the literature: skin-care functions of peptides prepared from Chinese quince seed protein: sequences analysis, tyrosinase inhibition and molecular docking study, yejunde et. Industrial Crops and Products, volume 148,June 2020,112331), indicating that the < 3kDa fraction has better tyrosinase inhibitory ability. Peptide fragment analysis was performed with the < 3kDa fraction as a further subject.
Example 2 structural identification of Pearl shell melanin inhibiting peptide, molecular docking screening and peptide Synthesis
Structural identification by LC-MS/MS: after desalination treatment<The 3kDa was loaded onto an Easy nLC 1200 nanoliter liquid phase system (ThermoFisher, USA) and analyzed on a C18 reverse phase chromatography column (2 μm,75 μm. Times.25 cm,acclaim PepMap RSLC) elution. Elution procedure was B (80)% acetonitrile, 0.1% formic acid) 0-60 min:5% -38%. Mass spectrometry was performed using a ThermoFisher Q Exactive system (ThermoFisher, USA) in combination with a nanoliter spray Nano Flex ion source (ThermoFisher, USA) at a spray voltage of 1.9kV and an ion transport tube heating temperature of 275 ℃. The molecular mass and amino acid sequence of the peptide fragment were determined sequentially by primary and secondary mass spectrometry, and the MS/MS original file was analyzed by using pFind search engine. The primary structure of the peptide fragment was determined by searching the Pinctada martensi species protein database in UniProt, and matching the peptide sequences.
Adopting LC-MS/MS to carry out structural identification on the component less than 3kDa, identifying 404 peptide fragments of the component less than 3kDa, and carrying out preliminary screening under the condition that amino acid residues are less than or equal to 10 and the confidence coefficient is more than or equal to 30 to obtain 117 peptide fragments.
Molecular docking and screening: and (3) respectively carrying out molecular docking on 117 peptide fragments obtained by preliminary screening and tyrosinase (PDB ID:2y9 x) on Autodock vina software, simulating a possible combination mode of peptide and tyrosinase, and screening peptide sequences with optimal tyrosinase inhibition potential. The three-dimensional coordinates of tyrosinase were downloaded from the protein database (https:// www.rcsb.org /). The three-dimensional structure of the peptide adopts a MarvinSketch design, and an energy-minimized three-dimensional conformation is exported, and tyrosinase and the peptide are respectively led into AutoDockTools (ADT) for pretreatment such as dehydration, hydrogenation and the like. Setting the center of the docking box as center_x: 7.384, center_y: 23.549 and center_z: -19.8, size size_x:47.25, size_y:47.25, size_z:47.25. to improve docking accuracy, the exhaustive number will be 20, the others being default parameters. An AutoDock vina docking program was run, and an optimal docking conformation was selected according to the built-in scoring function and visually analyzed using Discovery Studio Visualizer.
The 117 peptide fragments were molecular-docked with tyrosinase (PDB ID:2y9 x), respectively, and the peptide fragments with low binding energy were selected. The results of the docking of the pearl oyster melanin inhibiting peptide (sequence: SPSSS, namely Ser-Pro-Ser-Ser-Ser) with tyrosinase (2 y9 x) are shown in Table 1. The binding energy of the pearl oyster melanin inhibiting peptide and tyrosinase (2 y9 x) is-8.4 kcal/mol, and the pearl oyster melanin inhibiting peptide has good binding effect with tyrosinase (2 y9 x), and theoretically shows that the pearl oyster melanin inhibiting peptide has the capability of tightly binding with tyrosinase active center.
TABLE 1 molecular docking of Pearl shell melanin inhibiting peptides to tyrosinase (2 y9 x)
| Peptides | Molecular weight (Da) | Amino acid residues | Confidence level | Binding energy (kcal/mol) |
| Pearl shell melanin inhibiting peptide | 463.1914 | 5 | 35.4 | -8.4 |
The biological activity of a peptide fragment is related to its structure. The 3D and 2D visualization results of the docking of the pearl oyster melanin inhibiting peptide with tyrosinase (2 y9 x) are shown in fig. 2, wherein fig. 2A is a 3D visualization diagram of the docking of the pearl oyster melanin inhibiting peptide with tyrosinase (2 y9 x), and fig. 2B is a 2D visualization diagram of the docking of the pearl oyster melanin inhibiting peptide with tyrosinase (2 y9 x). As can be seen from FIG. 2, the pearl oyster melanin inhibiting peptide forms 11 hydrogen bonds with multiple sites of amino acid residues LYS379, ASP312, LYS376, GLN351, ASP353 and GLU356 of tyrosinase (2 y9 x) in total, and the bond length range isSpecific butt jointThe sites are shown in Table 2, and more hydrogen bonds and shorter bond length enable the pearl oyster melanin inhibiting peptide to be combined with the active center of tyrosinase (2 y9 x) stably on molecular mechanism, so that the activity of tyrosinase can be inhibited.
TABLE 2 molecular docking site of Pearl shell melanin inhibiting peptide and tyrosinase (2 y9 x)
Synthesis of pearl shell melanin inhibiting peptide: the purity of the synthesized pearl shell melanin inhibiting peptide is more than 98 percent by adopting a solid phase synthesis method and being synthesized by Nanje peptide biotechnology company, and the pearl shell melanin inhibiting peptide is preserved at the temperature of minus 20 ℃ and is used for subsequent test experiments.
Example 3 evaluation of in vitro tyrosinase inhibitory Activity of Pearl oyster melanin inhibiting peptides
The in vitro tyrosinase inhibitory activity of the pearl oyster melanin inhibitory peptide is evaluated according to the in vitro tyrosinase inhibitory activity experiment, which is shown in figure 3, and the result shows that the pearl oyster melanin inhibitory peptide has a monophenolase inhibitory rate of 65.26% to tyrosinase and a diphenolase inhibitory rate of 15.96% to tyrosinase at 1mg/mL, thus indicating that the pearl oyster melanin inhibitory peptide has good tyrosinase monophenolase inhibitory activity and tyrosinase diphenolase inhibitory activity.
The ratio of hydrophobic amino acid residues in the pearl shell melanin inhibiting peptide is 20%, and the hydrophobic side chain of the amino acid residue Pro can directly interact with the hydrophobic region of tyrosinase to inhibit the activity of tyrosinase. Meanwhile, the repeated amino acid residues Ser-Ser of the pearl oyster melanin inhibiting peptide can enhance the tyrosinase inhibiting capability of the pearl oyster melanin inhibiting peptide.
Example 4 study of the whitening efficacy of Pearl oyster melanin inhibiting peptides based on zebra fish model
4.1 cultivation of Zebra fish
The wild zebra fish is fed in an environment with the water temperature of 28.5 ℃ and the pH of 7.5-8.5, 10 groups of zebra fish are placed in a breeding jar with a baffle plate according to the breeding proportion of 1:2, the male and the female are separated, the light treatment is recovered after the dark treatment for 12 hours, and the baffle plate is extracted to lead the zebra fish to mate so as to obtain the fish eggs, wherein the fertilization rate of the healthy zebra fish is more than or equal to 80 percent, and the zebra fish can be selected for experiments.
4.2 Effect of pearl oyster melanin inhibiting peptide on survival of zebra fish
Zebra fish eggs have high sensitivity, and toxicity verification is carried out before an activity experiment. Healthy zebra fish eggs are collected and plated in 96-well plates at a density of 1 tail per well, 180 mu L of zebra fish culture water containing different concentrations of pearl shell melanin inhibiting peptides (25, 50, 100, 150, 200, 250 and 500 mu g/mL) is added into each well, egg death and teratogenesis are observed every 24 hours, continuous observation is carried out for 5 days, and the effect of the pearl shell melanin inhibiting peptides with different concentrations on the development of the zebra fish is observed, and the result is shown in figure 4. As can be seen from FIG. 4, the whole of the pearl oyster melanin inhibiting peptide-treated zebra fish survived in the concentration range of 25-500. Mu.g/mL, and the physiological state was normal. The whitening efficacy study of the pearl oyster melanin inhibiting peptide is carried out on the basis.
4.3 Effect of Pearl shell melanin inhibiting peptide on melanin content and tyrosinase activity of zebra fish
The whole body of the recently produced zebra fish egg is transparent, and along with the development of fertilized eggs, melanin on the body surface and in the body of the zebra fish egg is gradually generated, and finally the fish egg grows into fish, so that the black formation condition of the body surface of the zebra fish can be directly observed, the influence of a sample on the synthesis of the melanin in the zebra fish is reflected, and the whitening effect is further evaluated. Glutathione (GSH) is a short segment with antioxidant and whitening effects, often applied in functional foods or cosmetics, and can be used as a positive control of whitening active peptides.
Healthy zebra fish eggs after 24h fertilization are collected, plated at a density of 20 tails per well in a 12-well plate, 2mL of zebra fish culture water (10. Mu.g/mL, 50. Mu.g/mL, 200. Mu.g/mL) containing pearl oyster melanin inhibiting peptide is added, and a blank group (2 mL of culture water) and a positive control group (GSH-containing culture water, 10. Mu.g/mL, 50. Mu.g/mL, 200. Mu.g/mL) are set, respectively. After a constant temperature treatment of 48h at 28.5 ℃, zebra fish were taken under a body view mirror (Nikon SMZ460, nikon corporation, japan) to observe morphology and melanin distribution and to take back and side views. The rest zebra fish is collected, washed by distilled water, frozen (-80 ℃) and killed, 200 mu L of Western and IP cell lysate (containing 1% (volume fraction) of PMSF) after ice bath is added, and the broken fish body is repeatedly frozen and thawed for 3 times, and centrifuged at 4000r/min for 10min to obtain supernatant and precipitate.
The precipitate was taken for melanin content determination, 250. Mu.L of NaOH solution (1M, 10% DMSO) was added to the precipitate, water was used in a water bath at 85℃for 2 hours, 100. Mu.L was taken and added to a 96-well plate, and absorbance was measured at 405 nm. Each sample was normalized with BCA kit (bi yun). The relative melanin content was calculated according to formula (2), respectively.
Relative melanin content/% = (a t /A o )×100％ (2)
Wherein: a is that t Absorbance values for the nacre melanin inhibiting peptide treated group or the positive control (GSH) group; a is that 0 Absorbance values for the blank group.
The supernatant was used for measuring tyrosinase activity, 20. Mu.L of the supernatant and 180. Mu. L L-dopa (1 mg/mL) were mixed in a 96-well plate, incubated at 37℃for 2 hours in the absence of light, absorbance was measured at 470 nm, and relative tyrosinase activity was calculated according to formula (3), respectively.
Relative tyrosinase activity/% = (a t ’/A o ’)×100％ (3)
Wherein: a is that t ' absorbance value for peptide treated group or positive control (GSH) group with whitening activity; a is that 0 ' is the absorbance of the blank group.
The results of the relative melanin content test are shown in fig. 5. FIG. 5A is a back view and a side view of a zebra fish, compared with a blank, in which the black V-shaped spot area of the head of the zebra fish treated with the pearl shell melanin inhibiting peptide is obviously reduced in the back view, the black spot of the abdomen is reduced in the side view, and the fish body is transparent compared with the blank. From fig. 5B, it can be seen that the melanin content of the marfish treated with the pearl oyster melanin inhibiting peptide was significantly reduced (p < 0.05) as compared with that of the blank group. At concentrations of 10, 50 and 200 μg/mL, the melanin content in zebra fish was reduced by 25.53%, 37.44% and 38.52% compared to the blank component, respectively. This indicates that the pearl shell melanin inhibiting peptide exhibits good melanin inhibiting ability. At concentrations of 10, 50 and 200 μg/mL, the pearl oyster melanin inhibiting peptide treated groups reduced melanin content by 10.95%, 14.88% and 14.58% respectively, compared to the positive control Group (GSH) at the same concentration, indicating that the pearl oyster melanin inhibiting peptide exhibited a stronger melanin inhibiting effect than the positive control (GSH).
As shown in fig. 6, the results of the enzyme activity measurement show that compared with the blank group, the pearl shell melanin inhibiting peptide can significantly reduce tyrosinase activity (p < 0.05) in zebra fish. Under the treatment of the pearl oyster melanin inhibiting peptide with the concentration of 10, 50 and 200 mug/mL, the activity of the zebra fish tyrosinase is respectively reduced by 39.52 percent, 47.97 percent and 62.87 percent compared with a blank group, and simultaneously is respectively reduced by 8.83 percent, 12.94 percent and 26.42 percent compared with a positive control Group (GSH) with the same concentration. This indicates that the pearl oyster melanin inhibiting peptide exhibits good tyrosinase inhibiting ability, and the tyrosinase inhibiting ability of the pearl oyster melanin inhibiting peptide is significantly better than GSH (p < 0.05). The results show that the pearl shell melanin inhibiting peptide has good tyrosinase inhibiting activity on a zebra fish model, and can reduce melanin generation amount by inhibiting the enzyme activity, thereby achieving the whitening effect.
It is to be understood that the above examples of the present invention are provided by way of illustration only and not by way of limitation of the embodiments of the present invention. Other variations or modifications of the above teachings will be apparent to those of ordinary skill in the art. It is not necessary here nor is it exhaustive of all embodiments. Any modification, equivalent replacement, improvement, etc. which come within the spirit and principles of the invention are desired to be protected by the following claims.
Claims (10)
1. A pearl oyster melanin inhibiting peptide with whitening efficacy, which is characterized by having a nucleotide sequence shown in SEQ ID NO: 1.
2. The use of the nacre melanin inhibiting peptide of claim 1 in the preparation of whitening medicine.
3. The use of the nacre melanin inhibiting peptide of claim 2 for preparing a whitening medicine for inhibiting melanin production.
4. The use of the nacre melanin inhibiting peptide of claim 1 in the preparation of cosmetics.
5. The use of the nacre melanin inhibiting peptide of claim 1 in the preparation of functional foods.
6. The use of the nacre melanin inhibiting peptide of claim 1 in the preparation of tyrosinase inhibitors.
7. The use according to claim 6, wherein the nacre melanin inhibiting peptide is used for preparing tyrosinase inhibitors that bind to amino acid residues LYS379, ASP312, LYS376, GLN351, ASP353 and GLU356 of tyrosinase via hydrogen bonds.
8. The use according to claim 6, wherein the nacre melanin inhibiting peptide is used for preparing an inhibitor having tyrosinase monophenolase inhibiting activity and/or tyrosinase diphenolase inhibiting activity.
9. The use according to claim 8, wherein the nacre melanin inhibiting peptide is used for preparing an inhibitor having tyrosinase monophenolase inhibiting activity.
10. The use according to claim 8, wherein the nacre melanin inhibiting peptide is used for preparing an inhibitor having tyrosinase diphenolase inhibitory activity.
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| CN115477686A (en) * | 2022-09-22 | 2022-12-16 | 北海黑珍珠海洋生物科技有限公司 | Pearl oyster active peptide with whitening effect and application thereof |
| CN117106016A (en) * | 2023-09-01 | 2023-11-24 | 海南大学 | Donkey-hide gelatin source tyrosinase inhibitory peptide and application thereof |
| CN117106015A (en) * | 2023-09-01 | 2023-11-24 | 海南大学 | Coconut-derived active peptide and application thereof |
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Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
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| CN115477686A (en) * | 2022-09-22 | 2022-12-16 | 北海黑珍珠海洋生物科技有限公司 | Pearl oyster active peptide with whitening effect and application thereof |
| CN115477686B (en) * | 2022-09-22 | 2024-01-30 | 北海黑珍珠海洋生物科技有限公司 | Pearl shell active peptide with whitening effect and application thereof |
| CN117106016A (en) * | 2023-09-01 | 2023-11-24 | 海南大学 | Donkey-hide gelatin source tyrosinase inhibitory peptide and application thereof |
| CN117106015A (en) * | 2023-09-01 | 2023-11-24 | 海南大学 | Coconut-derived active peptide and application thereof |
| CN117106015B (en) * | 2023-09-01 | 2024-04-26 | 海南大学 | Coconut-derived active peptide and application thereof |
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