CN107118266A - A kind of sericin peptide taken and its preparation and application with α glucoside inhibiting activities - Google Patents
A kind of sericin peptide taken and its preparation and application with α glucoside inhibiting activities Download PDFInfo
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- CN107118266A CN107118266A CN201710239005.3A CN201710239005A CN107118266A CN 107118266 A CN107118266 A CN 107118266A CN 201710239005 A CN201710239005 A CN 201710239005A CN 107118266 A CN107118266 A CN 107118266A
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- Prior art keywords
- ser
- gly
- thr
- asp
- alpha
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- GLQFKOVWXPPFTP-VEVYYDQMSA-N Thr-Arg-Asp Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(O)=O GLQFKOVWXPPFTP-VEVYYDQMSA-N 0.000 description 1
- PQLXHSACXPGWPD-GSSVUCPTSA-N Thr-Asn-Thr Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O PQLXHSACXPGWPD-GSSVUCPTSA-N 0.000 description 1
- LMMDEZPNUTZJAY-GCJQMDKQSA-N Thr-Asp-Ala Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C)C(O)=O LMMDEZPNUTZJAY-GCJQMDKQSA-N 0.000 description 1
- OYTNZCBFDXGQGE-XQXXSGGOSA-N Thr-Gln-Ala Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](C)C(=O)O)N)O OYTNZCBFDXGQGE-XQXXSGGOSA-N 0.000 description 1
- UDQBCBUXAQIZAK-GLLZPBPUSA-N Thr-Glu-Glu Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(O)=O UDQBCBUXAQIZAK-GLLZPBPUSA-N 0.000 description 1
- YOOAQCZYZHGUAZ-KATARQTJSA-N Thr-Leu-Ser Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(O)=O YOOAQCZYZHGUAZ-KATARQTJSA-N 0.000 description 1
- ZSPQUTWLWGWTPS-HJGDQZAQSA-N Thr-Lys-Asp Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(O)=O)C(O)=O ZSPQUTWLWGWTPS-HJGDQZAQSA-N 0.000 description 1
- IVDFVBVIVLJJHR-LKXGYXEUSA-N Thr-Ser-Asp Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(O)=O)C(O)=O IVDFVBVIVLJJHR-LKXGYXEUSA-N 0.000 description 1
- IQPWNQRRAJHOKV-KATARQTJSA-N Thr-Ser-Lys Chemical compound C[C@@H](O)[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@H](C(O)=O)CCCCN IQPWNQRRAJHOKV-KATARQTJSA-N 0.000 description 1
- WPSKTVVMQCXPRO-BWBBJGPYSA-N Thr-Ser-Ser Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(O)=O WPSKTVVMQCXPRO-BWBBJGPYSA-N 0.000 description 1
- IEZVHOULSUULHD-XGEHTFHBSA-N Thr-Ser-Val Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](C(C)C)C(O)=O IEZVHOULSUULHD-XGEHTFHBSA-N 0.000 description 1
- ZMYCLHFLHRVOEA-HEIBUPTGSA-N Thr-Thr-Ser Chemical compound C[C@@H](O)[C@H](N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CO)C(O)=O ZMYCLHFLHRVOEA-HEIBUPTGSA-N 0.000 description 1
- LECUEEHKUFYOOV-ZJDVBMNYSA-N Thr-Thr-Val Chemical compound CC(C)[C@@H](C(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@@H](N)[C@@H](C)O LECUEEHKUFYOOV-ZJDVBMNYSA-N 0.000 description 1
- BGHVVGPELPHRCI-HZTRNQAASA-N Thr-Trp-Trp Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CC1=CNC2=CC=CC=C21)C(=O)N[C@@H](CC3=CNC4=CC=CC=C43)C(=O)O)N)O BGHVVGPELPHRCI-HZTRNQAASA-N 0.000 description 1
- OGOYMQWIWHGTGH-KZVJFYERSA-N Thr-Val-Ala Chemical compound C[C@@H](O)[C@H](N)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](C)C(O)=O OGOYMQWIWHGTGH-KZVJFYERSA-N 0.000 description 1
- KPMIQCXJDVKWKO-IFFSRLJSSA-N Thr-Val-Glu Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(O)=O)C(O)=O KPMIQCXJDVKWKO-IFFSRLJSSA-N 0.000 description 1
- IBBBOLAPFHRDHW-BPUTZDHNSA-N Trp-Asn-Arg Chemical compound C1=CC=C2C(=C1)C(=CN2)C[C@@H](C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](CCCN=C(N)N)C(=O)O)N IBBBOLAPFHRDHW-BPUTZDHNSA-N 0.000 description 1
- QNTBGBCOEYNAPV-CWRNSKLLSA-N Trp-Asn-Pro Chemical compound C1C[C@@H](N(C1)C(=O)[C@H](CC(=O)N)NC(=O)[C@H](CC2=CNC3=CC=CC=C32)N)C(=O)O QNTBGBCOEYNAPV-CWRNSKLLSA-N 0.000 description 1
- WXEQUSQNDDJEDZ-NYVOZVTQSA-N Trp-Trp-Asn Chemical compound C1=CC=C2C(=C1)C(=CN2)C[C@@H](C(=O)N[C@@H](CC3=CNC4=CC=CC=C43)C(=O)N[C@@H](CC(=O)N)C(=O)O)N WXEQUSQNDDJEDZ-NYVOZVTQSA-N 0.000 description 1
- SCCKSNREWHMKOJ-SRVKXCTJSA-N Tyr-Asn-Ser Chemical compound N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(O)=O SCCKSNREWHMKOJ-SRVKXCTJSA-N 0.000 description 1
- SOAUMCDLIUGXJJ-SRVKXCTJSA-N Tyr-Ser-Asn Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(O)=O SOAUMCDLIUGXJJ-SRVKXCTJSA-N 0.000 description 1
- GZWPQZDVTBZVEP-BZSNNMDCSA-N Tyr-Tyr-Asn Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC(N)=O)C(O)=O GZWPQZDVTBZVEP-BZSNNMDCSA-N 0.000 description 1
- NWEGIYMHTZXVBP-JSGCOSHPSA-N Tyr-Val-Gly Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](C(C)C)C(=O)NCC(O)=O NWEGIYMHTZXVBP-JSGCOSHPSA-N 0.000 description 1
- RVGVIWNHABGIFH-IHRRRGAJSA-N Tyr-Val-Ser Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CO)C(O)=O RVGVIWNHABGIFH-IHRRRGAJSA-N 0.000 description 1
- XTAUQCGQFJQGEJ-NHCYSSNCSA-N Val-Gln-Arg Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CCCN=C(N)N)C(=O)O)N XTAUQCGQFJQGEJ-NHCYSSNCSA-N 0.000 description 1
- PWRITNSESKQTPW-NRPADANISA-N Val-Gln-Ser Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CO)C(=O)O)N PWRITNSESKQTPW-NRPADANISA-N 0.000 description 1
- RWOGENDAOGMHLX-DCAQKATOSA-N Val-Lys-Ala Chemical compound C[C@@H](C(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C(C)C)N RWOGENDAOGMHLX-DCAQKATOSA-N 0.000 description 1
- DEGUERSKQBRZMZ-FXQIFTODSA-N Val-Ser-Ala Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(O)=O DEGUERSKQBRZMZ-FXQIFTODSA-N 0.000 description 1
- JXCOEPXCBVCTRD-JYJNAYRXSA-N Val-Tyr-Arg Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CC1=CC=C(C=C1)O)C(=O)N[C@@H](CCCN=C(N)N)C(=O)O)N JXCOEPXCBVCTRD-JYJNAYRXSA-N 0.000 description 1
- NLNCNKIVJPEFBC-DLOVCJGASA-N Val-Val-Glu Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](C(C)C)C(=O)N[C@H](C(O)=O)CCC(O)=O NLNCNKIVJPEFBC-DLOVCJGASA-N 0.000 description 1
- FZNCGRZWXLXZSZ-CIQUZCHMSA-N Voglibose Chemical compound OCC(CO)N[C@H]1C[C@](O)(CO)[C@@H](O)[C@H](O)[C@H]1O FZNCGRZWXLXZSZ-CIQUZCHMSA-N 0.000 description 1
- 230000021736 acetylation Effects 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 108010076324 alanyl-glycyl-glycine Proteins 0.000 description 1
- 108010047495 alanylglycine Proteins 0.000 description 1
- 108010070944 alanylhistidine Proteins 0.000 description 1
- 108010070783 alanyltyrosine Proteins 0.000 description 1
- 239000003888 alpha glucosidase inhibitor Substances 0.000 description 1
- 102000016679 alpha-Glucosidases Human genes 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 239000012491 analyte Substances 0.000 description 1
- 230000000844 anti-bacterial effect Effects 0.000 description 1
- 229940127003 anti-diabetic drug Drugs 0.000 description 1
- 230000003064 anti-oxidating effect Effects 0.000 description 1
- 230000000840 anti-viral effect Effects 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 230000003078 antioxidant effect Effects 0.000 description 1
- 235000006708 antioxidants Nutrition 0.000 description 1
- 108010013835 arginine glutamate Proteins 0.000 description 1
- 108010001271 arginyl-glutamyl-arginine Proteins 0.000 description 1
- 108010068380 arginylarginine Proteins 0.000 description 1
- 108010062796 arginyllysine Proteins 0.000 description 1
- 108010093581 aspartyl-proline Proteins 0.000 description 1
- 125000005605 benzo group Chemical group 0.000 description 1
- 230000023555 blood coagulation Effects 0.000 description 1
- 230000036772 blood pressure Effects 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 150000001722 carbon compounds Chemical class 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- 230000006866 deterioration Effects 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 238000002330 electrospray ionisation mass spectrometry Methods 0.000 description 1
- 239000003480 eluent Substances 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 230000032050 esterification Effects 0.000 description 1
- 238000005886 esterification reaction Methods 0.000 description 1
- 229950003499 fibrin Drugs 0.000 description 1
- 239000002778 food additive Substances 0.000 description 1
- 235000013373 food additive Nutrition 0.000 description 1
- 230000009246 food effect Effects 0.000 description 1
- 235000013376 functional food Nutrition 0.000 description 1
- 239000007789 gas Substances 0.000 description 1
- 230000002496 gastric effect Effects 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 239000003292 glue Substances 0.000 description 1
- 108010042598 glutamyl-aspartyl-glycine Proteins 0.000 description 1
- 229930182470 glycoside Natural products 0.000 description 1
- 150000002338 glycosides Chemical class 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 108010038983 glycyl-histidyl-lysine Proteins 0.000 description 1
- 108010089804 glycyl-threonine Proteins 0.000 description 1
- 108010015792 glycyllysine Proteins 0.000 description 1
- 230000012447 hatching Effects 0.000 description 1
- 108010025306 histidylleucine Proteins 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 230000000640 hydroxylating effect Effects 0.000 description 1
- 201000001421 hyperglycemia Diseases 0.000 description 1
- 230000002218 hypoglycaemic effect Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 238000007689 inspection Methods 0.000 description 1
- 108010044374 isoleucyl-tyrosine Proteins 0.000 description 1
- 125000001449 isopropyl group Chemical group [H]C([H])([H])C([H])(*)C([H])([H])[H] 0.000 description 1
- 108010053037 kyotorphin Proteins 0.000 description 1
- 230000031700 light absorption Effects 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 235000012054 meals Nutrition 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 235000020124 milk-based beverage Nutrition 0.000 description 1
- 230000003387 muscular Effects 0.000 description 1
- 229920005615 natural polymer Polymers 0.000 description 1
- 108010084572 phenylalanyl-valine Proteins 0.000 description 1
- 108010012581 phenylalanylglutamate Proteins 0.000 description 1
- 229910052698 phosphorus Inorganic materials 0.000 description 1
- 239000011574 phosphorus Substances 0.000 description 1
- 230000007180 physiological regulation Effects 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000013094 purity test Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 239000013049 sediment Substances 0.000 description 1
- 229940039354 sericin 1 Drugs 0.000 description 1
- 108010007375 seryl-seryl-seryl-arginine Proteins 0.000 description 1
- 229910000077 silane Inorganic materials 0.000 description 1
- 210000000813 small intestine Anatomy 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 108010072986 threonyl-seryl-lysine Proteins 0.000 description 1
- 108010051110 tyrosyl-lysine Proteins 0.000 description 1
- 229960001729 voglibose Drugs 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/43504—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates
- C07K14/43563—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates from insects
- C07K14/43586—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from invertebrates from insects from silkworms
-
- 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
- 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
- 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
- Y02P—CLIMATE CHANGE MITIGATION TECHNOLOGIES IN THE PRODUCTION OR PROCESSING OF GOODS
- Y02P20/00—Technologies relating to chemical industry
- Y02P20/50—Improvements relating to the production of bulk chemicals
- Y02P20/55—Design of synthesis routes, e.g. reducing the use of auxiliary or protecting groups
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Toxicology (AREA)
- Tropical Medicine & Parasitology (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Biochemistry (AREA)
- Insects & Arthropods (AREA)
- Mycology (AREA)
- Nutrition Science (AREA)
- Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
Abstract
The invention discloses a kind of sericin peptide taken with α glucoside inhibiting activities, the sequence such as SEQ ID No of sericin peptide taken:Shown in 1；The invention further relates to a kind of synthetically prepared and its biological activity application of the sericin peptide taken with α glucoside inhibiting activities simultaneously.The sericin peptide taken that the present invention is provided is significant to the food, health products and medicine for developing food, health products and medicine and exploitation treatment diabetes B with drop postprandial blood sugar.
Description
Technical field
The present invention relates to biotechnology field of polypeptide preparation, more particularly to a kind of silk gum with alpha-glucoside inhibiting activity
Peptide and its preparation and application.
Background technology
Biologically active peptide is as sanatory bioactive ingredients, with a variety of body metabolisms and physiological regulation function,
It is easy to digest to absorb, there are the effects such as immune promotion, hormone control, antibacterial, antiviral, lowering blood pressure and blood fat, be current international food
The function factor of the popular research topic in boundary and great development prospect.Various active peptides are used for frequently as functional food adding ingredient
The practice production of food or medicine, particularly has been achieved with well in the application aspect of milk beverage, food additives, health food
Effect.
In recent years, as the improvement of people's living standards, the trend risen year by year is just presented in the incidence of diabetes.Its
In, diabetes B is the principal mode of diabetes, and cardinal symptom is that postprandial blood sugar content is higher.In modem medical practices, it is
The further deterioration of control diabetes, it is also main to control based on postprandial blood sugar content.Alpha-glucosidase is used for positioned at small intestine
By the enzyme that carbon compound decomposition is glucose, hence in so that blood-sugar content is raised.By the activity for suppressing alpha-glucosidase so that form sediment
The speed that powder class is decomposed into glucose slows down, so as to slow down the absorption of glucose in enteron aisle, reduces postprandial hyperglycemia, to reach
Treat the purpose of diabetes.The alpha-glucosidase inhibitor class antidiabetic drug clinically applied at present mainly has acarbose and Fu Ge
Array wave sugar, for reducing postprandial blood sugar content.But, acarbose and voglibose can all cause a certain degree of abdominal distension to be arranged
The gastrointestinal reactions such as gas, while hepar damnification can be caused if long-term taking.
Sericin is the natural polymer fibrin extracted from silk, and content accounts for the 70%~80% of silk.
With the development of medical biotechnology, sericin, especially sericin or sericin peptide taken have been widely used in new work(
Can property material.Sericin peptide taken is added in food, there is significant anti-oxidation efficacy；Meanwhile, the reducing blood lipid of sericin peptide taken, hypotensive, drop blood
The function such as sugared, anti-tampon and blood coagulation and enhancing muscular energy is by wide coverage.It is can be found that according to current progress
Sericin peptide taken has a great application value in terms of anti-oxidant, hypoglycemic, hypotensive, therefore sericin peptide taken and its with identical biological living
Property derivative polypeptide produce in enormous quantities technology of preparing turn into health food and biological medicine research direction.
Therefore, those skilled in the art is directed to exploitation a kind of sericin peptide taken and its system with alpha-glucoside inhibiting activity
It is standby with application.
The content of the invention
In view of the drawbacks described above of prior art, the technical problems to be solved by the invention are to provide a kind of with α-glucosides
The sericin peptide taken of enzyme inhibition activity and its preparation and application.
To achieve the above object, the first aspect of the invention provides a kind of silk gum with alpha-glucoside inhibiting activity
Peptide.
In a preferred embodiment, the sericin peptide taken that should have alpha-glucoside inhibiting activity includes following sequence (SEQ
ID No:1)：SEDSSEVDIDLGN, i.e. Ser Glu Asp Ser Ser Glu Val Asp Ile Asp Leu Gly Asn.
Alternatively, on the amino acid side groups of above-mentioned sericin peptide taken, aminoterminal or c-terminus carry out hydroxylating, carboxylated,
Be carbonylated, methylate, acetylation, phosphorylation, esterification or glycosylation modified.
Further, the above-mentioned sericin peptide taken source with alpha-glucoside inhibiting activity is sericin.
Further, the above-mentioned sericin peptide taken with alpha-glucoside inhibiting activity derives from sericin (Protein:
Sericin 1,Organism:Bombyx mori (Silk moth)), and be sericin (SEQ ID NO:The 490th 2)~
The amino acid residue of 502.
Further, the above-mentioned sericin peptide taken with alpha-glucoside inhibiting activity has external alpha-glucoside inhibiting activity.
Further, the above-mentioned sericin peptide taken with alpha-glucoside inhibiting activity can be by the method and chemistry of genetic engineering
Method is artificial synthesized, can also from silk by isolating and purifying, enzyme degraded method obtain.
The second aspect of the present invention provides the preparation method of above-mentioned sericin peptide taken.In a preferred embodiment, the system
The step of Preparation Method, is as follows：
(1) amino resins for weighing n equivalents is put into reactor, adds dichloromethane (DCM) and is swelled, then takes out DCM, with
Activation is stand-by；
(2) first amino acid is connected：First amino acid of 2n equivalents in sequence is added, DCM, dimethyl formyl is added
The diisopropylethylamine (DIEA) of amine (DMF) and 2n equivalents, nitrogen bubble reaction.Then methanol is added, 30min is reacted, takes out
Fall reaction solution, with DMF and methanol cleaning；
(3) condensation reaction：Second amino acid of 2n equivalents in sequence, the nitrogen of benzo three of 2n equivalents are added into reactor
Azoles-N, N, N', N'- tetramethylurea hexafluorophosphate (HBTU) and DIEA, wash liquid, ninhydrin inspection off after nitrogen bubble reaction
Survey；
(4) capping：Add pyridine and acetic anhydride is blocked, clean；
(5) Fmoc protection groups are taken off：Addition is raised one's hat liquid, and liquid of raising one's hat is the DFM solution containing 20% hexahydropyridine), reaction of raising one's hat
After slough Fmoc blocking groups, then clean, ninhydrin detection；
(6) amino acid different in sequence are sequentially added according to step (3), (4) and (5) and carries out phosphorylation modification；
(7) cutting liquid cracking polypeptide is added, resin is filtered after concussion；
(8) ether is added into filtrate, the crude product that sequence is obtained after crude product, eccentric cleaning is separated out；
(9) crude product is purified with high-efficient liquid phase chromatogram technology；
(10) after peptide purity reaches more than 99%, carry out secondary prepare and purify, thousand points are separately added into water and acetonitrile
One of phosphoric acid, the impurity such as the trifluoroacetic acid remained to remove in building-up process effectively increases conjunction in phosphate system
Into the bioactivity of peptide, elute and freezed after polypeptide from pillar.
Preferably, amino resins is swelled activation using DCM in step (1), and swelling time is 30min.
Preferably, DCM and DMF additions in step (2), are advisable so that resin can be agitated fully.
Preferably, the blistering reaction time is 60min in step (2).
Preferably, the reaction time is raised one's hat in step (5) for 30min.
Preferably, the modification of diversified forms can be carried out by being sequentially added in step (6) after amino acid different in sequence, from
And change the protein conformation of the sericin peptide taken of synthesis, and then change its biological activity.
Preferably, the volume components ratio of cutting liquid described in step (7) is trifluoroacetic acid (TFA)：Dithioglycol：Three isopropyls
Base silane (TIS)：H2O=95:2:2:1；Described clipping time is 1-4h.
Preferably, step 9) in efficient liquid phase technology use Kromasil 100-5C18 posts；Mobile phase A, B are respectively
The acetonitrile solution of the 0.1%TFA aqueous solution and 0.1%TFA；Sample size is 10 μ L；Carry out
15%-48%B phases obtain gradient elution.
The third aspect of the invention provides the application of above-mentioned sericin peptide taken.
Above-mentioned application is the application in food, health products and the medicine for preparing alpha-glucosidase activity or drop postprandial blood sugar.
The fourth aspect of the invention provides a kind of bioactive substance for suppressing alpha-glucosidase activity, and it is included as above
The described sericin peptide taken with alpha-glucoside inhibiting activity.
The medicine of suppression alpha-glucosidase activity can be hypoglycemic drug after the meal.
The sericin peptide taken with alpha-glucoside inhibiting activity that the present invention is provided has good suppression alpha-glucosidase activity,
IC500.39mg/mL can be reached, can reach reduction postprandial blood sugar effect, to develop with treatment diabetes B food,
Health products and medicine tool are of great significance and application value.
The technique effect of design and the generation of the present invention is described further below with reference to accompanying drawing, to be fully understood from
The purpose of the present invention, feature and effect.
Brief description of the drawings
Fig. 1 is the HPLC elution collection of illustrative plates of synthesis polypeptide；
Fig. 2 is the ESI-MS collection of illustrative plates of synthesis polypeptide；
Fig. 3 is the relative activity that synthesis polypeptide suppresses to alpha-glucosidase.
Embodiment
Before the specific embodiment of the invention is further described, it should be appreciated that protection scope of the present invention is not limited to down
Belong to specific specific embodiment；It is also understood that the term used in the embodiment of the present invention is specific specific in order to describe
Embodiment, the protection domain being not intended to be limiting of the invention.
Unless otherwise defined, all technologies and scientific terminology that are used in the present invention and those skilled in the art of the present technique are usual
The meaning of understanding is identical.In addition to the specific method used in embodiment, equipment, material, according to those skilled in the art
Grasp to prior art and the record of the present invention, can also be used in method described in the embodiment of the present invention, equipment, material
Any method, equipment and the material of similar or equivalent prior art realizes the present invention.
Unless otherwise indicated, disclosed in this invention experimental method, detection method, preparation method using this technology lead
The conventional molecular biology in domain, biochemistry, the routine techniques of analytical chemistry and association area.
Embodiment 1
It is prepared by a kind of sericin peptide taken with alpha-glucoside inhibiting activity：
Wherein, the sericin peptide taken with alpha-glucoside inhibiting activity has such as SEQ ID No:Amino acid sequence shown in 1.Its
Preparation process is as follows：
(1) n equivalent resins are weighed and are put into reactor, DCM is added and is swelled half an hour, then take out DCM, add in sequence
First amino acid 2n equivalent, plus 2n equivalents DIEA, appropriate DMF, DCM (refers to resin can be made fully to agitate in right amount
It is advisable), nitrogen bubble reaction 60min.Then add the methanol of about 5n equivalents, react half an hour, take out reaction solution, with DMF,
MEOH is cleaned；
(2) toward second amino acid (being also 2n equivalents), 2n equivalent HBTU and DIEA, nitrogen in addition sequence in reactor
Blistering reaction half an hour, wash liquid off, then ninhydrin detection is blocked with pyridine and acetic anhydride.Finally clean, add in right amount
DFM solution containing 20% hexahydropyridine removes Fmoc protection groups, cleans, ninhydrin detection；
(3) amino acid different in sequence are sequentially added according to the mode of step (2)；
(4) remove, pour into flask from reaction column after resin is dried up with nitrogen, then toward in flask plus a certain amount of
Cutting liquid (ratio of cutting liquid and resin is about with 10mL/g ratio), the volume components ratio of the cutting liquid is trifluoroacetic acid
(TFA)：Dithioglycol：Tri isopropyl silane (TIS)：H2O=95:2:2:1；Cut and shaken after 2h, filter resin；
(5) filtrate is obtained, a large amount of ether are then added into filtrate, crude product is separated out, is then centrifuged for, cleaning is i.e. available
The crude product of sequence；
(6) crude product is purified to by the method for high performance liquid chromatography and requires purity, and be converted into phosphate system, because
Added for phosphate and eliminate the impurity such as the trifluoroacetic acid remained in building-up process, synthesis is effectively increased in phosphate system
The bioactivity of peptide.
Embodiment 2
Synthesize elution and the purity testing of sericin peptide taken：
Take and synthesize complete peptide crude product a little, with the 10% acetonitrile solution sample dissolution containing 0.1% (v/v) TFA, dissolved
Cheng Hou, takes 10 μ L sample introductions into Kromasil 100-5C18 chromatographic columns, is respectively the 0.1%TFA aqueous solution using mobile phase A, B
The gradient elution of 15%-48%B phases is carried out with the eluent of 0.1%TFA acetonitrile solutions.As shown in figure 1, the silk that the present invention is synthesized
Glue peptide molecule size is 1379.36Da eluting peak, and its retention time is 7.752min.
Take main elution peak sample to carry out mass spectroscopy, contained according to required molecular weight analyte 1379.36 and main peak relative area
Amount determines sample purity, as shown in Fig. 2 the sericin peptide taken that the present invention is synthesized is reachable by the purity for purifying the sericin peptide taken synthesized
To 99.11%.
After peptide purity reaches more than 99%, carry out secondary prepare and purify, it is each in water and acetonitrile solution to add 0.1% phosphorus
Acid, elutes polypeptide from pillar, then freezes and obtains the synthetic peptide sterling without trifluoroacetic acid.
Embodiment 3
Synthesize sericin peptide taken and suppress alpha-glucosidase determination of activity：
Reagent：Alpha-glucosidase (EC 3.2.1.20,19.3units/mg) from saccharomyces cerevisiae be purchased from U.S. Sigma-
Aldrich；PNPG (p- nitrobenzene-β-D- synthesis) is purchased from U.S. Sigma-Aldrich；Other reagents
It is that analysis is pure；The biologically active polypeptide synthesized in embodiment 1.
Experimental principle：Alpha-glucosaccharase enzymatic pNPG produces p-nitrophenol, there is characteristic absorption peak at 405nm, because
We utilize dynamics/ultraviolet absorption peak of time software measure at 405nm of ultraviolet specrophotometer for this, so as to pass through number
Word shows that the biologically active polypeptide synthesized in embodiment 1 suppresses the effect of alpha-glucosidase.
At 37 DEG C, in pH6.8 phosphate (0.05mol/L) buffer system, 200 μ L alpha-glucosidases (0.175U/
Ml) and after the hatching of the μ L sericin peptide takens of various concentrations 100 30min, plus 200 μ LpNPG (10mmol/L), surveyed every 60s at 405nm
Determine the change of light absorption value, 20min is determined altogether, and alpha-glucosidase activity is estimated by following equation：
Formula：Relative activity (%)=(R/R0) × 100%.
Wherein R0The slope of absorbance change during for without inhibitor, R is in the system containing various concentrations sericin peptide taken
The slope of middle absorbance change.
The sericin peptide taken of table 1 suppresses alpha-glucosidase Activity Results
Suppress alpha-glucosidase activity to synthesis sericin peptide taken by the above method to be determined, it is found that it has and suppress to live
Property, specific IC50(mg/mL) value is shown in Table 1.
Alpha-glucosidase relative activity and sericin peptide taken relation with contents are illustrated in figure 3, with the rise of silk gum peptide content, α-sugar
Glycosides enzyme relative activity is gradually reduced.Show that sericin peptide taken has higher alpha-glucosidase rejection ability, its IC50It can reach
0.39mg/mL。
Preferred embodiment of the invention described in detail above.It should be appreciated that the ordinary skill of this area is without wound
The property made work just can make many modifications and variations according to the design of the present invention.Therefore, all technical staff in the art
Pass through the available technology of logical analysis, reasoning, or a limited experiment on the basis of existing technology under this invention's idea
Scheme, all should be in the protection domain being defined in the patent claims.
Sequence table
<110>Shanghai Communications University
<120>A kind of sericin peptide taken and its preparation and application with alpha-glucoside inhibiting activity
<160> 2
<170> PatentIn version 3.5
<210> 1
<211> 13
<212> PRT
<213>Artificial sequence
<220>
<223>Sericin peptide taken
<400> 1
Ser Glu Asp Ser Ser Glu Val Asp Ile Asp Leu Gly Asn
1 5 10
<210> 2
<211> 1186
<212> PRT
<213>Silkworm moth (Bombyx mori)
<400> 2
Met Arg Phe Val Leu Cys Cys Thr Leu Ile Ala Leu Ala Ala Leu Ser
1 5 10 15
Val Lys Ala Phe Gly His His Pro Gly Asn Arg Asp Thr Val Glu Val
20 25 30
Lys Asn Arg Lys Tyr Asn Ala Ala Ser Ser Glu Ser Ser Tyr Leu Asn
35 40 45
Lys Asp Asn Asp Ser Ile Ser Ala Gly Ala His Arg Ala Lys Ser Val
50 55 60
Glu Gln Ser Gln Asp Lys Ser Lys Tyr Thr Ser Gly Pro Glu Gly Val
65 70 75 80
Ser Tyr Ser Gly Arg Ser Gln Asn Tyr Lys Asp Ser Lys Gln Ala Tyr
85 90 95
Ala Asp Tyr His Ser Asp Pro Asn Gly Gly Ser Ala Ser Ala Gly Gln
100 105 110
Ser Arg Asp Ser Ser Leu Arg Glu Arg Asn Val His Tyr Val Ser Asp
115 120 125
Gly Glu Ala Val Ala Ala Ser Ser Asp Ala Arg Asp Glu Asn Arg Ser
130 135 140
Ala Gln Gln Asn Ala Gln Ala Asn Trp Asn Ala Asp Gly Ser Tyr Gly
145 150 155 160
Val Ser Ala Asp Arg Ser Gly Ser Ala Ser Ser Arg Arg Arg Gln Ala
165 170 175
Asn Tyr Tyr Ser Asp Lys Asp Ile Thr Ala Ala Ser Lys Asp Asp Ser
180 185 190
Arg Ala Asp Ser Ser Arg Arg Ser Asn Ala Tyr Tyr Asn Arg Asp Ser
195 200 205
Asp Gly Ser Glu Ser Ala Gly Leu Ser Asp Arg Ser Ala Ser Ser Ser
210 215 220
Lys Asn Asp Asn Val Phe Val Tyr Arg Thr Lys Asp Ser Ile Gly Gly
225 230 235 240
Gln Ala Lys Ser Ser Arg Ser Ser His Ser Gln Glu Ser Asp Ala Tyr
245 250 255
Tyr Asn Ser Ser Pro Asp Gly Ser Tyr Asn Ala Gly Thr Arg Asp Ser
260 265 270
Ser Ile Ser Asn Lys Lys Lys Ala Ser Ser Thr Ile Tyr Ala Asp Lys
275 280 285
Asp Gln Ile Arg Ala Ala Asn Asp Arg Ser Ser Ser Lys Gln Leu Lys
290 295 300
Gln Ser Ser Ala Gln Ile Ser Ser Gly Pro Glu Gly Thr Ser Val Ser
305 310 315 320
Ser Lys Asp Arg Gln Tyr Ser Asn Asp Lys Arg Ser Lys Ser Asp Ala
325 330 335
Tyr Val Gly Arg Asp Gly Thr Val Ala Tyr Ser Asn Lys Asp Ser Glu
340 345 350
Lys Thr Ser Arg Gln Ser Asn Thr Asn Tyr Ala Asp Gln Asn Ser Val
355 360 365
Arg Ser Asp Ser Ala Ala Ser Asp Gln Thr Ser Lys Ser Tyr Asp Arg
370 375 380
Gly Tyr Ser Asp Lys Asn Ile Val Ala His Ser Ser Gly Ser Arg Gly
385 390 395 400
Ser Gln Asn Gln Lys Ser Ser Ser Tyr Arg Ala Asp Lys Asp Gly Phe
405 410 415
Ser Ser Ser Thr Asn Thr Glu Lys Ser Lys Phe Ser Ser Ser Asn Ser
420 425 430
Val Val Glu Thr Ser Asp Gly Ala Ser Ala Ser Arg Glu Ser Ser Ala
435 440 445
Glu Asp Thr Lys Ser Ser Asn Ser Asn Val Gln Ser Asp Glu Lys Ser
450 455 460
Ala Ser Gln Ser Ser Ser Ser Arg Ser Ser Gln Glu Ser Ala Ser Tyr
465 470 475 480
Ser Ser Ser Ser Ser Ser Ser Thr Leu Ser Glu Asp Ser Ser Glu Val
485 490 495
Asp Ile Asp Leu Gly Asn Leu Gly Trp Trp Trp Asn Ser Asp Asn Lys
500 505 510
Val Gln Arg Ala Ala Gly Gly Ala Thr Lys Ser Gly Ala Ser Ser Ser
515 520 525
Thr Gln Ala Thr Thr Val Ser Gly Ala Asp Asp Ser Ala Asp Ser Tyr
530 535 540
Thr Trp Trp Trp Asn Pro Arg Arg Ser Ser Ser Ser Ser Ser Ser Ala
545 550 555 560
Ser Ser Ser Ser Ser Gly Ser Asn Val Gly Gly Ser Ser Gln Ser Ser
565 570 575
Gly Ser Ser Thr Ser Gly Ser Asn Ala Arg Gly His Leu Gly Thr Val
580 585 590
Ser Ser Thr Gly Ser Thr Ser Asn Thr Asp Ser Ser Ser Lys Ser Ala
595 600 605
Gly Ser Arg Thr Ser Gly Gly Ser Ser Thr Tyr Gly Tyr Ser Ser Ser
610 615 620
His Arg Gly Gly Ser Val Ser Ser Thr Gly Ser Ser Ser Asn Thr Asp
625 630 635 640
Ser Ser Thr Lys Asn Ala Gly Ser Ser Thr Ser Gly Gly Ser Ser Thr
645 650 655
Tyr Gly Tyr Ser Ser Ser His Arg Gly Gly Ser Val Ser Ser Thr Gly
660 665 670
Ser Ser Ser Asn Thr Asp Ser Ser Thr Lys Ser Ala Gly Ser Ser Thr
675 680 685
Ser Gly Gly Ser Ser Thr Tyr Gly Tyr Ser Ser Arg His Arg Gly Gly
690 695 700
Arg Val Ser Ser Thr Gly Ser Ser Ser Thr Thr Asp Ala Ser Ser Asn
705 710 715 720
Ser Val Gly Ser Ser Thr Ser Gly Gly Ser Ser Thr Tyr Gly Tyr Ser
725 730 735
Ser Asn Ser Arg Asp Gly Ser Val Ser Ser Thr Gly Ser Ser Ser Asn
740 745 750
Thr Asp Ser Asn Ser Asn Ser Ala Gly Ser Ser Thr Ser Gly Gly Ser
755 760 765
Ser Thr Tyr Gly Tyr Ser Ser Asn Ser Arg Asp Gly Ser Val Ser Ser
770 775 780
Thr Gly Ser Ser Ser Asn Thr Asp Ser Asn Ser Asn Ser Ala Gly Ser
785 790 795 800
Ser Thr Ser Gly Gly Ser Ser Thr Tyr Gly Tyr Ser Ser Asn Ser Arg
805 810 815
Asp Gly Ser Val Ser Ser Thr Gly Ser Ser Ser Asn Thr Asp Ala Ser
820 825 830
Thr Asp Leu Thr Gly Ser Ser Thr Ser Gly Gly Ser Ser Thr Tyr Gly
835 840 845
Tyr Ser Ser Asp Ser Arg Asp Gly Ser Val Ser Ser Thr Gly Ser Ser
850 855 860
Ser Asn Thr Asp Ala Ser Thr Asp Leu Ala Gly Ser Ser Thr Ser Gly
865 870 875 880
Gly Ser Ser Thr Tyr Gly Tyr Ser Ser Asp Cys Gly Asp Gly Ser Val
885 890 895
Ser Ser Thr Gly Ser Ser Ser Asn Thr Asp Ala Ser Thr Asp Leu Ala
900 905 910
Gly Ser Ser Thr Ser Gly Gly Ser Ser Thr Tyr Gly Tyr Ser Ser Asp
915 920 925
Ser Arg Asp Gly Ser Val Ser Ser Thr Gly Ser Ser Ser Asn Thr Asp
930 935 940
Ala Ser Thr Asp Leu Ala Gly Ser Ser Thr Ser Gly Gly Ser Ser Thr
945 950 955 960
Tyr Gly Tyr Ser Ser Asn Ser Arg Asp Gly Ser Val Ser Ser Thr Gly
965 970 975
Ser Ser Ser Asn Thr Asp Ala Ser Thr Asp Leu Thr Gly Ser Ser Thr
980 985 990
Ser Gly Gly Ser Ser Thr Tyr Gly Tyr Ser Ser Ser Asn Arg Asp Gly
995 1000 1005
Ser Val Leu Ala Thr Gly Ser Ser Ser Asn Thr Asp Ala Ser Thr
1010 1015 1020
Thr Glu Glu Ser Thr Thr Ser Ala Gly Ser Ser Thr Glu Gly Tyr
1025 1030 1035
Ser Ser Ser Ser His Asp Gly Ser Val Thr Ser Thr Asp Gly Ser
1040 1045 1050
Ser Thr Ser Gly Gly Ala Ser Ser Ser Ser Ala Ser Thr Ala Lys
1055 1060 1065
Ser Asp Ala Ala Ser Ser Glu Asp Gly Phe Trp Trp Trp Asn Arg
1070 1075 1080
Arg Lys Ser Gly Ser Gly His Lys Ser Ala Thr Val Gln Ser Ser
1085 1090 1095
Thr Thr Asp Lys Thr Ser Thr Asp Ser Ala Ser Ser Thr Asp Ser
1100 1105 1110
Thr Ser Ser Thr Ser Gly Ala Ser Thr Thr Thr Ser Gly Ser Ser
1115 1120 1125
Ser Thr Ser Gly Gly Ser Ser Thr Ser Asp Ala Ser Ser Thr Ser
1130 1135 1140
Ser Ser Val Ser Arg Ser His His Ser Gly Val Asn Arg Leu Leu
1145 1150 1155
His Lys Pro Gly Gln Gly Lys Ile Cys Leu Cys Phe Glu Asn Ile
1160 1165 1170
Phe Asp Ile Pro Tyr His Leu Arg Lys Asn Ile Gly Val
1175 1180 1185
Claims (10)
1. a kind of sericin peptide taken with alpha-glucoside inhibiting activity, it is characterised in that described has alpha-glucoside inhibiting activity
Sericin peptide taken amino acid sequence such as SEQ ID No:Shown in 1.
2. a kind of preparation method of the sericin peptide taken as claimed in claim 1 with alpha-glucoside inhibiting activity, it is characterised in that
Comprise the following steps：
1) amino resins for weighing n equivalents is put into reactor, adds dichloromethane and is swelled, then takes out dichloromethane, activation is treated
With；
2) first amino acid is connected：First amino acid in the sequence of 2n equivalents is added, dichloromethane, dimethyl formyl is added
The diisopropylethylamine of amine and 2n equivalents, nitrogen bubble reaction, then adds methanol, reacts 30min, takes out reaction solution, uses
Dimethylformamide and methanol cleaning；
3) condensation reaction：Second amino acid, the BTA-N, N, N', N'- of 2n equivalents in sequence are added into reactor
Tetramethylurea hexafluorophosphate and diisopropylethylamine, wash liquid, ninhydrin detection off after nitrogen bubble reaction；
4) capping：Add pyridine and acetic anhydride is blocked, clean；
5) Fmoc protection groups are taken off：Addition is raised one's hat liquid, and liquid of raising one's hat is the dimethyl formamide solution containing 20% hexahydropyridine, is raised one's hat anti-
Should after slough Fmoc blocking groups, then clean, ninhydrin detection；
6) according to step 3), the 4) amino acid different in sequence with 5) sequentially adding；
7) cutting liquid cracking polypeptide is added, resin is filtered after concussion；
8) ether is added into filtrate, the crude product that sequence is obtained after crude product, eccentric cleaning is separated out；
9) crude product is purified with high-efficient liquid phase chromatogram technology；
10) it is secondary to prepare purifying, when peptide purity is more than 99%, millesimal phosphoric acid is separately added into water and acetonitrile, from post
Polypeptide is eluted in son, is then freezed.
3. preparation method as claimed in claim 2, it is characterised in that step 1) described in amino resins use dichloromethane
Activation is swelled, swelling time is 30min.
4. preparation method as claimed in claim 2, it is characterised in that step 2) described in dichloromethane and dimethyl formyl
Amine addition, is advisable so that resin can be agitated fully.
5. preparation method as claimed in claim 2, it is characterised in that step 2) described in the nitrogen bubble reaction time be
60min。
6. preparation method as claimed in claim 2, it is characterised in that step 5) described in reaction time of raising one's hat for 30min.
7. preparation method as claimed in claim 2, it is characterised in that step 7) described in the volume components ratio of cutting liquid be three
Fluoroacetic acid：Dithioglycol：Tri isopropyl silane：H2O=95:2:2:1；Described clipping time is 1-4h.
8. preparation method as claimed in claim 2, it is characterised in that step 9) described in efficient liquid phase technology use
Kromasil 100-5C18 posts；Mobile phase A, B are respectively the 0.1%TFA aqueous solution and 0.1%TFA acetonitrile solution；Sample size
For 10 μ L；Carry out 15%-48%B phases and obtain gradient elution.
9. a kind of application of the sericin peptide taken as claimed in claim 1 with alpha-glucoside inhibiting activity, it is characterised in that described
Using for prepare suppress alpha-glucosidase activity or drop postprandial blood sugar food, health products and medicine in application.
10. a kind of bioactive substance for suppressing alpha-glucosidase activity, it is characterised in that the bioactive substance is included as weighed
Profit requires the sericin peptide taken with alpha-glucoside inhibiting activity described in 1.
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Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN110179127A (en) * | 2019-06-25 | 2019-08-30 | 南通大学 | A kind of nutrition fortifier and preparation method promoting iron zinc calcium uptake |
| CN112194715A (en) * | 2020-11-03 | 2021-01-08 | 西南大学 | Anti-inflammatory sericin peptide and application thereof |
| CN112225791A (en) * | 2020-11-03 | 2021-01-15 | 西南大学 | Sericin peptide and application thereof |
| CN112300258A (en) * | 2020-11-03 | 2021-02-02 | 西南大学 | Anti-inflammatory sericin peptide and application thereof |
| CN114113376A (en) * | 2021-11-10 | 2022-03-01 | 广东一方制药有限公司 | Bombyx Batryticatus characteristic polypeptide and identification method of Bombyx Batryticatus, Bombyx Batryticatus water extract product and other Bombyx Batryticatus products |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| KR20020064085A (en) * | 2001-01-31 | 2002-08-07 | (주)샘스텍 | Blood sugar regulating agent which comprises sericin-peptide from cocoons of Bombyx mori as an effective component and method thereof |
-
2017
- 2017-04-13 CN CN201710239005.3A patent/CN107118266A/en active Pending
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| KR20020064085A (en) * | 2001-01-31 | 2002-08-07 | (주)샘스텍 | Blood sugar regulating agent which comprises sericin-peptide from cocoons of Bombyx mori as an effective component and method thereof |
Non-Patent Citations (2)
| Title |
|---|
| YUWEN FANG 等: "The kinetics and mechanism of α-glucosidase inhibition by F5-SP, a novel compound derived from sericin peptides", 《ROYAL SOCIETY OF CHEMISTRY》 * |
| 于烽 等: "α-促黑激素的固相合成研究", 《现代生物医学进展》 * |
Cited By (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN110179127A (en) * | 2019-06-25 | 2019-08-30 | 南通大学 | A kind of nutrition fortifier and preparation method promoting iron zinc calcium uptake |
| CN110179127B (en) * | 2019-06-25 | 2022-04-22 | 南通大学 | Nutrient supplement for promoting absorption of iron, zinc and calcium and preparation method thereof |
| CN112194715A (en) * | 2020-11-03 | 2021-01-08 | 西南大学 | Anti-inflammatory sericin peptide and application thereof |
| CN112225791A (en) * | 2020-11-03 | 2021-01-15 | 西南大学 | Sericin peptide and application thereof |
| CN112300258A (en) * | 2020-11-03 | 2021-02-02 | 西南大学 | Anti-inflammatory sericin peptide and application thereof |
| CN112225791B (en) * | 2020-11-03 | 2021-10-22 | 西南大学 | Sericin peptide and application thereof |
| CN114113376A (en) * | 2021-11-10 | 2022-03-01 | 广东一方制药有限公司 | Bombyx Batryticatus characteristic polypeptide and identification method of Bombyx Batryticatus, Bombyx Batryticatus water extract product and other Bombyx Batryticatus products |
| CN114113376B (en) * | 2021-11-10 | 2023-08-29 | 广东一方制药有限公司 | Method for identifying characteristic polypeptide of stiff silkworm, water extract product of stiff silkworm and other stiff silkworm products |
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