CN107903313A - A kind of biologically active polypeptide GLNYYQQKPVAL and its preparation method and application - Google Patents
A kind of biologically active polypeptide GLNYYQQKPVAL and its preparation method and application Download PDFInfo
- Publication number
- CN107903313A CN107903313A CN201711122919.8A CN201711122919A CN107903313A CN 107903313 A CN107903313 A CN 107903313A CN 201711122919 A CN201711122919 A CN 201711122919A CN 107903313 A CN107903313 A CN 107903313A
- Authority
- CN
- China
- Prior art keywords
- glnyyqqkpval
- biologically active
- active polypeptide
- polypeptide
- derivative
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Withdrawn
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 132
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 109
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 104
- 238000002360 preparation method Methods 0.000 title claims abstract description 13
- 230000003064 anti-oxidating effect Effects 0.000 claims abstract description 28
- 235000013305 food Nutrition 0.000 claims abstract description 20
- 230000036541 health Effects 0.000 claims abstract description 18
- 150000001413 amino acids Chemical group 0.000 claims abstract description 14
- 239000003814 drug Substances 0.000 claims abstract description 14
- 230000003005 anti-senility effect Effects 0.000 claims abstract description 3
- 238000000034 method Methods 0.000 claims description 34
- 239000000047 product Substances 0.000 claims description 22
- 230000003078 antioxidant effect Effects 0.000 claims description 20
- 239000003963 antioxidant agent Substances 0.000 claims description 18
- 235000006708 antioxidants Nutrition 0.000 claims description 18
- 230000003712 anti-aging effect Effects 0.000 claims description 14
- 238000007254 oxidation reaction Methods 0.000 claims description 14
- 235000013336 milk Nutrition 0.000 claims description 12
- 239000008267 milk Substances 0.000 claims description 12
- 210000004080 milk Anatomy 0.000 claims description 12
- 230000003647 oxidation Effects 0.000 claims description 11
- 230000008859 change Effects 0.000 claims description 7
- 239000012634 fragment Substances 0.000 claims description 7
- 230000021736 acetylation Effects 0.000 claims description 6
- 238000006640 acetylation reaction Methods 0.000 claims description 6
- 230000032050 esterification Effects 0.000 claims description 6
- 238000005886 esterification reaction Methods 0.000 claims description 6
- 230000013595 glycosylation Effects 0.000 claims description 6
- 238000006206 glycosylation reaction Methods 0.000 claims description 6
- 230000000640 hydroxylating effect Effects 0.000 claims description 6
- 230000026731 phosphorylation Effects 0.000 claims description 6
- 238000006366 phosphorylation reaction Methods 0.000 claims description 6
- 108090000623 proteins and genes Proteins 0.000 claims description 6
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 5
- 239000002537 cosmetic Substances 0.000 claims description 5
- 239000002773 nucleotide Substances 0.000 claims description 4
- 125000003729 nucleotide group Chemical group 0.000 claims description 4
- 239000003795 chemical substances by application Substances 0.000 claims description 3
- 238000003786 synthesis reaction Methods 0.000 claims description 3
- 241000005787 Cistanche Species 0.000 claims description 2
- 239000002253 acid Substances 0.000 claims description 2
- 125000002915 carbonyl group Chemical group [*:2]C([*:1])=O 0.000 claims description 2
- 235000013365 dairy product Nutrition 0.000 claims description 2
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 claims 1
- 230000001035 methylating effect Effects 0.000 claims 1
- 238000002474 experimental method Methods 0.000 abstract description 28
- 230000000694 effects Effects 0.000 abstract description 16
- 150000003254 radicals Chemical class 0.000 abstract description 10
- 230000032683 aging Effects 0.000 abstract description 7
- 102000004190 Enzymes Human genes 0.000 abstract description 5
- 108090000790 Enzymes Proteins 0.000 abstract description 5
- 238000000338 in vitro Methods 0.000 abstract description 3
- XZLLTYBONVKGLO-SDDRHHMPSA-N Gln-Lys-Pro Chemical compound C1C[C@@H](N(C1)C(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(=O)N)N)C(=O)O XZLLTYBONVKGLO-SDDRHHMPSA-N 0.000 abstract description 2
- IUZGUFAJDBHQQV-YUMQZZPRSA-N Gly-Leu-Asn Chemical compound NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(O)=O IUZGUFAJDBHQQV-YUMQZZPRSA-N 0.000 abstract description 2
- DJSYPCWZPNHQQE-FHWLQOOXSA-N Tyr-Tyr-Gln Chemical compound C([C@H](N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CCC(N)=O)C(O)=O)C1=CC=C(O)C=C1 DJSYPCWZPNHQQE-FHWLQOOXSA-N 0.000 abstract description 2
- 230000003035 anti-peroxidant effect Effects 0.000 abstract description 2
- 230000036259 sexual stimuli Effects 0.000 abstract description 2
- 241000244206 Nematoda Species 0.000 description 54
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 39
- 239000000243 solution Substances 0.000 description 21
- 239000011347 resin Substances 0.000 description 20
- 229920005989 resin Polymers 0.000 description 20
- HHEAADYXPMHMCT-UHFFFAOYSA-N dpph Chemical compound [O-][N+](=O)C1=CC([N+](=O)[O-])=CC([N+]([O-])=O)=C1[N]N(C=1C=CC=CC=1)C1=CC=CC=C1 HHEAADYXPMHMCT-UHFFFAOYSA-N 0.000 description 18
- 238000005516 engineering process Methods 0.000 description 14
- 239000007788 liquid Substances 0.000 description 11
- 241000894006 Bacteria Species 0.000 description 10
- 239000003153 chemical reaction reagent Substances 0.000 description 9
- 230000017448 oviposition Effects 0.000 description 9
- 238000012216 screening Methods 0.000 description 9
- 239000006228 supernatant Substances 0.000 description 9
- 102000002322 Egg Proteins Human genes 0.000 description 8
- 108010000912 Egg Proteins Proteins 0.000 description 8
- 238000006243 chemical reaction Methods 0.000 description 8
- 238000001514 detection method Methods 0.000 description 8
- 230000012010 growth Effects 0.000 description 8
- 210000004681 ovum Anatomy 0.000 description 8
- 230000004083 survival effect Effects 0.000 description 8
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 8
- YMWUJEATGCHHMB-UHFFFAOYSA-N Dichloromethane Chemical compound ClCCl YMWUJEATGCHHMB-UHFFFAOYSA-N 0.000 description 7
- 238000005119 centrifugation Methods 0.000 description 7
- 229910000359 iron(II) sulfate Inorganic materials 0.000 description 7
- 230000031700 light absorption Effects 0.000 description 7
- 238000012545 processing Methods 0.000 description 7
- WFDIJRYMOXRFFG-UHFFFAOYSA-N Acetic anhydride Chemical compound CC(=O)OC(C)=O WFDIJRYMOXRFFG-UHFFFAOYSA-N 0.000 description 6
- 241000588724 Escherichia coli Species 0.000 description 6
- 239000007853 buffer solution Substances 0.000 description 6
- 230000006378 damage Effects 0.000 description 6
- 238000007689 inspection Methods 0.000 description 6
- 150000003053 piperidines Chemical class 0.000 description 6
- 239000000843 powder Substances 0.000 description 6
- 230000008569 process Effects 0.000 description 6
- 229920001817 Agar Polymers 0.000 description 5
- 108010076119 Caseins Proteins 0.000 description 5
- 102000011632 Caseins Human genes 0.000 description 5
- GLEVLJDDWXEYCO-UHFFFAOYSA-N Trolox Chemical compound O1C(C)(C(O)=O)CCC2=C1C(C)=C(C)C(O)=C2C GLEVLJDDWXEYCO-UHFFFAOYSA-N 0.000 description 5
- 239000008272 agar Substances 0.000 description 5
- 238000004458 analytical method Methods 0.000 description 5
- 239000005018 casein Substances 0.000 description 5
- 238000002376 fluorescence recovery after photobleaching Methods 0.000 description 5
- 235000015097 nutrients Nutrition 0.000 description 5
- 230000036542 oxidative stress Effects 0.000 description 5
- 238000011160 research Methods 0.000 description 5
- 108010077544 Chromatin Proteins 0.000 description 4
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 4
- IMQLKJBTEOYOSI-GPIVLXJGSA-N Inositol-hexakisphosphate Chemical compound OP(O)(=O)O[C@H]1[C@H](OP(O)(O)=O)[C@@H](OP(O)(O)=O)[C@H](OP(O)(O)=O)[C@H](OP(O)(O)=O)[C@@H]1OP(O)(O)=O IMQLKJBTEOYOSI-GPIVLXJGSA-N 0.000 description 4
- IMQLKJBTEOYOSI-UHFFFAOYSA-N Phytic acid Natural products OP(O)(=O)OC1C(OP(O)(O)=O)C(OP(O)(O)=O)C(OP(O)(O)=O)C(OP(O)(O)=O)C1OP(O)(O)=O IMQLKJBTEOYOSI-UHFFFAOYSA-N 0.000 description 4
- 210000003483 chromatin Anatomy 0.000 description 4
- 230000034994 death Effects 0.000 description 4
- 238000004519 manufacturing process Methods 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 4
- 230000004048 modification Effects 0.000 description 4
- 238000012986 modification Methods 0.000 description 4
- 229940068041 phytic acid Drugs 0.000 description 4
- 235000002949 phytic acid Nutrition 0.000 description 4
- 239000000467 phytic acid Substances 0.000 description 4
- 239000013641 positive control Substances 0.000 description 4
- 125000003088 (fluoren-9-ylmethoxy)carbonyl group Chemical group 0.000 description 3
- BDNKZNFMNDZQMI-UHFFFAOYSA-N 1,3-diisopropylcarbodiimide Chemical compound CC(C)N=C=NC(C)C BDNKZNFMNDZQMI-UHFFFAOYSA-N 0.000 description 3
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- 241000244203 Caenorhabditis elegans Species 0.000 description 3
- 241000238631 Hexapoda Species 0.000 description 3
- 238000010521 absorption reaction Methods 0.000 description 3
- 238000003556 assay Methods 0.000 description 3
- 230000001580 bacterial effect Effects 0.000 description 3
- 238000004061 bleaching Methods 0.000 description 3
- 239000007844 bleaching agent Substances 0.000 description 3
- 238000004587 chromatography analysis Methods 0.000 description 3
- 235000020247 cow milk Nutrition 0.000 description 3
- 238000005520 cutting process Methods 0.000 description 3
- 238000004042 decolorization Methods 0.000 description 3
- BGRWYRAHAFMIBJ-UHFFFAOYSA-N diisopropylcarbodiimide Natural products CC(C)NC(=O)NC(C)C BGRWYRAHAFMIBJ-UHFFFAOYSA-N 0.000 description 3
- 235000013601 eggs Nutrition 0.000 description 3
- 230000002708 enhancing effect Effects 0.000 description 3
- 239000012530 fluid Substances 0.000 description 3
- 230000008014 freezing Effects 0.000 description 3
- 238000007710 freezing Methods 0.000 description 3
- 210000004349 growth plate Anatomy 0.000 description 3
- 210000002429 large intestine Anatomy 0.000 description 3
- 150000002632 lipids Chemical class 0.000 description 3
- 238000002156 mixing Methods 0.000 description 3
- FEMOMIGRRWSMCU-UHFFFAOYSA-N ninhydrin Chemical compound C1=CC=C2C(=O)C(O)(O)C(=O)C2=C1 FEMOMIGRRWSMCU-UHFFFAOYSA-N 0.000 description 3
- 230000000474 nursing effect Effects 0.000 description 3
- 150000002978 peroxides Chemical class 0.000 description 3
- 235000018102 proteins Nutrition 0.000 description 3
- 102000004169 proteins and genes Human genes 0.000 description 3
- BAZAXWOYCMUHIX-UHFFFAOYSA-M sodium perchlorate Chemical compound [Na+].[O-]Cl(=O)(=O)=O BAZAXWOYCMUHIX-UHFFFAOYSA-M 0.000 description 3
- 229910001488 sodium perchlorate Inorganic materials 0.000 description 3
- 230000001954 sterilising effect Effects 0.000 description 3
- 238000004659 sterilization and disinfection Methods 0.000 description 3
- 238000004704 ultra performance liquid chromatography Methods 0.000 description 3
- 239000011534 wash buffer Substances 0.000 description 3
- 239000012224 working solution Substances 0.000 description 3
- GVJHHUAWPYXKBD-UHFFFAOYSA-N (±)-α-Tocopherol Chemical compound OC1=C(C)C(C)=C2OC(CCCC(C)CCCC(C)CCCC(C)C)(C)CCC2=C1C GVJHHUAWPYXKBD-UHFFFAOYSA-N 0.000 description 2
- KMVWNDHKTPHDMT-UHFFFAOYSA-N 2,4,6-tripyridin-2-yl-1,3,5-triazine Chemical compound N1=CC=CC=C1C1=NC(C=2N=CC=CC=2)=NC(C=2N=CC=CC=2)=N1 KMVWNDHKTPHDMT-UHFFFAOYSA-N 0.000 description 2
- 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 2
- 108020004414 DNA Proteins 0.000 description 2
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
- 108090001005 Interleukin-6 Proteins 0.000 description 2
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 2
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 2
- 102100040247 Tumor necrosis factor Human genes 0.000 description 2
- CUTSCJHLMGPBEJ-UHFFFAOYSA-N [N].CN(C)C=O Chemical compound [N].CN(C)C=O CUTSCJHLMGPBEJ-UHFFFAOYSA-N 0.000 description 2
- 108010044940 alanylglutamine Proteins 0.000 description 2
- 125000000539 amino acid group Chemical group 0.000 description 2
- 230000000903 blocking effect Effects 0.000 description 2
- 235000019282 butylated hydroxyanisole Nutrition 0.000 description 2
- 238000011088 calibration curve Methods 0.000 description 2
- 235000021240 caseins Nutrition 0.000 description 2
- 210000004027 cell Anatomy 0.000 description 2
- 201000010099 disease Diseases 0.000 description 2
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 2
- 238000000605 extraction Methods 0.000 description 2
- 235000019253 formic acid Nutrition 0.000 description 2
- 230000007760 free radical scavenging Effects 0.000 description 2
- 108010050848 glycylleucine Proteins 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 2
- 230000033001 locomotion Effects 0.000 description 2
- 230000004792 oxidative damage Effects 0.000 description 2
- 230000035790 physiological processes and functions Effects 0.000 description 2
- 230000001681 protective effect Effects 0.000 description 2
- 230000002000 scavenging effect Effects 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- 238000010183 spectrum analysis Methods 0.000 description 2
- 239000007921 spray Substances 0.000 description 2
- 230000035882 stress Effects 0.000 description 2
- 230000009747 swallowing Effects 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 230000035922 thirst Effects 0.000 description 2
- 235000021246 κ-casein Nutrition 0.000 description 2
- MZOFCQQQCNRIBI-VMXHOPILSA-N (3s)-4-[[(2s)-1-[[(2s)-1-[[(1s)-1-carboxy-2-hydroxyethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-3-[[2-[[(2s)-2,6-diaminohexanoyl]amino]acetyl]amino]-4-oxobutanoic acid Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](N)CCCCN MZOFCQQQCNRIBI-VMXHOPILSA-N 0.000 description 1
- WIXDSJRJFDWTNY-UHFFFAOYSA-N 1,3-ditert-butyl-5-methylbenzene Chemical class CC1=CC(C(C)(C)C)=CC(C(C)(C)C)=C1 WIXDSJRJFDWTNY-UHFFFAOYSA-N 0.000 description 1
- KVWLTGNCJYDJET-LSJOCFKGSA-N Ala-Arg-His Chemical compound C[C@@H](C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@@H](CC1=CN=CN1)C(=O)O)N KVWLTGNCJYDJET-LSJOCFKGSA-N 0.000 description 1
- NINQYGGNRIBFSC-CIUDSAMLSA-N Ala-Lys-Ser Chemical compound NCCCC[C@H](NC(=O)[C@@H](N)C)C(=O)N[C@@H](CO)C(O)=O NINQYGGNRIBFSC-CIUDSAMLSA-N 0.000 description 1
- IYKVSFNGSWTTNZ-GUBZILKMSA-N Ala-Val-Arg Chemical compound C[C@H](N)C(=O)N[C@@H](C(C)C)C(=O)N[C@H](C(O)=O)CCCN=C(N)N IYKVSFNGSWTTNZ-GUBZILKMSA-N 0.000 description 1
- QCTOLCVIGRLMQS-HRCADAONSA-N Arg-Tyr-Pro Chemical compound C1C[C@@H](N(C1)C(=O)[C@H](CC2=CC=C(C=C2)O)NC(=O)[C@H](CCCN=C(N)N)N)C(=O)O QCTOLCVIGRLMQS-HRCADAONSA-N 0.000 description 1
- QPTAGIPWARILES-AVGNSLFASA-N Asn-Gln-Phe Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC1=CC=CC=C1)C(O)=O QPTAGIPWARILES-AVGNSLFASA-N 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- BVFQOPGFOQVZTE-ACZMJKKPSA-N Cys-Gln-Ala Chemical compound [H]N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](C)C(O)=O BVFQOPGFOQVZTE-ACZMJKKPSA-N 0.000 description 1
- 241000255581 Drosophila <fruit fly, genus> Species 0.000 description 1
- 241000255601 Drosophila melanogaster Species 0.000 description 1
- GHASVSINZRGABV-UHFFFAOYSA-N Fluorouracil Chemical compound FC1=CNC(=O)NC1=O GHASVSINZRGABV-UHFFFAOYSA-N 0.000 description 1
- MADFVRSKEIEZHZ-DCAQKATOSA-N Gln-Gln-Lys Chemical compound C(CCN)C[C@@H](C(=O)O)NC(=O)[C@H](CCC(=O)N)NC(=O)[C@H](CCC(=O)N)N MADFVRSKEIEZHZ-DCAQKATOSA-N 0.000 description 1
- ZQPOVSJFBBETHQ-CIUDSAMLSA-N Gln-Glu-Gln Chemical compound [H]N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(N)=O)C(O)=O ZQPOVSJFBBETHQ-CIUDSAMLSA-N 0.000 description 1
- FTIJVMLAGRAYMJ-MNXVOIDGSA-N Gln-Ile-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@@H](N)CCC(N)=O FTIJVMLAGRAYMJ-MNXVOIDGSA-N 0.000 description 1
- LTUVYLVIZHJCOQ-KKUMJFAQSA-N Glu-Arg-Phe Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC1=CC=CC=C1)C(O)=O LTUVYLVIZHJCOQ-KKUMJFAQSA-N 0.000 description 1
- ALCAUWPAMLVUDB-FXQIFTODSA-N Glu-Gln-Asn Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O ALCAUWPAMLVUDB-FXQIFTODSA-N 0.000 description 1
- GXMXPCXXKVWOSM-KQXIARHKSA-N Glu-Ile-Pro Chemical compound CC[C@H](C)[C@@H](C(=O)N1CCC[C@@H]1C(=O)O)NC(=O)[C@H](CCC(=O)O)N GXMXPCXXKVWOSM-KQXIARHKSA-N 0.000 description 1
- CUPSDFQZTVVTSK-GUBZILKMSA-N Glu-Lys-Asp Chemical compound OC(=O)C[C@@H](C(O)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)CCC(O)=O CUPSDFQZTVVTSK-GUBZILKMSA-N 0.000 description 1
- JWNZHMSRZXXGTM-XKBZYTNZSA-N Glu-Ser-Thr Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(O)=O JWNZHMSRZXXGTM-XKBZYTNZSA-N 0.000 description 1
- GZUKEVBTYNNUQF-WDSKDSINSA-N Gly-Ala-Gln Chemical compound NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCC(N)=O)C(O)=O GZUKEVBTYNNUQF-WDSKDSINSA-N 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- LVXFNTIIGOQBMD-SRVKXCTJSA-N His-Leu-Ser Chemical compound [H]N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(O)=O LVXFNTIIGOQBMD-SRVKXCTJSA-N 0.000 description 1
- UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 description 1
- NCSIQAFSIPHVAN-IUKAMOBKSA-N Ile-Asn-Thr Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H]([C@@H](C)O)C(=O)O)N NCSIQAFSIPHVAN-IUKAMOBKSA-N 0.000 description 1
- HTDRTKMNJRRYOJ-SIUGBPQLSA-N Ile-Gln-Tyr Chemical compound CC[C@H](C)[C@H](N)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(O)=O)CC1=CC=C(O)C=C1 HTDRTKMNJRRYOJ-SIUGBPQLSA-N 0.000 description 1
- KLBVGHCGHUNHEA-BJDJZHNGSA-N Ile-Leu-Ala Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)O)N KLBVGHCGHUNHEA-BJDJZHNGSA-N 0.000 description 1
- 108010055461 Ile-Pro-Pro-Lys-Lys-Asn-Gln-Asp-Lys-Thr-Glu Proteins 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 108010065920 Insulin Lispro Proteins 0.000 description 1
- 108090000978 Interleukin-4 Proteins 0.000 description 1
- WXHFZJFZWNCDNB-KKUMJFAQSA-N Leu-Asn-Tyr Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(O)=O)CC1=CC=C(O)C=C1 WXHFZJFZWNCDNB-KKUMJFAQSA-N 0.000 description 1
- HFBCHNRFRYLZNV-GUBZILKMSA-N Leu-Glu-Asp Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(O)=O HFBCHNRFRYLZNV-GUBZILKMSA-N 0.000 description 1
- USLNHQZCDQJBOV-ZPFDUUQYSA-N Leu-Ile-Asn Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(N)=O)C(O)=O USLNHQZCDQJBOV-ZPFDUUQYSA-N 0.000 description 1
- UCXQIIIFOOGYEM-ULQDDVLXSA-N Leu-Pro-Tyr Chemical compound CC(C)C[C@H](N)C(=O)N1CCC[C@H]1C(=O)N[C@H](C(O)=O)CC1=CC=C(O)C=C1 UCXQIIIFOOGYEM-ULQDDVLXSA-N 0.000 description 1
- KZZCOWMDDXDKSS-CIUDSAMLSA-N Leu-Ser-Asn Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(O)=O KZZCOWMDDXDKSS-CIUDSAMLSA-N 0.000 description 1
- QWWPYKKLXWOITQ-VOAKCMCISA-N Leu-Thr-Leu Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@H](C(O)=O)CC(C)C QWWPYKKLXWOITQ-VOAKCMCISA-N 0.000 description 1
- SLQJJFAVWSZLBL-BJDJZHNGSA-N Lys-Ile-Ala Chemical compound OC(=O)[C@H](C)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@@H](N)CCCCN SLQJJFAVWSZLBL-BJDJZHNGSA-N 0.000 description 1
- BOJYMMBYBNOOGG-DCAQKATOSA-N Lys-Pro-Ala Chemical compound [H]N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)N[C@@H](C)C(O)=O BOJYMMBYBNOOGG-DCAQKATOSA-N 0.000 description 1
- IMDJSVBFQKDDEQ-MGHWNKPDSA-N Lys-Tyr-Ile Chemical compound CC[C@H](C)[C@@H](C(=O)O)NC(=O)[C@H](CC1=CC=C(C=C1)O)NC(=O)[C@H](CCCCN)N IMDJSVBFQKDDEQ-MGHWNKPDSA-N 0.000 description 1
- CRVSHEPROQHVQT-AVGNSLFASA-N Met-Met-Lys Chemical compound CSCC[C@@H](C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCCN)C(=O)O)N CRVSHEPROQHVQT-AVGNSLFASA-N 0.000 description 1
- 101100001708 Mus musculus Angptl4 gene Proteins 0.000 description 1
- JGFZNNIVVJXRND-UHFFFAOYSA-N N,N-Diisopropylethylamine (DIPEA) Chemical compound CCN(C(C)C)C(C)C JGFZNNIVVJXRND-UHFFFAOYSA-N 0.000 description 1
- SITLTJHOQZFJGG-UHFFFAOYSA-N N-L-alpha-glutamyl-L-valine Natural products CC(C)C(C(O)=O)NC(=O)C(N)CCC(O)=O SITLTJHOQZFJGG-UHFFFAOYSA-N 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- SZYBZVANEAOIPE-UBHSHLNASA-N Phe-Met-Ala Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](C)C(O)=O SZYBZVANEAOIPE-UBHSHLNASA-N 0.000 description 1
- XDMMOISUAHXXFD-SRVKXCTJSA-N Phe-Ser-Asp Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(O)=O)C(O)=O XDMMOISUAHXXFD-SRVKXCTJSA-N 0.000 description 1
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 1
- YTWNSIDWAFSEEI-RWMBFGLXSA-N Pro-His-Pro Chemical compound C1C[C@H](NC1)C(=O)N[C@@H](CC2=CN=CN2)C(=O)N3CCC[C@@H]3C(=O)O YTWNSIDWAFSEEI-RWMBFGLXSA-N 0.000 description 1
- SOACYAXADBWDDT-CYDGBPFRSA-N Pro-Ile-Arg Chemical compound [H]N1CCC[C@H]1C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O SOACYAXADBWDDT-CYDGBPFRSA-N 0.000 description 1
- WHNJMTHJGCEKGA-ULQDDVLXSA-N Pro-Phe-Leu Chemical compound [H]N1CCC[C@H]1C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CC(C)C)C(O)=O WHNJMTHJGCEKGA-ULQDDVLXSA-N 0.000 description 1
- RFWXYTJSVDUBBZ-DCAQKATOSA-N Pro-Pro-Glu Chemical compound OC(=O)CC[C@@H](C(O)=O)NC(=O)[C@@H]1CCCN1C(=O)[C@H]1NCCC1 RFWXYTJSVDUBBZ-DCAQKATOSA-N 0.000 description 1
- RMJZWERKFFNNNS-XGEHTFHBSA-N Pro-Thr-Ser Chemical compound [H]N1CCC[C@H]1C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CO)C(O)=O RMJZWERKFFNNNS-XGEHTFHBSA-N 0.000 description 1
- GZNYIXWOIUFLGO-ZJDVBMNYSA-N Pro-Thr-Thr Chemical compound [H]N1CCC[C@H]1C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O GZNYIXWOIUFLGO-ZJDVBMNYSA-N 0.000 description 1
- XDKKMRPRRCOELJ-GUBZILKMSA-N Pro-Val-Ala Chemical compound OC(=O)[C@H](C)NC(=O)[C@H](C(C)C)NC(=O)[C@@H]1CCCN1 XDKKMRPRRCOELJ-GUBZILKMSA-N 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 208000034189 Sclerosis Diseases 0.000 description 1
- MIJWOJAXARLEHA-WDSKDSINSA-N Ser-Gly-Glu Chemical compound OC[C@H](N)C(=O)NCC(=O)N[C@H](C(O)=O)CCC(O)=O MIJWOJAXARLEHA-WDSKDSINSA-N 0.000 description 1
- RRVFEDGUXSYWOW-BZSNNMDCSA-N Ser-Phe-Phe Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CC1=CC=CC=C1)C(O)=O RRVFEDGUXSYWOW-BZSNNMDCSA-N 0.000 description 1
- ADJDNJCSPNFFPI-FXQIFTODSA-N Ser-Pro-Ala Chemical compound OC(=O)[C@H](C)NC(=O)[C@@H]1CCCN1C(=O)[C@@H](N)CO ADJDNJCSPNFFPI-FXQIFTODSA-N 0.000 description 1
- BSXKBOUZDAZXHE-CIUDSAMLSA-N Ser-Pro-Glu Chemical compound [H]N[C@@H](CO)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(O)=O)C(O)=O BSXKBOUZDAZXHE-CIUDSAMLSA-N 0.000 description 1
- FHXGMDRKJHKLKW-QWRGUYRKSA-N Ser-Tyr-Gly Chemical compound OC[C@H](N)C(=O)N[C@H](C(=O)NCC(O)=O)CC1=CC=C(O)C=C1 FHXGMDRKJHKLKW-QWRGUYRKSA-N 0.000 description 1
- BLRPTPMANUNPDV-UHFFFAOYSA-N Silane Chemical compound [SiH4] BLRPTPMANUNPDV-UHFFFAOYSA-N 0.000 description 1
- 102000019197 Superoxide Dismutase Human genes 0.000 description 1
- 108010012715 Superoxide dismutase Proteins 0.000 description 1
- VGYBYGQXZJDZJU-XQXXSGGOSA-N Thr-Glu-Ala Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(O)=O VGYBYGQXZJDZJU-XQXXSGGOSA-N 0.000 description 1
- XOWKUMFHEZLKLT-CIQUZCHMSA-N Thr-Ile-Ala Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](C)C(O)=O XOWKUMFHEZLKLT-CIQUZCHMSA-N 0.000 description 1
- PAXANSWUSVPFNK-IUKAMOBKSA-N Thr-Ile-Asn Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CC(=O)N)C(=O)O)NC(=O)[C@H]([C@@H](C)O)N PAXANSWUSVPFNK-IUKAMOBKSA-N 0.000 description 1
- GVMXJJAJLIEASL-ZJDVBMNYSA-N Thr-Pro-Thr Chemical compound C[C@@H](O)[C@H](N)C(=O)N1CCC[C@H]1C(=O)N[C@@H]([C@@H](C)O)C(O)=O GVMXJJAJLIEASL-ZJDVBMNYSA-N 0.000 description 1
- RVMNUBQWPVOUKH-HEIBUPTGSA-N Thr-Ser-Thr Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(O)=O RVMNUBQWPVOUKH-HEIBUPTGSA-N 0.000 description 1
- QNXZCKMXHPULME-ZNSHCXBVSA-N Thr-Val-Pro Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](C(C)C)C(=O)N1CCC[C@@H]1C(=O)O)N)O QNXZCKMXHPULME-ZNSHCXBVSA-N 0.000 description 1
- ATJFFYVFTNAWJD-UHFFFAOYSA-N Tin Chemical compound [Sn] ATJFFYVFTNAWJD-UHFFFAOYSA-N 0.000 description 1
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical class OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 1
- JLTQXEOXIJMCLZ-ZVZYQTTQSA-N Trp-Gln-Val Chemical compound C1=CC=C2C(C[C@H](N)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](C(C)C)C(O)=O)=CNC2=C1 JLTQXEOXIJMCLZ-ZVZYQTTQSA-N 0.000 description 1
- MWUYSCVVPVITMW-IGNZVWTISA-N Tyr-Tyr-Ala Chemical compound C([C@@H](C(=O)N[C@@H](C)C(O)=O)NC(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=C(O)C=C1 MWUYSCVVPVITMW-IGNZVWTISA-N 0.000 description 1
- SLLKXDSRVAOREO-KZVJFYERSA-N Val-Ala-Thr Chemical compound C[C@H]([C@@H](C(=O)O)NC(=O)[C@H](C)NC(=O)[C@H](C(C)C)N)O SLLKXDSRVAOREO-KZVJFYERSA-N 0.000 description 1
- UZDHNIJRRTUKKC-DLOVCJGASA-N Val-Gln-Val Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](C(C)C)C(=O)O)N UZDHNIJRRTUKKC-DLOVCJGASA-N 0.000 description 1
- VXDSPJJQUQDCKH-UKJIMTQDSA-N Val-Ile-Glu Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)O)NC(=O)[C@H](C(C)C)N VXDSPJJQUQDCKH-UKJIMTQDSA-N 0.000 description 1
- BTWMICVCQLKKNR-DCAQKATOSA-N Val-Leu-Ser Chemical compound CC(C)[C@H]([NH3+])C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C([O-])=O BTWMICVCQLKKNR-DCAQKATOSA-N 0.000 description 1
- JVGDAEKKZKKZFO-RCWTZXSCSA-N Val-Val-Thr Chemical compound C[C@H]([C@@H](C(=O)O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](C(C)C)N)O JVGDAEKKZKKZFO-RCWTZXSCSA-N 0.000 description 1
- 229930003427 Vitamin E Natural products 0.000 description 1
- 208000027418 Wounds and injury Diseases 0.000 description 1
- 240000008042 Zea mays Species 0.000 description 1
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 1
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 230000003679 aging effect Effects 0.000 description 1
- 108010086434 alanyl-seryl-glycine Proteins 0.000 description 1
- 230000002605 anti-dotal effect Effects 0.000 description 1
- 230000006907 apoptotic process Effects 0.000 description 1
- -1 aromatic amino acid Chemical class 0.000 description 1
- 210000001367 artery Anatomy 0.000 description 1
- 108010092854 aspartyllysine Proteins 0.000 description 1
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- UHOVQNZJYSORNB-UHFFFAOYSA-N benzene Substances C1=CC=CC=C1 UHOVQNZJYSORNB-UHFFFAOYSA-N 0.000 description 1
- 230000000975 bioactive effect Effects 0.000 description 1
- 238000005842 biochemical reaction Methods 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 235000010290 biphenyl Nutrition 0.000 description 1
- 239000004305 biphenyl Substances 0.000 description 1
- 230000017531 blood circulation Effects 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
- 229940021722 caseins Drugs 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 238000005352 clarification Methods 0.000 description 1
- 210000003022 colostrum Anatomy 0.000 description 1
- 235000021277 colostrum Nutrition 0.000 description 1
- 238000009833 condensation Methods 0.000 description 1
- 230000005494 condensation Effects 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- 235000005822 corn Nutrition 0.000 description 1
- 239000008367 deionised water Substances 0.000 description 1
- 229910021641 deionized water Inorganic materials 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 235000021245 dietary protein Nutrition 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 229960002949 fluorouracil Drugs 0.000 description 1
- WIGCFUFOHFEKBI-UHFFFAOYSA-N gamma-tocopherol Natural products CC(C)CCCC(C)CCCC(C)CCCC1CCC2C(C)C(O)C(C)C(C)C2O1 WIGCFUFOHFEKBI-UHFFFAOYSA-N 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- LHGVFZTZFXWLCP-UHFFFAOYSA-N guaiacol Chemical class COC1=CC=CC=C1O LHGVFZTZFXWLCP-UHFFFAOYSA-N 0.000 description 1
- 108010085325 histidylproline Proteins 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 229960002163 hydrogen peroxide Drugs 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 229940088592 immunologic factor Drugs 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 208000014674 injury Diseases 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 210000002490 intestinal epithelial cell Anatomy 0.000 description 1
- 210000000936 intestine Anatomy 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 229910052742 iron Inorganic materials 0.000 description 1
- 125000001449 isopropyl group Chemical group [H]C([H])([H])C([H])(*)C([H])([H])[H] 0.000 description 1
- 235000014655 lactic acid Nutrition 0.000 description 1
- 239000004310 lactic acid Substances 0.000 description 1
- 230000003050 macronutrient Effects 0.000 description 1
- 235000021073 macronutrients Nutrition 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 238000001819 mass spectrum Methods 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 230000035764 nutrition Effects 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 230000004783 oxidative metabolism Effects 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 230000000737 periodic effect Effects 0.000 description 1
- 108010073025 phenylalanylphenylalanine Proteins 0.000 description 1
- ZUOUZKKEUPVFJK-UHFFFAOYSA-N phenylbenzene Natural products C1=CC=CC=C1C1=CC=CC=C1 ZUOUZKKEUPVFJK-UHFFFAOYSA-N 0.000 description 1
- 230000000770 proinflammatory effect Effects 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000001850 reproductive effect Effects 0.000 description 1
- 201000003068 rheumatic fever Diseases 0.000 description 1
- 239000011435 rock Substances 0.000 description 1
- 238000005070 sampling Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 229910000077 silane Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000012086 standard solution Substances 0.000 description 1
- 210000002784 stomach Anatomy 0.000 description 1
- 238000005728 strengthening Methods 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 229940126680 traditional chinese medicines Drugs 0.000 description 1
- 150000003852 triazoles Chemical class 0.000 description 1
- 108010020532 tyrosyl-proline Proteins 0.000 description 1
- 108010003137 tyrosyltyrosine Proteins 0.000 description 1
- 238000000825 ultraviolet detection Methods 0.000 description 1
- 235000019165 vitamin E Nutrition 0.000 description 1
- 229940046009 vitamin E Drugs 0.000 description 1
- 239000011709 vitamin E Substances 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 239000003643 water by type Substances 0.000 description 1
- 238000005303 weighing Methods 0.000 description 1
- 235000013618 yogurt Nutrition 0.000 description 1
- 235000021247 β-casein Nutrition 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
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4732—Casein
-
- 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
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
- A61Q19/08—Anti-ageing preparations
-
- 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
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Organic Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gerontology & Geriatric Medicine (AREA)
- Mycology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Dermatology (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Toxicology (AREA)
- Medicinal Chemistry (AREA)
- Nutrition Science (AREA)
- Engineering & Computer Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Birds (AREA)
- Epidemiology (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
The present invention relates to albumen field, and in particular to its amino acid sequence of a kind of biologically active polypeptide GLNYYQQKPVAL and its preparation method and application, biologically active polypeptide GLNYYQQKPVAL is Gly Leu Asn Tyr Tyr Gln Gln Lys Pro Val Ala Leu.Tested by antioxidation in vitro, internal Antisenility Experiment, polypeptide GLNYYQQKPVAL is demonstrated with preferable antioxidation biology activity and activity of fighting against senium, on the one hand, the biologically active polypeptide GLNYYQQKPVAL of the present invention has preferable antioxidation activity, free radical that can be in removing machine body, improves the quality of life；On the other hand, the vigor of internal anti-peroxidation enzyme system can be improved, strengthen the function of body resistance external source sexual stimulus, so as to reduce organism aging process, aging and sick probability, exploitation is of great significance with anti-oxidation function, the food of anti-senescence function, health products and medicine tool.
Description
Technical field
The present invention relates to albumen field, more particularly, to a kind of biologically active polypeptide GLNYYQQKPVAL and preparation method thereof
And application.
Background technology
During cow's milk is through lactobacillus-fermented, a part of protein in cow's milk is metabolized by lactic acid bacteria to be utilized, concurrently
A series of biochemical reactions have been given birth to, protein is changed into polypeptide or free amino acid, is digested or passes through
The absorption and transport of intestinal epithelial cell is directly entered the blood circulation of human body.In these polypeptides, some is with special
Physiological function, is referred to as " biologically active peptide ".
It is particularly important that safe biologically active peptide is found in natural food source.In recent years, it has been found that some foods
The polypeptides matter in thing source has good bioactivity, such as corn small peptide, soybean peptide, cow's milk polypeptide.These polypeptides can
To be obtained by number of ways such as microbial fermentation, digestion enzymolysis, and biologically active polypeptide is by 2~20 mostly
Amino acid residue forms, and molecular weight is less than 6000Da, contains a certain amount of hydrophobic amino acid, aromatic amino acid.
Oxidation reaction and oxidative metabolism are all vital for food and human body, and free radical and active oxygen cause
A series of oxidation reaction.When excessive free radical is formed, they can exceed protective enzyme such as superoxide dismutase, peroxide
Change the protective effect of hydrogen enzyme, so as to cause a series of side effect such as lipid oxidation, Apoptosis to produce.This kind of oxidation is anti-
Should, the shelf-life of the food containing fat is not only influenced, certain harm also is caused to the health of human body, such as rheumatic arthritis, sugar
Urinate disease, artery sclerosis etc..In addition, Collins et al. researchs in 2005 find that oxidative damage of the generation of cancer also with DNA has
Close.
Some artificial synthesized antioxidant such as butylated hydroxy anisoles (BHA), 2,6- di-t-butyl -4- methylbenzenes in early days
Phenol (BHT) is applied in food, as the antioxidant of lipid, but these artificial synthesized additives have for human body it is latent
Risk.In the research process of natural, from the anti-oxidation peptide of food proteins become popular research it
One.It is not only safe, is easier to be absorbed and used than macro-nutrients such as protein, and such as calcium, iron can be promoted micro-
The absorption of nutrient is measured, also with preferable antioxidation activity, is had a extensive future.
Aging is a natural phenomena, and process is often accompanied by the change of antioxidant levels, organ-tissue, immune factor, its
The change of complexity, the trend that such as proinflammatory cytokine IL-6, IL-4, TNF-α presentation increase, IL-6 occur for middle cell factor
It is all considered to play an important role in the generating process of geriatric disease with TNF-a.With science of heredity and molecular biology
Development, the research of biological decay mechanism achieve gratifying progress.Researcher by using some model organisms, as mouse,
The term single gene mutating experiment of drosophila and C. Elegans Automatic Screening etc., it is found that some genes can dramatically increase service lifes of these organisms and reach
As many as 6 times.
Anti-aging peptide in terms of physiological function there is amino acid cannot compare excellent as a kind of emerging antidotal agent
Gesture, it can produce promotion or inhibitory action to the enzyme in organism, improve absorption and the profit to mineral matter and other nutrients
With, removing interior free yl, the resistance to oxidation of enhancing body itself, to slow down aging.Therefore, the nutrition and health care of biologically active peptide
Effect has become the emphasis of domestic and foreign scholars' subject study.Qiu Juan et al. pass through experimental studies have found that, milk-derived bioactive micro peptide
Life span of drosophila melanogaster can effectively be extended, delay its aging, and also there is preferable antioxidation, thus it is speculated that be probably wherein to be rich in coloured glaze
Base peptides.SOD vigor in serum, reduces its lipid in discovery bovine colostrum extract energy conspicuousness raising the elderly's body such as the brightness in week
Peroxide and enhancing body resistance to oxidation, have certain anti-senescence function.
The research on biologically active polypeptide has much at present, for example Chinese patent CN105254738A discloses one kind and comes
The milk-derived biologically active polypeptide DELQDKIH of beta-casein is come from, Chinese patent CN105254739A discloses one kind and derives from
The milk-derived biologically active polypeptide GTQYTD of α s1- caseins, Chinese patent CN105254740A, which are disclosed, a kind of derives from α s2-
The milk-derived biologically active polypeptide NQFYQKF of casein.
The content of the invention
It is an object of the invention to provide a kind of biologically active polypeptide GLNYYQQKPVAL and its preparation method and application.
The purpose of the present invention can be achieved through the following technical solutions：
First aspect present invention, there is provided a kind of biologically active polypeptide GLNYYQQKPVAL, its amino acid sequence are Gly-
Leu-Asn-Tyr-Tyr-Gln-Gln-Lys-Pro-Val-Ala-Leu, such as SEQ ID NO：Shown in 1.
Preferably, the biologically active polypeptide is milk-derived.Specific source κ-casein, and be κ-ss-casein variants A
The amino acid residue of the 60th~71.κ-ss-casein variants A amino acid sequences such as SEQ ID NO：Shown in 3.
The amino acid sequence of κ-casein and corresponding nucleotides sequence are classified as existing technology, encode κ-ss-casein variants A
The biologically active polypeptide GLNYYQQKPVAL of the nucleotide fragments energy encoding mature of 60th~71 amino acids residue.
The biologically active polypeptide has anti-oxidation function and anti-senescence function.
Second aspect of the present invention, there is provided the nucleotide fragments of the biologically active polypeptide GLNYYQQKPVAL are encoded, its
Sequence is：5 '-gga ctc aat tac tac caa cag aaa cca gtt gca cta-3 ', such as SEQ ID NO：2 institutes
Show.
Third aspect present invention, there is provided the preparation method of the biologically active polypeptide GLNYYQQKPVAL, can pass through
The method of genetic engineering is artificial synthesized, can be directly obtained, can directly passed through by the method isolated and purified from dairy products
It is prepared by chemical synthesis.
Fourth aspect present invention, there is provided the biologically active polypeptide GLNYYQQKPVAL has anti-oxidation function in preparation
Food, health products, the application in medicine or cosmetics.
Fifth aspect present invention, there is provided the biologically active polypeptide GLNYYQQKPVAL has anti-senescence function in preparation
Food, the application in health products or medicine.
Sixth aspect present invention, there is provided the biologically active polypeptide GLNYYQQKPVAL is being prepared while had anti-oxidant
Application in the food of function and anti-senescence function, health products or medicine.
Specifically, biologically active polypeptide GLNYYQQKPVAL of the invention, which can be used for preparing, reduces free radical to skin
The cosmetics of injury, preparation have anti-oxidant and/or anti-aging medicine；And due to the biologically active polypeptide of the present invention
Product after GLNYYQQKPVAL is degraded by intestines and stomach still has bioactivity, therefore can be also used for preparing the food such as Yoghourt
Product, oxidation-resisting health-care product, and what is taken orally are used to prepare with anti-oxidant and/or anti-aging medicine.
Seventh aspect present invention, there is provided a kind of oxidation resistant product, including the biologically active polypeptide GLNYYQQKPVAL
Or the derivative of the biologically active polypeptide GLNYYQQKPVAL；The oxidation resistant product includes antioxidant food, anti-oxidant
Health products, anti-oxidation medicine or antioxidation cosmetic product；The derivative of the biologically active polypeptide GLNYYQQKPVAL, refers in life
On the amino acid side groups of thing active peptides GLNYYQQKPVAL, aminoterminal or c-terminus carry out hydroxylating, carboxylated, carbonyl
Change, methylate, acetylation, phosphorylation, the modification such as esterification or glycosylation, obtained polypeptide derivative.
Eighth aspect present invention, there is provided a kind of anti-aging product, including the biologically active polypeptide GLNYYQQKPVAL
Or the derivative of the biologically active polypeptide GLNYYQQKPVAL；The anti-aging product includes antisenility cistanche food, anti-aging
Health products or antiaging agent；The derivative of the biologically active polypeptide GLNYYQQKPVAL, refers in biologically active polypeptide
On the amino acid side groups of GLNYYQQKPVAL, aminoterminal or c-terminus carry out hydroxylating, carboxylated, be carbonylated, methylate,
Acetylation, phosphorylation, esterification or glycosylation etc. are modified, obtained polypeptide derivative.
Ninth aspect present invention, there is provided product a kind of while that there is anti-oxidation function and anti-senescence function, including institute
State the derivative of biologically active polypeptide GLNYYQQKPVAL or described biologically active polypeptides GLNYYQQKPVAL；With anti-oxidant work(
It can include food, health products or medicine with the product of anti-senescence function；The derivative of the biologically active polypeptide GLNYYQQKPVAL
Thing, refer on the amino acid side groups of biologically active polypeptide GLNYYQQKPVAL, aminoterminal or c-terminus carry out hydroxylating,
Carboxylated, be carbonylated, methylate, acetylation, phosphorylation, the modification such as esterification or glycosylation, obtained polypeptide derivative.
Biologically active polypeptide GLNYYQQKPVAL's of the present invention has the beneficial effect that：The milk-derived biologically active polypeptide of the present invention
GLNYYQQKPVAL has preferable antioxidation activity and activity of fighting against senium；On the one hand, biologically active polypeptide of the invention
GLNYYQQKPVAL has preferable antioxidation activity, free radical that can be in removing machine body, improves the quality of life；The opposing party
Face, it is possible to increase the vigor of internal anti-peroxidation enzyme system, the function of enhancing body resistance external source sexual stimulus, so that it is old to reduce body
Change, aging and sick probability, to developing with anti-oxidation function, the food of anti-senescence function, health products and medicine with ten
Divide important meaning.
Brief description of the drawings
Fig. 1：Mass chromatography extraction figure (m/z=697.8743)；
Fig. 2：Mass-to-charge ratio is the second order ms figure of 697.8743 fragment；
Fig. 3：Mass-to-charge ratio is 697.8743 polypeptide az, by crack conditions；
Fig. 4：[DPPH] methanol standard curve；
Fig. 5：FeSO4Standard curve；
Fig. 6：Influences of the biologically active polypeptide GLNYYQQKPVAL to C. Elegans Automatic Screening locomitivity；
Fig. 7：Influences of the biologically active polypeptide GLNYYQQKPVAL to the C. Elegans Automatic Screening service life；
Fig. 8：Influences of the biologically active polypeptide GLNYYQQKPVAL to C. Elegans Automatic Screening under oxidative stress.
Embodiment
Before specific embodiments of the present invention are further described, it should be appreciated that protection scope of the present invention is not limited to down
State 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.
When embodiment provides number range, it should be appreciated that except non-invention is otherwise noted, two ends of each number range
Any one numerical value can be selected between point and two endpoints.Unless otherwise defined, in the present invention all technologies for using and
Scientific terminology is identical with the normally understood meaning of those skilled in the art of the present technique.Except used in embodiment specific method, equipment,
Outside material, according to grasp of the those skilled in the art to the prior art and the record of the present invention, it can also use and this
Any method, equipment and the material of the similar or equivalent prior art of method, equipment described in inventive embodiments, material come real
The existing present invention.
Unless otherwise stated, disclosed in this invention experimental method, detection method, preparation method using this technology lead
Molecular biology, biochemistry, chromatin Structure and the analysis of domain routine, analytical chemistry, cell culture, recombinant DNA technology and
The routine techniques of association area.These technologies existing perfect explanation in the prior art, for details, reference can be made to Sambrook etc.
MOLECULAR CLONING：A LABORATORY MANUAL, Second edition, Cold Spring Harbor
Laboratory Press, 1989and Third edition, 2001；Ausubel etc., CURRENT PROTOCOLS IN
MOLECULAR BIOLOGY, John Wiley＆Sons, New York, 1987and periodic updates；the
Series METHODS IN ENZYMOLOGY, Academic Press, San Diego；Wolffe, CHROMATIN
STRUCTURE AND FUNCTION, Third edition, Academic Press, San Diego, 1998；METHODS IN
ENZYMOLOGY, Vol.304, Chromatin (P.M.Wassarman and A.P.Wolffe, eds.), Academic
Press, San Diego, 1999；With METHODS IN MOLECULAR BIOLOGY, Vol.119, Chromatin
Protocols (P.B.Becker, ed.) Humana Press, Totowa, 1999 etc..
The present invention is described in detail with specific embodiment below in conjunction with the accompanying drawings.
1 active peptide GLNYYQQKPVAL's of embodiment is artificial synthesized
First, the synthesis of biologically active peptide
1. RINK resin 3g (substitution value 0.3mmol/g) are weighed in the reactor of 150ml, with the dichloromethane of 50ml
(DCM) soak.
2.2 it is small when after, wash resin with nitrogen-dimethylformamide (DMF) of 3 times of resin volumes, then drain, so weight
It is four times multiple, resin is drained rear stand-by.
3. a certain amount of 20% piperidines (piperidines/DMF=1 is added into reactor:4,v:V), it is placed on decolorization swinging table and shakes
20min is shaken, the Fmoc blocking groups on resin are sloughed with this.Washed four times with the DMF of 3 times of resin volumes after having taken off protection,
Then drain.
4. take the detection of a small amount of resin ninhydrin (nine well ninhydrins) method (each two drop of inspection A, inspection B, 100 DEG C of reactions
1min), resin has color, illustrates to be deprotected successfully.
5. weigh amino acid Gly in right amount and 1- hydroxyls-benzene a pair of horses going side by side triazole (HOBT) is in right amount in the centrifuge tube of 50ml, addition
The DMF of 20ml is dissolved, and then adds the N of 3ml, and N diisopropylcarbodiimide (DIC) vibration shakes up 1min, treats that solution is clear
It is added to after clear in reactor, then reactor is placed in 30 DEG C of shaking table and is reacted.
6.2 it is small when after, with a certain amount of acetic anhydride end socket (acetic anhydride:DIEA:DCM=1:1:2,v:v:V) half an hour, so
Washed four times, drained stand-by with the DMF of 3 times of resin volumes afterwards.
7. a certain amount of 20% piperidines (piperidines/DMF=1 is added into reactor:4, v:V), it is placed on decolorization swinging table and shakes
20min is shaken, the Fmoc blocking groups on resin are sloughed with this.Washed four times with DMF after having taken off protection, then drained.
8. take the detection of a small amount of resin ninhydrin (nine well ninhydrins) method (each two drop of inspection A, inspection B, 100 DEG C of reactions
1min), resin has color, illustrates to be deprotected successfully.
9. weighing second amino acid next in right amount and HOBT being in right amount in the centrifuge tube of 50ml, the DMF generals of 25ml are added
It is dissolved, and the DIC vibrations for then adding 2.5ml shake up 1min, are added to after solution clarification in reactor, then by reactor
It is placed in 30 DEG C of shaking table and reacts.
10.1 it is small when after, take a small amount of resin to detect, (each two drop of inspection A, inspection B, 100 DEG C of reactions detected with ninhydrin method
1min), if resin is colourless, illustrate that the reaction was complete；If resin has color, illustrate that condensation is incomplete, the reaction was continued.
11. after complete reaction, washing resin four times with DMF, then drain, a certain amount of 20% is added into reactor
Piperidines (piperidines/DMF=1:4,v:V), it is placed on decolorization swinging table and rocks 20min, the Fmoc protection groups on resin is sloughed with this
Group.Washed four times with DMF after having taken off protection, then drain whether detection protection sloughs.
12. amino acid Leu, Asn, Tyr, Tyr, Gln, Gln, Lys, Pro, Val, Ala are connected successively according to step 9-11
And Leu.
13. after last amino acid is connected, protection is sloughed, is washed four times with DMF, is then taken out resin with methanol
It is dry.Then with 95 cutting liquid (trifluoroacetic acids:1,2 dithioglycols:3, isopropyl base silane:Water=95:2:2:1, v:v:V) by polypeptide
Cut down from resin (every gram of resin adds 10ml cutting liquids), and with ice ether (cutting liquid：Ether=1:9,v:V) centrifugation is heavy
Drop four times.
So far, artificial synthesized biologically active peptide GLNYYQQKPVAL.
2nd, the confirmation of biologically active peptide
1) UPLC is analyzed
UPLC conditions are as follows：
Instrument：Waters ACQUITY UPLC ultra high efficiency liquid phase-electron spray-level Four bar-time of-flight mass spectrometer
Chromatographic column specification：BEH C18 chromatographic columns
Flow velocity：0.4mL/min
Temperature：50℃
Ultraviolet detection wavelength：210nm
Sample size：2μL
Gradient condition：A liquid：Water containing 0.1% formic acid (v/v), B liquid：Acetonitrile containing 0.1% formic acid (v/v)
2) mass spectral analysis
Mass Spectrometry Conditions are as follows：
Ionic means：ES+
Mass range (m/z)：100-1000
Capillary voltage (Capillary) (kV)：3.0
Sampling spiroid (V)：35.0
Ion source temperature (DEG C)：115
Remove solvent temperature (DEG C)：350
Go solvent stream (L/hr)：700.0
Collision energy (eV)：4.0
Sweep time (sec)：0.25
Interior sweep time (sec)：0.02
According to above analysis method, using ultra high efficiency liquid phase-electron spray-level Four bar-flight time mass spectrum, to bioactivity
Peptide GLNYYQQKPVAL carries out chromatography and mass spectral analysis, its mass chromatography extraction figure is as shown in Figure 1, extract the two level at this peak
As shown in Figures 2 and 3, the polypeptide mass-to-charge ratio that can obtain this peak is 697.8743Da, and retention time is for mass spectrogram and az, by crack conditions
53.0min。
3) result
From the figure 3, it may be seen that situation about being broken according to az, by, calculates by Mascot software analysis, obtains mass-to-charge ratio
697.8743Da fragment sequence be Gly-Leu-Asn-Tyr-Tyr-Gln-Gln-Lys-Pro-Val-Ala-Leu
(GLNYYQQKPVAL), SEQ ID NO are denoted as：1.The fragment is opposite with the residue sequence of κ-ss-casein variants A the 60th~71
Should, the GenBank numberings of κ-casamino acid sequence are AAA30433.1, and sequence is shown in SEQ ID NO：3.
The antioxidation activity experiment of 2 biologically active peptide of embodiment
First, the antioxidation activity in vitro of [DPPH] method measure biologically active peptide GLNYYQQKPVAL
1. experiment reagent and instrument：
Reagent：1,1- diphenyl -2- trinitrophenyl-hydrazines (1,1-Diphenyl-2-picrylhydrazyl [DPPH]),
Japanese Wako companies production；Methanol, Shanghai traditional Chinese medicines company provide；The milk-derived biologically active polypeptide that embodiment 1 obtains
GLNYYQQKPVAL。
Key instrument：Sunrise microplate reader, Austrian Tecan Products；96 porocyte culture plates, the U.S.
Millipore companies manufacture；Assay balance, Meitelei-tolido Products.
2. experimental method：
(1) 1mmol/L [DPPH] methanol solution
0.349mg [DPPH] is weighed with assay balance to be dissolved in 1mL methanol solutions, the 1mmol/L prepared
[DPPH] methanol solution, tinfoil are kept in dark place, i.e., with i.e. use.
(2) measure of [DPPH] methanol standard curve
100 μ L [DPPH] methanol standard curve samples are separately added into by table 1 in 96 orifice plates, are stored at room temperature 90min, are used
Microplate reader detects light absorption value at 517nm.
[DPPH] methanol of table 1 calibration curve solution is prepared
According to experimental result, using Excel matched curves and regression equation is calculated, the result is shown in Fig. 4 (regression equations：Y=-
0.192x+0.2271, R2=0.9991).The linear relationship of [DPPH] methanol standard curve is good, related coefficient 0.999,
Show that [DPPH] methanol standard curve preci-sion and accuracy meets testing requirements.In terms of result, absorbance with
[DPPH] content is in inverse relation, and [DPPH] content is fewer, and light absorption value is higher, i.e. the ability of sample removing free radical is got over
By force.
(3) antioxidation activity of [DPPH] method measure biologically active peptide GLNYYQQKPVAL
1) sample sets：80 μ L concentration are added in 96 orifice plates for 1mmol/L [DPPH] methanol solution, by table 2 respectively to add
Enter the sample to be tested (GLNYYQQKPVAL), positive control 1 (Trolox of 2.5mg/mL), positive control 2 of 20 μ L various concentrations
(Trolox of 0.025mg/mL), and negative control (phytic acid)；
2) blank group：On same 96 orifice plate, to add 80 μ L concentration as 1mmol/L [DPPH] methanol solutions and 20 μ L
The sample of deionized water does blank control.
After detected sample is loaded, 90min is stored at room temperature, light absorption value is detected at 517nm with microplate reader.Under
Formula calculates free radical scavenging activity, and experimental result is shown in Table 2.
Table 2 [DPPH] method measures the antioxidation activity result of biologically active polypeptide
From table 2 it can be seen that the Trolox as the 2.5mg/mL of positive control have under the same conditions it is most strong clear
Except the ability of free radical, free radical all in solution can be almost removed, is secondly the Trolox, phytic acid, work of 0.025mg/mL
Property polypeptide.It is 32.73% that polypeptide GLNYYQQKPVAL, which removes [DPPH] free radical rate, and with GLNYYQQKPVAL concentration
Reduction, Scavenging ability weaken.
2nd, FARP methods measure biologically active peptide GLNYYQQKPVAL antioxidant activity in vitro
1) experiment reagent and instrument
Total antioxidant capacity detection kit (Ferric Reducing Ability of Plasma FRAP methods), is purchased from
The green skies biotechnology company in Shanghai；FeSO4Solution (10mmol/L), watermiscible vitamin E (Trolox solution) (10mmol/
L), the milk-derived biologically active polypeptide GLNYYQQKPVAL that embodiment 1 obtains.
Key instrument：Sunrise microplate reader, Austrian Tecan Products；96 porocyte culture plates, the U.S.
Millipore companies manufacture；Assay balance, Meitelei-tolido Products；HWS26 type electric-heated thermostatic water baths, Shanghai
One permanent Science and Technology Ltd.'s manufacture.
2) experimental method
(1) preparation of FRAP working solutions
According to total antioxidant capacity detection kit, TPTZ 7.5mL dilutions, 750 μ L solution of TPTZ, detection are buffered
750 μ L of liquid are uniformly mixed, and are incubated in 37 DEG C of water-baths, 2 it is small when h in be finished.
(2)FeSO4The making measure of standard curve curve
180 μ LFRAP working solutions are first added in 96 orifice plates, 5 μ L FeSO are added by table 34Calibration curve solution, is gently mixed
It is even, after 37 DEG C are incubated 3-5min, light absorption value is measured at 593nm with microplate reader.
Table 3FeSO4The solution of standard curve determination is prepared
FeSO4Concentration and light absorption value are in good proportional relation, FeSO4Concentration is higher, and light absorption value is higher.FeSO of the present invention4
Standard curve is the result is shown in Fig. 5, and the linear relationship of standard curve is good, related coefficient 0.998, FeSO4The precision of standard curve
Degree and accuracy meet testing requirements, are calculated available for follow-up.
(3) oxidation resistance of FRAP methods measure biologically active polypeptide GLNYYQQKPVAL
180 μ L FRAP working solutions are first added in 96 orifice plates, 5 μ L ddH are added in blank control wells2O, sample detection hole
5 μ L phytic acid are added in 5 μ L samples to be tested of interior addition, positive control, are gently mixed, after 37 DEG C are incubated 3-5min, are existed with microplate reader
Light absorption value is measured at 593nm.Total antioxidant capacity representation is with FeSO4The concentration of standard solution represents.Count according to the following formula
Free radical scavenging activity is calculated, experimental result is shown in Table 4.
The total antioxidant capacity result of table 4FARP methods measure biologically active polypeptide GLNYYQQKPVAL
By total antioxidant capacity method (Ferric Reducing Ability Power FRAP methods) to polypeptide
The external total antioxidant activity of GLNYYQQKPVAL is determined, it is found that it is preferable biologically active polypeptide GLNYYQQKPVAL has
Reduction-oxidation material ability；In the case of concentration is 4mg/mL, the total antioxidation level of polypeptide GLNYYQQKPVAL reaches
0.0218mmol/g；Illustrate the total antioxidant capacity of biologically active polypeptide GLNYYQQKPVAL, higher than having under comparable sodium
The phytic acid of weak antioxidation activity, has conspicuousness (p>0.05) difference.Therefore, the biologically active polypeptide of invention can be assert
GLNYYQQKPVAL has significant oxidation resistance.
The activity of fighting against senium experiment of 3 biologically active peptide of embodiment
First, the experiment that biologically active polypeptide GLNYYQQKPVAL influences C. Elegans Automatic Screening locomitivity
1. experiment reagent and instrument：
Reagent：C. Elegans Automatic Screening (Caenorhabditis elegans), attached Chinese and Western binding institute of Fudan University；Large intestine
Bacterial strain E.coli OP50, attached Chinese and Western binding institute of Fudan University；Agar powder, Sinopharm Chemical Reagent Co., Ltd.；Ferment
Female powder, Sinopharm Chemical Reagent Co., Ltd.；The milk-derived biologically active polypeptide GLNYYQQKPVAL that embodiment 1 obtains.
Instrument and equipment：Power health RO15 pure water systems, Li Kang biologic medicals Science and Technology Ltd.；G136T types Zealway intelligence
High-temperature sterilization pot, Xiamen Zhi Wei instruments Science and Technology Ltd.；THZ-32 type Desk type constant-temperatureoscillator oscillators, Shanghai precision experimental facilities have
Limit company；TDL-40B centrifuges, Anting Scientific Instrument Factory, Shanghai；Lu Xiang instrument GL-22M high speed freezing centrifuges, Shanghai Lu Xiang instrument
Instrument Ltd.；Win fast BJ-CD SERIES Biohazard Safety Equipments, Shanghai Bo Xun Industrial Co., Ltd.s；Nikko is inverted electronic display
Micro mirror, Nikon Corp..
2. experimental method：
(1) prepared by NGM tablets
Taking strain Escherichia coli, picking single bacterium is fallen within 10ml LB fluid nutrient mediums, 37 DEG C in LB plate streakings,
200rpm, shaken cultivation 24h, are used to be inoculated with NGM tablets nursing nematode to OD600=0.4.100 μ L bacterium solutions are taken to be applied to 60mm
NGM tablets, notice that bacterium solution edge should be apart from plate edge 0.5cm or so.The NGM tablets having been coated with are in room temperature (21-25 DEG C) mistake
It can be used after night.
(2) culture of nematodes
Nematode used is hermaphroditic in this experiment, Standard culture conditions (20 DEG C of temperature, humidity 40%~
60%) growth is cultivated under.
(3) the synchronization processing of nematode
1) sodium perchlorate bleaching
Prepare pregnant worm growth plate (more than 80% insect is in reproduction period i.e. in plate) 2-3 plates, take 5ml M9 wash buffers 2
It is secondary, buffer solution is sucked in 15ml centrifuge tubes, 1000r/min centrifugation 3min, supernatant discarding.5ml is added newly to bleach with synchronization
Liquid, acutely vibrates 2.5min, adult polypide is corroded at room temperature.Centrifugation, supernatant discarding.Ensure total processing time no more than
5min, prevents damage worm's ovum.Resuspension will be precipitated by adding M9 buffer solutions, be centrifuged after mixing, supernatant discarding, be repeated this process 3 times.
2) prescribe a time limit oviposition method
Some nematodes in the egg-laying season of picking are in same tablet, and the particular number of picking is with required synchronization nematode
Number is foundation.Under general condition, an egg-laying season nematode can lay eggs 6 or so within 1h.After 0.5h being cultivated in tablet,
Choose nematode in tablet, then the ovum in tablet is in same growth period.
(4) index determining
Experiment packet：Blank group and polypeptide group.Movement velocity and track can reflect whether the growth conditions of nematode are good.
Since the movement locus of nematode is rendered as sinusoidal pattern, and if along non-sinusoidal cuve track move when, show the line
Worm loses moving equilibrium ability, and growth is affected.The nematode of each group synchronization culture is growing to the L4 phases (culture 4 days or so)
When, 40 nematodes of picking to respective NGM tablets, its peak number got within 1min was measured every 2 days respectively, respectively 4 days,
6 days, 8 days, 10 days, 12 days, 14 days, 16 days and 18 days, every group took its average value.
3. experimental result and analysis：
Nematode is counted into its peak number got within 1min since the L4 phases (the 4th day), continuous statistics 14 days, until
18th day (nematode high-volume is dead), can intuitively reflect nematode under different condition of culture to the shadow of its locomitivity
Ring.It can be found that the polypeptide GLNYYQQKPVAL of 300mg/L can improve nematode per minute interior to a certain extent from Fig. 6
The peak number got over, strengthens its locomitivity, will not cause damage to the moving equilibrium ability of nematode.
2nd, experiments of the biologically active polypeptide GLNYYQQKPVAL to C. Elegans Automatic Screening aging effects
1. experiment reagent and instrument：
Reagent：C. Elegans Automatic Screening (Caenorhabditis elegans), attached Chinese and Western binding institute of Fudan University；Large intestine
Bacterial strain E.coli OP50, attached Chinese and Western binding institute of Fudan University；Agar powder, Sinopharm Chemical Reagent Co., Ltd.；Ferment
Female powder, Sinopharm Chemical Reagent Co., Ltd.；5-fluor-uracil, Sigma Co., USA；The milk-derived life that embodiment 1 obtains
Thing active peptides GLNYYQQKPVAL.
Instrument and equipment：Power health RO15 pure water systems, Li Kang biologic medicals Science and Technology Ltd.；G136T types Zealway intelligence
High-temperature sterilization pot, Xiamen Zhi Wei instruments Science and Technology Ltd.；THZ-32 type Desk type constant-temperatureoscillator oscillators, Shanghai precision experimental facilities have
Limit company；TDL-40B centrifuges, Anting Scientific Instrument Factory, Shanghai；Lu Xiang instrument GL-22M high speed freezing centrifuges, Shanghai Lu Xiang instrument
Instrument Ltd.；Win fast BJ-CD SERIES Biohazard Safety Equipments, Shanghai Bo Xun Industrial Co., Ltd.s；Nikko is inverted electronic display
Micro mirror, Nikon Corp..
2. experimental method：
(1) prepared by NGM tablets
Taking strain Escherichia coli, picking single bacterium is fallen within 10ml LB fluid nutrient mediums, 37 DEG C in LB plate streakings,
200rpm, shaken cultivation 24h, are used to be inoculated with NGM tablets nursing nematode to OD600=0.4.100 μ L bacterium solutions are taken to be applied to 60mm
NGM tablets, notice that bacterium solution edge should be apart from plate edge 0.5cm or so.The NGM tablets having been coated with are in room temperature (21-25 DEG C) mistake
It can be used after night.
(2) culture of nematodes
Nematode used is hermaphroditic in this experiment, Standard culture conditions (20 DEG C of temperature, humidity 40%~
60%) growth is cultivated under.
(3) the synchronization processing of nematode
1) sodium perchlorate bleaching
Prepare pregnant worm growth plate (more than 80% insect is in reproduction period i.e. in plate) 2-3 plates, take 5ml M9 wash buffers 2
It is secondary, buffer solution is sucked in 15ml centrifuge tubes, 1000r/min centrifugation 3min, supernatant discarding.5ml is added newly to bleach with synchronization
Liquid, acutely vibrates 2.5min, adult polypide is corroded at room temperature.Centrifugation, supernatant discarding.Ensure total processing time no more than
5min, prevents damage worm's ovum.Resuspension will be precipitated by adding M9 buffer solutions, be centrifuged after mixing, supernatant discarding, be repeated this process 3 times.
2) prescribe a time limit oviposition method
Some nematodes in the egg-laying season of picking are in same tablet, and the particular number of picking is with required synchronization nematode
Number is foundation.Under general condition, an egg-laying season nematode can lay eggs 6 or so within 1h.After 0.5h being cultivated in tablet,
Choose nematode in tablet, then the ovum in tablet is in same growth period.
(4) index determining
Experiment packet：Blank group and polypeptide group.Some of L4 phase nematodes are chosen, after synchronization processing, are respectively placed in corresponding
In NGM plates；Every group of nematode population is no less than 60, is denoted as 0 day, is transferred them to daily in new plate at this time, to the reproduction later stage
Do not retransfer.Record nematode is dead daily and eliminates the bar number of experiment.Wherein contain in each NGM plates of life experiment
12.5mg/L 5-fluor-uracils are to suppress nematode reproduction.Nematode death criterion：Without mobile and swallowing act, after touching still
Without any reaction.Rejecting standard：1. flee to tablet wall or cover and thirst；2. worm's ovum is hatched into bag sample worm in vivo：③
Pierce in agar.
3. experimental result and analysis：
Influences of the 5 biologically active polypeptide GLNYYQQKPVAL of table to the nematode service life
It can be seen from table 5 and Fig. 7 when the mass concentration of feeding polypeptide GLNYYQQKPVAL is 300mg/L, experimental group
The average life span of middle nematode extends about 9.54% respectively, meanwhile, its half death time has even more obtained conspicuousness raising
(P ＜ 0.05), MaLS time also extend 4 days respectively compared to blank group.It is even more to be intuitive to see in Fig. 7, it is identical
At time point, nematode survival rate was extended apparently higher than blank group, nematode service life in experimental group.It is demonstrated experimentally that what experiment used
Peptide masses concentration is suitable.It can effectively delay nematode aging, improve survival rate, and also further demonstrate that polypeptide at the same time
The effect that GLNYYQQKPVAL extends the service life is realized not by nematode reproductive capacity is suppressed, because it has good anti-oxidant work(
Can be with stronger Scavenging ability.
3rd, the Acute oxidative of biologically active polypeptide GLNYYQQKPVAL stress survival experiment
1. experiment reagent and instrument：
Reagent：C. Elegans Automatic Screening (Caenorhabditis elegans), attached Chinese and Western binding institute of Fudan University；Large intestine
Bacterial strain E.coli OP50, attached Chinese and Western binding institute of Fudan University；Agar powder, Sinopharm Chemical Reagent Co., Ltd.；Ferment
Female powder, Sinopharm Chemical Reagent Co., Ltd.；30% hydrogenperoxide steam generator, Sinopharm Chemical Reagent Co., Ltd.；Implement
The milk-derived biologically active polypeptide GLNYYQQKPVAL that example 1 obtains.
Instrument and equipment：Power health RO15 pure water systems, Li Kang biologic medicals Science and Technology Ltd.；G136T types Zealway intelligence
High-temperature sterilization pot, Xiamen Zhi Wei instruments Science and Technology Ltd.；THZ-32 type Desk type constant-temperatureoscillator oscillators, Shanghai precision experimental facilities have
Limit company；TDL-40B centrifuges, Anting Scientific Instrument Factory, Shanghai；Lu Xiang instrument GL-22M high speed freezing centrifuges, Shanghai Lu Xiang instrument
Instrument Ltd.；Win fast BJ-CD SERIES Biohazard Safety Equipments, Shanghai Bo Xun Industrial Co., Ltd.s；Nikko is inverted electronic display
Micro mirror, Nikon Corp..
2. experimental method：
(1) prepared by NGM tablets
Taking strain Escherichia coli, picking single bacterium is fallen within 10ml LB fluid nutrient mediums, 37 DEG C in LB plate streakings,
200rpm, shaken cultivation 24h, are used to be inoculated with NGM tablets nursing nematode to OD600=0.4.100 μ L bacterium solutions are taken to be applied to 60mm
NGM tablets, notice that bacterium solution edge should be apart from plate edge 0.5cm or so.The NGM tablets having been coated with are in room temperature (21-25 DEG C) mistake
It can be used after night.
(2) culture of nematodes
Nematode used is hermaphroditic in this experiment, Standard culture conditions (20 DEG C of temperature, humidity 40%~
60%) growth is cultivated under.
(3) the synchronization processing of nematode
1) sodium perchlorate bleaching
Prepare pregnant worm growth plate (more than 80% insect is in reproduction period i.e. in plate) 2-3 plates, take 5ml M9 wash buffers 2
It is secondary, buffer solution is sucked in 15ml centrifuge tubes, 1000r/min centrifugation 3min, supernatant discarding.5ml is added newly to bleach with synchronization
Liquid, acutely vibrates 2.5min, adult polypide is corroded at room temperature.Centrifugation, supernatant discarding.Ensure total processing time no more than
5min, prevents damage worm's ovum.Resuspension will be precipitated by adding M9 buffer solutions, be centrifuged after mixing, supernatant discarding, be repeated this process 3 times.
2) prescribe a time limit oviposition method
Some nematodes in the egg-laying season of picking are in same tablet, and the particular number of picking is with required synchronization nematode
Number is foundation.Under general condition, an egg-laying season nematode can lay eggs 6 or so within 1h.After 0.5h being cultivated in tablet,
Choose nematode in tablet, then the ovum in tablet is in same growth period.
(4) index determining
Experiment packet：Blank group and polypeptide group.L4 phase nematodes after synchronization is handled are placed in corresponding NGM plates, experiment
In H containing 20mM2O2NGM tablets in carry out, 10 are no less than per plate quantity, counts that nematode is dead, viable count per half an hour,
Nematode death criterion：Without mobile and swallowing act, still without any reaction after touching.Rejecting standard：1. flee to tablet wall
Or cover and thirst；2. worm's ovum is hatched into bag sample worm in vivo：3. pierce in agar.
3. experimental result and analysis：
Influences of the 5 biologically active polypeptide GLNYYQQKPVAL of table to nematode under oxidative stress
As can be seen from Table 5, there is conspicuousness to improve (P ＜ 0.05) for experimental group nematode average life span under oxidative stress,
Extremely significant difference (P is presented in polypeptide GLNYYQQKPVAL groups<0.05).The each group half death time is also accordingly to a certain degree
On extended, compared with other experimental groups hybrid peptide group present conspicuousness improve (P<0.05).As shown in figure 8, should in oxidation
Under the conditions of swashing, experimental group survival rate is obviously higher than blank group survival rate.This explanation is under the conditions of oxidative stress, the survival of nematode
Rate is significantly improved, it may be possible to since polypeptide GLNYYQQKPVAL can effectively help nematode to resist oxidative damage, removes body
The free radical of interior generation and the accumulation for reducing peroxide, rather than realized by strengthening its heat hardiness.Organism life-span prolongs
Length is due to improve resistance of the cell to stress conditions to a certain extent, thus under anti-aging and pressure stressed condition
Survival rate there are much relations.This results show polypeptide GLNYYQQKPVAL can significantly increase the oxidative stress of nematode
Ability, improves the survival rate of nematode, illustrates that certain density polypeptide GLNYYQQKPVAL has anti-aging function for nematode.
Above example illustrates that biologically active polypeptide GLNYYQQKPVAL of the present invention has anti-oxidation function and anti-aging work(
Energy.
The above-mentioned description to embodiment is understood that for ease of those skilled in the art and using invention.
Person skilled in the art obviously easily can make these embodiments various modifications, and described herein general
Principle is applied in other embodiment without by performing creative labour.Therefore, the invention is not restricted to above-described embodiment, ability
Field technique personnel disclose according to the present invention, do not depart from improvement that scope made and modification all should be the present invention's
Within protection domain.
Sequence table
<110>Shanghai Communications University；Zhejiang Hui Tai life and healths Science and Technology Ltd.
<120>A kind of biologically active polypeptide GLNYYQQKPVAL and its preparation method and application
<160> 3
<170> SIPOSequenceListing 1.0
<210> 1
<211> 12
<212> PRT
<213>Artificial sequence (Artificial Sequence)
<400> 1
Gly Leu Asn Tyr Tyr Gln Gln Lys Pro Val Ala Leu
1 5 10
<210> 2
<211> 36
<212> DNA
<213>Artificial sequence (Artificial Sequence)
<400> 2
ggactcaatt actaccaaca gaaaccagtt gcacta 36
<210> 3
<211> 190
<212> PRT
<213>Artificial sequence (Artificial Sequence)
<400> 3
Met Met Lys Ser Phe Phe Leu Val Val Thr Ile Leu Ala Leu Thr Leu
1 5 10 15
Pro Phe Leu Gly Ala Gln Glu Gln Asn Gln Glu Gln Pro Ile Arg Cys
20 25 30
Glu Lys Asp Glu Arg Phe Phe Ser Asp Lys Ile Ala Lys Tyr Ile Pro
35 40 45
Ile Gln Tyr Val Leu Ser Arg Tyr Pro Ser Tyr Gly Leu Asn Tyr Tyr
50 55 60
Gln Gln Lys Pro Val Ala Leu Ile Asn Asn Gln Phe Leu Pro Tyr Pro
65 70 75 80
Tyr Tyr Ala Lys Pro Ala Ala Val Arg Ser Pro Ala Gln Ile Leu Gln
85 90 95
Trp Gln Val Leu Ser Asn Thr Val Pro Ala Lys Ser Cys Gln Ala Gln
100 105 110
Pro Thr Thr Met Ala Arg His Pro His Pro His Leu Ser Phe Met Ala
115 120 125
Ile Pro Pro Lys Lys Asn Gln Asp Lys Thr Glu Ile Pro Thr Ile Asn
130 135 140
Thr Ile Ala Ser Gly Glu Pro Thr Ser Thr Pro Thr Thr Glu Ala Val
145 150 155 160
Glu Ser Thr Val Ala Thr Leu Glu Asp Ser Pro Glu Val Ile Glu Ser
165 170 175
Pro Pro Glu Ile Asn Thr Val Gln Val Thr Ser Thr Ala Val
180 185 190
Claims (10)
1. a kind of biologically active polypeptide GLNYYQQKPVAL, it is characterised in that its amino acid sequence is Gly-Leu-Asn-Tyr-
Tyr-Gln-Gln-Lys-Pro-Val-Ala-Leu。
A kind of 2. biologically active polypeptide GLNYYQQKPVAL according to claim 1, it is characterised in that the bioactivity
Polypeptide is milk-derived.
3. encode the nucleotide fragments of biologically active polypeptide GLNYYQQKPVAL described in claim 1, it is characterised in that the core
The sequence of acid fragments such as SEQ ID NO：Shown in 2.
4. the preparation method of biologically active polypeptide GLNYYQQKPVAL as claimed in claim 1, it is characterised in that pass through gene work
The method of journey is artificial synthesized, or is directly obtained from dairy products by the method isolated and purified, or directly by chemical synthesis system
It is standby.
5. the application of biologically active polypeptide GLNYYQQKPVAL as claimed in claim 1, it is characterised in that the bioactivity is more
Applications of the peptide GLNYYQQKPVAL in the food with anti-oxidation function, health products, medicine or cosmetics are prepared.
6. the application of biologically active polypeptide GLNYYQQKPVAL as claimed in claim 1, it is characterised in that the bioactivity is more
Applications of the peptide GLNYYQQKPVAL in the food with anti-senescence function, health products or medicine is prepared.
7. the application of biologically active polypeptide GLNYYQQKPVAL as claimed in claim 1, it is characterised in that the bioactivity is more
Applications of the peptide GLNYYQQKPVAL in the food with anti-oxidation function and anti-senescence function, health products or medicine is prepared.
A kind of 8. oxidation resistant product, it is characterised in that including biologically active polypeptide GLNYYQQKPVAL as claimed in claim 1 or
The derivative of the biologically active polypeptide GLNYYQQKPVAL；The oxidation resistant product includes antioxidant food, anti-oxidant guarantor
Strong product, anti-oxidation medicine or antioxidation cosmetic product；The derivative of the biologically active polypeptide GLNYYQQKPVAL, refers in biology
On the amino acid side groups of active peptides GLNYYQQKPVAL, aminoterminal or c-terminus carry out hydroxylating, carboxylated, carbonyl
Change, methylate, acetylation, phosphorylation, esterification or glycosylation modified, obtained polypeptide derivative.
A kind of 9. anti-aging product, it is characterised in that including biologically active polypeptide GLNYYQQKPVAL as claimed in claim 1 or
The derivative of the biologically active polypeptide GLNYYQQKPVAL；The anti-aging product includes antisenility cistanche food, anti-aging is protected
Strong product or antiaging agent；The derivative of the biologically active polypeptide GLNYYQQKPVAL, refers in biologically active polypeptide
On the amino acid side groups of GLNYYQQKPVAL, aminoterminal or c-terminus carry out hydroxylating, carboxylated, be carbonylated, methylate,
Acetylation, phosphorylation, esterification or glycosylation modified, obtained polypeptide derivative.
10. a kind of product with anti-oxidation function and anti-senescence function, it is characterised in that including raw as claimed in claim 1
The derivative of thing active peptides GLNYYQQKPVAL or described biologically active polypeptides GLNYYQQKPVAL；With anti-oxidation function and
The product of anti-senescence function includes food, health products or medicine；The derivative of the biologically active polypeptide GLNYYQQKPVAL, is
Refer on the amino acid side groups of biologically active polypeptide GLNYYQQKPVAL, aminoterminal or c-terminus carry out hydroxylating, carboxyl
Change, be carbonylated, methylating, acetylation, phosphorylation, esterification or glycosylation modified, obtained polypeptide derivative.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201711122919.8A CN107903313A (en) | 2017-11-14 | 2017-11-14 | A kind of biologically active polypeptide GLNYYQQKPVAL and its preparation method and application |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201711122919.8A CN107903313A (en) | 2017-11-14 | 2017-11-14 | A kind of biologically active polypeptide GLNYYQQKPVAL and its preparation method and application |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN107903313A true CN107903313A (en) | 2018-04-13 |
Family
ID=61844060
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201711122919.8A Withdrawn CN107903313A (en) | 2017-11-14 | 2017-11-14 | A kind of biologically active polypeptide GLNYYQQKPVAL and its preparation method and application |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN107903313A (en) |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN104479001A (en) * | 2014-12-19 | 2015-04-01 | 上海交通大学 | Preparation and application of kappa-casein derived bioactive peptides |
| CN107176995A (en) * | 2017-07-06 | 2017-09-19 | 浙江辉肽生命健康科技有限公司 | A kind of biologically active polypeptide SKVLPVPEKAVPYPQ and its preparation method and application |
| CN107226860A (en) * | 2017-07-06 | 2017-10-03 | 浙江辉肽生命健康科技有限公司 | A kind of biologically active polypeptide SKHSSLDCVL and its preparation method and application |
-
2017
- 2017-11-14 CN CN201711122919.8A patent/CN107903313A/en not_active Withdrawn
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN104479001A (en) * | 2014-12-19 | 2015-04-01 | 上海交通大学 | Preparation and application of kappa-casein derived bioactive peptides |
| CN107176995A (en) * | 2017-07-06 | 2017-09-19 | 浙江辉肽生命健康科技有限公司 | A kind of biologically active polypeptide SKVLPVPEKAVPYPQ and its preparation method and application |
| CN107226860A (en) * | 2017-07-06 | 2017-10-03 | 浙江辉肽生命健康科技有限公司 | A kind of biologically active polypeptide SKHSSLDCVL and its preparation method and application |
Non-Patent Citations (2)
| Title |
|---|
| YAN JIN等: "Peptide profiling and the bioactivity character of yogurt in the simulated gastrointestinal digestion", 《JOURNAL OF PROTEOMICS》 * |
| 高扬等: "乳源性小肽QEPV的抗衰老功能研究", 《中国乳品工业》 * |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN107200780A (en) | A kind of biologically active polypeptide LVYPFPG and its preparation method and application | |
| CN107226860A (en) | A kind of biologically active polypeptide SKHSSLDCVL and its preparation method and application | |
| CN107236031A (en) | A kind of biologically active polypeptide PMIGVNQELAY and its preparation method and application | |
| CN108794587A (en) | A kind of biologically active polypeptide KVTPYQA and its preparation method and application | |
| CN107840880A (en) | A kind of biologically active polypeptide GLNYYQQKPVA and its preparation method and application | |
| CN107814844A (en) | A kind of biologically active polypeptide VVPPFL and its preparation method and application | |
| CN107840881A (en) | A kind of biologically active polypeptide AQQKEPMIGVNQELA and its preparation method and application | |
| CN108017703B (en) | Bioactive polypeptide VPITPT L N and preparation method and application thereof | |
| CN108794603A (en) | A kind of biologically active polypeptide TVTMLMTTIL and its preparation method and application | |
| CN107814842A (en) | A kind of biologically active polypeptide SQSKVLPVPE and its preparation method and application | |
| CN108586588A (en) | A kind of biologically active polypeptide APMISAASVH and its preparation method and application | |
| CN108794596A (en) | A kind of biologically active polypeptide ENPRAF and its preparation method and application | |
| CN107759666A (en) | A kind of biologically active polypeptide AQTQSLVYPFPGPIHN and its preparation method and application | |
| CN109160945A (en) | A kind of biologically active polypeptide DKLAQ and its preparation method and application | |
| CN107903313A (en) | A kind of biologically active polypeptide GLNYYQQKPVAL and its preparation method and application | |
| CN109180782B (en) | Bioactive polypeptide DDVTEVM and preparation method and application thereof | |
| CN107814843A (en) | A kind of biologically active polypeptide VMFPPQ and its preparation method and application | |
| CN108794601A (en) | A kind of biologically active polypeptide PLLPQSL and its preparation method and application | |
| CN107880103A (en) | Biologically active polypeptide qpevmgvskvkeamapkqkempfpky and its preparation and application | |
| CN107880106A (en) | A kind of biologically active polypeptide VPITPTLNRE and its preparation method and application | |
| CN108017709A (en) | A kind of biologically active polypeptide KEPMIGVNQELA and its preparation method and application | |
| CN107814835A (en) | A kind of biologically active polypeptide AVPITPTLNREQ and its preparation method and application | |
| CN107880102A (en) | A kind of biologically active polypeptide PEVIESPPEIN and its preparation method and application | |
| CN107814841A (en) | A kind of biologically active polypeptide QQPVLGPVRGP and its preparation method and application | |
| CN107892716A (en) | A kind of biologically active polypeptide LPPLL and its preparation method and application |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PB01 | Publication | ||
| PB01 | Publication | ||
| SE01 | Entry into force of request for substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| WW01 | Invention patent application withdrawn after publication | ||
| WW01 | Invention patent application withdrawn after publication |
Application publication date: 20180413 |