CA2936092A1 - Stabilized hepatitis b core polypeptide - Google Patents
Stabilized hepatitis b core polypeptide Download PDFInfo
- Publication number
- CA2936092A1 CA2936092A1 CA2936092A CA2936092A CA2936092A1 CA 2936092 A1 CA2936092 A1 CA 2936092A1 CA 2936092 A CA2936092 A CA 2936092A CA 2936092 A CA2936092 A CA 2936092A CA 2936092 A1 CA2936092 A1 CA 2936092A1
- Authority
- CA
- Canada
- Prior art keywords
- hbc
- polypeptide
- amino acid
- seq
- protein
- 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.)
- Abandoned
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 101
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 95
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 95
- 208000006454 hepatitis Diseases 0.000 title description 2
- 231100000283 hepatitis Toxicity 0.000 title description 2
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 109
- 239000002245 particle Substances 0.000 claims abstract description 17
- 241000700605 Viruses Species 0.000 claims abstract description 16
- 235000001014 amino acid Nutrition 0.000 claims description 142
- 150000001413 amino acids Chemical class 0.000 claims description 123
- 229940024606 amino acid Drugs 0.000 claims description 122
- 108090000623 proteins and genes Proteins 0.000 claims description 113
- 235000018102 proteins Nutrition 0.000 claims description 107
- NNWQLZWAZSJGLY-VKHMYHEASA-N (2s)-2-azaniumyl-4-azidobutanoate Chemical compound OC(=O)[C@@H](N)CCN=[N+]=[N-] NNWQLZWAZSJGLY-VKHMYHEASA-N 0.000 claims description 43
- 238000006243 chemical reaction Methods 0.000 claims description 42
- 238000000034 method Methods 0.000 claims description 32
- 239000000539 dimer Substances 0.000 claims description 24
- 238000006467 substitution reaction Methods 0.000 claims description 24
- 239000011541 reaction mixture Substances 0.000 claims description 18
- 239000000178 monomer Substances 0.000 claims description 15
- 230000014616 translation Effects 0.000 claims description 15
- 238000001243 protein synthesis Methods 0.000 claims description 12
- 102220277072 rs1553408398 Human genes 0.000 claims description 11
- 239000013598 vector Substances 0.000 claims description 10
- 102220364092 c.229G>C Human genes 0.000 claims description 9
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 claims description 9
- 102220280387 rs201054129 Human genes 0.000 claims description 9
- 230000003612 virological effect Effects 0.000 claims description 7
- 102000040430 polynucleotide Human genes 0.000 claims description 6
- 108091033319 polynucleotide Proteins 0.000 claims description 6
- 239000002157 polynucleotide Substances 0.000 claims description 6
- 102220493349 40S ribosomal protein S3_T70R_mutation Human genes 0.000 claims description 5
- 102220534940 Integrator complex subunit 13_M66T_mutation Human genes 0.000 claims description 5
- 102220345529 c.192C>G Human genes 0.000 claims description 5
- 230000002209 hydrophobic effect Effects 0.000 claims description 5
- 102200004150 rs147750704 Human genes 0.000 claims description 5
- 102220074259 rs180177181 Human genes 0.000 claims description 5
- 102200135505 rs2273535 Human genes 0.000 claims description 5
- 102200109609 rs281875332 Human genes 0.000 claims description 5
- 102200108206 rs756233241 Human genes 0.000 claims description 5
- NEMHIKRLROONTL-QMMMGPOBSA-N (2s)-2-azaniumyl-3-(4-azidophenyl)propanoate Chemical compound OC(=O)[C@@H](N)CC1=CC=C(N=[N+]=[N-])C=C1 NEMHIKRLROONTL-QMMMGPOBSA-N 0.000 claims description 3
- ZXSBHXZKWRIEIA-JTQLQIEISA-N (2s)-3-(4-acetylphenyl)-2-azaniumylpropanoate Chemical compound CC(=O)C1=CC=C(C[C@H](N)C(O)=O)C=C1 ZXSBHXZKWRIEIA-JTQLQIEISA-N 0.000 claims description 3
- 102220528631 Aurora kinase A_I57V_mutation Human genes 0.000 claims description 3
- 102220166168 rs201614099 Human genes 0.000 claims description 3
- 108020001507 fusion proteins Proteins 0.000 claims description 2
- 102000037865 fusion proteins Human genes 0.000 claims description 2
- 239000000376 reactant Substances 0.000 claims description 2
- 102220032374 rs104895262 Human genes 0.000 claims 1
- 150000007523 nucleic acids Chemical group 0.000 abstract description 22
- 102000039446 nucleic acids Human genes 0.000 abstract description 20
- 108020004707 nucleic acids Proteins 0.000 abstract description 20
- 239000000126 substance Chemical group 0.000 abstract description 7
- 208000015181 infectious disease Diseases 0.000 abstract description 5
- 229960005486 vaccine Drugs 0.000 abstract description 5
- 239000003814 drug Substances 0.000 abstract description 4
- 230000002458 infectious effect Effects 0.000 abstract description 3
- 108091005461 Nucleic proteins Chemical group 0.000 abstract description 2
- 230000004700 cellular uptake Effects 0.000 abstract description 2
- 230000010189 intracellular transport Effects 0.000 abstract description 2
- 230000003252 repetitive effect Effects 0.000 abstract description 2
- 230000021615 conjugation Effects 0.000 description 32
- 210000004027 cell Anatomy 0.000 description 30
- 238000001542 size-exclusion chromatography Methods 0.000 description 27
- 239000000872 buffer Substances 0.000 description 23
- 125000003275 alpha amino acid group Chemical group 0.000 description 22
- 108020004414 DNA Proteins 0.000 description 21
- 238000000502 dialysis Methods 0.000 description 20
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 20
- GHURLXDGHMZIGJ-UHFFFAOYSA-N 4-hydroxy-6-(2-oxoheptyl)pyran-2-one Chemical compound CCCCCC(=O)CC1=CC(O)=CC(=O)O1 GHURLXDGHMZIGJ-UHFFFAOYSA-N 0.000 description 19
- -1 about 1.5 M salt Chemical class 0.000 description 18
- 230000015572 biosynthetic process Effects 0.000 description 18
- 239000000499 gel Substances 0.000 description 18
- 238000003786 synthesis reaction Methods 0.000 description 18
- 108020004705 Codon Proteins 0.000 description 15
- 238000004458 analytical method Methods 0.000 description 14
- 239000010949 copper Substances 0.000 description 14
- KIDHWZJUCRJVML-UHFFFAOYSA-N putrescine Chemical compound NCCCCN KIDHWZJUCRJVML-UHFFFAOYSA-N 0.000 description 14
- ATHGHQPFGPMSJY-UHFFFAOYSA-N spermidine Chemical compound NCCCCNCCCN ATHGHQPFGPMSJY-UHFFFAOYSA-N 0.000 description 14
- 239000000203 mixture Substances 0.000 description 13
- 239000008186 active pharmaceutical agent Substances 0.000 description 12
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 11
- 108010040721 Flagellin Proteins 0.000 description 11
- OAKJQQAXSVQMHS-UHFFFAOYSA-N Hydrazine Chemical compound NN OAKJQQAXSVQMHS-UHFFFAOYSA-N 0.000 description 11
- 239000003054 catalyst Substances 0.000 description 11
- 238000012650 click reaction Methods 0.000 description 11
- 101100096719 Arabidopsis thaliana SSL2 gene Proteins 0.000 description 10
- 108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 description 10
- 102000004457 Granulocyte-Macrophage Colony-Stimulating Factor Human genes 0.000 description 10
- 101100366560 Panax ginseng SS10 gene Proteins 0.000 description 10
- 210000000234 capsid Anatomy 0.000 description 10
- 239000000284 extract Substances 0.000 description 10
- 239000000463 material Substances 0.000 description 10
- MUBZPKHOEPUJKR-UHFFFAOYSA-N Oxalic acid Chemical compound OC(=O)C(O)=O MUBZPKHOEPUJKR-UHFFFAOYSA-N 0.000 description 9
- 108020004566 Transfer RNA Proteins 0.000 description 9
- 239000003153 chemical reaction reagent Substances 0.000 description 9
- 235000006109 methionine Nutrition 0.000 description 9
- 230000035772 mutation Effects 0.000 description 9
- 150000001345 alkine derivatives Chemical group 0.000 description 8
- 239000003795 chemical substances by application Substances 0.000 description 8
- 235000018417 cysteine Nutrition 0.000 description 8
- 239000003623 enhancer Substances 0.000 description 8
- 208000002672 hepatitis B Diseases 0.000 description 8
- 238000004519 manufacturing process Methods 0.000 description 8
- 108020004999 messenger RNA Proteins 0.000 description 8
- 239000013612 plasmid Substances 0.000 description 8
- 239000000047 product Substances 0.000 description 8
- 230000002829 reductive effect Effects 0.000 description 8
- 150000003839 salts Chemical class 0.000 description 8
- 101710132601 Capsid protein Proteins 0.000 description 7
- 102100029880 Glycodelin Human genes 0.000 description 7
- 239000005700 Putrescine Substances 0.000 description 7
- 230000000694 effects Effects 0.000 description 7
- 230000003993 interaction Effects 0.000 description 7
- 239000003446 ligand Substances 0.000 description 7
- 229940063673 spermidine Drugs 0.000 description 7
- HYKCGNHOSRPGCP-UHFFFAOYSA-N 1-(2h-triazol-4-yl)-n,n-bis(2h-triazol-4-ylmethyl)methanamine Chemical compound C=1NN=NC=1CN(CC=1N=NNC=1)CC1=CNN=N1 HYKCGNHOSRPGCP-UHFFFAOYSA-N 0.000 description 6
- BAWFJGJZGIEFAR-NNYOXOHSSA-N NAD zwitterion Chemical compound NC(=O)C1=CC=C[N+]([C@H]2[C@@H]([C@H](O)[C@@H](COP([O-])(=O)OP(O)(=O)OC[C@@H]3[C@H]([C@@H](O)[C@@H](O3)N3C4=NC=NC(N)=C4N=C3)O)O2)O)=C1 BAWFJGJZGIEFAR-NNYOXOHSSA-N 0.000 description 6
- 229930006000 Sucrose Natural products 0.000 description 6
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 6
- 239000000427 antigen Substances 0.000 description 6
- 108091007433 antigens Proteins 0.000 description 6
- 102000036639 antigens Human genes 0.000 description 6
- 238000000211 autoradiogram Methods 0.000 description 6
- 230000027455 binding Effects 0.000 description 6
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 6
- 229930182817 methionine Natural products 0.000 description 6
- 230000004048 modification Effects 0.000 description 6
- 238000012986 modification Methods 0.000 description 6
- 238000007254 oxidation reaction Methods 0.000 description 6
- 230000010627 oxidative phosphorylation Effects 0.000 description 6
- 229920001223 polyethylene glycol Polymers 0.000 description 6
- 239000012146 running buffer Substances 0.000 description 6
- 239000005720 sucrose Substances 0.000 description 6
- 230000002103 transcriptional effect Effects 0.000 description 6
- 108091026890 Coding region Proteins 0.000 description 5
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 5
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 5
- FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 5
- 238000001042 affinity chromatography Methods 0.000 description 5
- 150000001875 compounds Chemical class 0.000 description 5
- 229910052749 magnesium Inorganic materials 0.000 description 5
- 239000011777 magnesium Substances 0.000 description 5
- 239000012528 membrane Substances 0.000 description 5
- 150000002742 methionines Chemical class 0.000 description 5
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 5
- 239000007800 oxidant agent Substances 0.000 description 5
- 239000000546 pharmaceutical excipient Substances 0.000 description 5
- DTBNBXWJWCWCIK-UHFFFAOYSA-N phosphoenolpyruvic acid Chemical compound OC(=O)C(=C)OP(O)(O)=O DTBNBXWJWCWCIK-UHFFFAOYSA-N 0.000 description 5
- 230000001105 regulatory effect Effects 0.000 description 5
- RGJOEKWQDUBAIZ-IBOSZNHHSA-N CoASH Chemical compound O[C@@H]1[C@H](OP(O)(O)=O)[C@@H](COP(O)(=O)OP(O)(=O)OCC(C)(C)[C@@H](O)C(=O)NCCC(=O)NCCS)O[C@H]1N1C2=NC=NC(N)=C2N=C1 RGJOEKWQDUBAIZ-IBOSZNHHSA-N 0.000 description 4
- 101710094648 Coat protein Proteins 0.000 description 4
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 4
- 102000004190 Enzymes Human genes 0.000 description 4
- 108090000790 Enzymes Proteins 0.000 description 4
- 102100021181 Golgi phosphoprotein 3 Human genes 0.000 description 4
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 4
- 101710125418 Major capsid protein Proteins 0.000 description 4
- 102100029268 Neurotrophin-3 Human genes 0.000 description 4
- 108090000099 Neurotrophin-4 Proteins 0.000 description 4
- 101710141454 Nucleoprotein Proteins 0.000 description 4
- 101710083689 Probable capsid protein Proteins 0.000 description 4
- 238000010958 [3+2] cycloaddition reaction Methods 0.000 description 4
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 4
- IVRMZWNICZWHMI-UHFFFAOYSA-N azide group Chemical group [N-]=[N+]=[N-] IVRMZWNICZWHMI-UHFFFAOYSA-N 0.000 description 4
- 230000004071 biological effect Effects 0.000 description 4
- 239000007795 chemical reaction product Substances 0.000 description 4
- RGJOEKWQDUBAIZ-UHFFFAOYSA-N coenzime A Natural products OC1C(OP(O)(O)=O)C(COP(O)(=O)OP(O)(=O)OCC(C)(C)C(O)C(=O)NCCC(=O)NCCS)OC1N1C2=NC=NC(N)=C2N=C1 RGJOEKWQDUBAIZ-UHFFFAOYSA-N 0.000 description 4
- 239000005516 coenzyme A Substances 0.000 description 4
- 229940093530 coenzyme a Drugs 0.000 description 4
- KDTSHFARGAKYJN-UHFFFAOYSA-N dephosphocoenzyme A Natural products OC1C(O)C(COP(O)(=O)OP(O)(=O)OCC(C)(C)C(O)C(=O)NCCC(=O)NCCS)OC1N1C2=NC=NC(N)=C2N=C1 KDTSHFARGAKYJN-UHFFFAOYSA-N 0.000 description 4
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 4
- 229940088598 enzyme Drugs 0.000 description 4
- 239000008103 glucose Substances 0.000 description 4
- 229950006238 nadide Drugs 0.000 description 4
- 230000001590 oxidative effect Effects 0.000 description 4
- 229910052760 oxygen Inorganic materials 0.000 description 4
- 239000001301 oxygen Substances 0.000 description 4
- 229930029653 phosphoenolpyruvate Natural products 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- 102220184129 rs778408190 Human genes 0.000 description 4
- 102220059876 rs786201800 Human genes 0.000 description 4
- 238000004062 sedimentation Methods 0.000 description 4
- 230000006641 stabilisation Effects 0.000 description 4
- 238000011105 stabilization Methods 0.000 description 4
- 238000000856 sucrose gradient centrifugation Methods 0.000 description 4
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 3
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 3
- 102000052866 Amino Acyl-tRNA Synthetases Human genes 0.000 description 3
- 108700028939 Amino Acyl-tRNA Synthetases Proteins 0.000 description 3
- 108090000565 Capsid Proteins Proteins 0.000 description 3
- RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 0.000 description 3
- VMQMZMRVKUZKQL-UHFFFAOYSA-N Cu+ Chemical compound [Cu+] VMQMZMRVKUZKQL-UHFFFAOYSA-N 0.000 description 3
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 3
- 108090000723 Insulin-Like Growth Factor I Proteins 0.000 description 3
- 102000004218 Insulin-Like Growth Factor I Human genes 0.000 description 3
- 241001465754 Metazoa Species 0.000 description 3
- 108010025020 Nerve Growth Factor Proteins 0.000 description 3
- 108091028043 Nucleic acid sequence Proteins 0.000 description 3
- 108091034117 Oligonucleotide Proteins 0.000 description 3
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 3
- 108020005038 Terminator Codon Proteins 0.000 description 3
- 230000003321 amplification Effects 0.000 description 3
- 230000001580 bacterial effect Effects 0.000 description 3
- 210000004899 c-terminal region Anatomy 0.000 description 3
- 229910052802 copper Inorganic materials 0.000 description 3
- 241001493065 dsRNA viruses Species 0.000 description 3
- 238000009472 formulation Methods 0.000 description 3
- 230000006870 function Effects 0.000 description 3
- 238000000338 in vitro Methods 0.000 description 3
- 239000003112 inhibitor Substances 0.000 description 3
- 229920002521 macromolecule Polymers 0.000 description 3
- 235000013918 magnesium diglutamate Nutrition 0.000 description 3
- 229940063886 magnesium glutamate Drugs 0.000 description 3
- MYUGVHJLXONYNC-QHTZZOMLSA-J magnesium;(2s)-2-aminopentanedioate Chemical group [Mg+2].[O-]C(=O)[C@@H](N)CCC([O-])=O.[O-]C(=O)[C@@H](N)CCC([O-])=O MYUGVHJLXONYNC-QHTZZOMLSA-J 0.000 description 3
- 239000002609 medium Substances 0.000 description 3
- 238000003199 nucleic acid amplification method Methods 0.000 description 3
- 235000006408 oxalic acid Nutrition 0.000 description 3
- NFHFRUOZVGFOOS-UHFFFAOYSA-N palladium;triphenylphosphane Chemical compound [Pd].C1=CC=CC=C1P(C=1C=CC=CC=1)C1=CC=CC=C1.C1=CC=CC=C1P(C=1C=CC=CC=1)C1=CC=CC=C1.C1=CC=CC=C1P(C=1C=CC=CC=1)C1=CC=CC=C1.C1=CC=CC=C1P(C=1C=CC=CC=1)C1=CC=CC=C1 NFHFRUOZVGFOOS-UHFFFAOYSA-N 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 230000002285 radioactive effect Effects 0.000 description 3
- 230000010076 replication Effects 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 238000013518 transcription Methods 0.000 description 3
- 230000035897 transcription Effects 0.000 description 3
- 238000013519 translation Methods 0.000 description 3
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 2
- VVIAGPKUTFNRDU-UHFFFAOYSA-N 6S-folinic acid Natural products C1NC=2NC(N)=NC(=O)C=2N(C=O)C1CNC1=CC=C(C(=O)NC(CCC(O)=O)C(O)=O)C=C1 VVIAGPKUTFNRDU-UHFFFAOYSA-N 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 2
- 102000007350 Bone Morphogenetic Proteins Human genes 0.000 description 2
- 108010007726 Bone Morphogenetic Proteins Proteins 0.000 description 2
- 244000025254 Cannabis sativa Species 0.000 description 2
- 102100023321 Ceruloplasmin Human genes 0.000 description 2
- 102000007644 Colony-Stimulating Factors Human genes 0.000 description 2
- 108010071942 Colony-Stimulating Factors Proteins 0.000 description 2
- 102000012410 DNA Ligases Human genes 0.000 description 2
- 108010061982 DNA Ligases Proteins 0.000 description 2
- 108090000626 DNA-directed RNA polymerases Proteins 0.000 description 2
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- MPJKWIXIYCLVCU-UHFFFAOYSA-N Folinic acid Natural products NC1=NC2=C(N(C=O)C(CNc3ccc(cc3)C(=O)NC(CCC(=O)O)CC(=O)O)CN2)C(=O)N1 MPJKWIXIYCLVCU-UHFFFAOYSA-N 0.000 description 2
- 102100039620 Granulocyte-macrophage colony-stimulating factor Human genes 0.000 description 2
- 101000746373 Homo sapiens Granulocyte-macrophage colony-stimulating factor Proteins 0.000 description 2
- 102000004877 Insulin Human genes 0.000 description 2
- 108090001061 Insulin Proteins 0.000 description 2
- 108090001117 Insulin-Like Growth Factor II Proteins 0.000 description 2
- 102000048143 Insulin-Like Growth Factor II Human genes 0.000 description 2
- 102000015696 Interleukins Human genes 0.000 description 2
- 108010063738 Interleukins Proteins 0.000 description 2
- 229930194542 Keto Natural products 0.000 description 2
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 2
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 2
- 239000007987 MES buffer Substances 0.000 description 2
- ZMXDDKWLCZADIW-UHFFFAOYSA-N N,N-Dimethylformamide Chemical compound CN(C)C=O ZMXDDKWLCZADIW-UHFFFAOYSA-N 0.000 description 2
- 108090000742 Neurotrophin 3 Proteins 0.000 description 2
- 102000003683 Neurotrophin-4 Human genes 0.000 description 2
- 102100033857 Neurotrophin-4 Human genes 0.000 description 2
- 102220567424 Ornithine decarboxylase antizyme 1_D78K_mutation Human genes 0.000 description 2
- OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical compound [P] OAICVXFJPJFONN-UHFFFAOYSA-N 0.000 description 2
- 108010038512 Platelet-Derived Growth Factor Proteins 0.000 description 2
- 102000010780 Platelet-Derived Growth Factor Human genes 0.000 description 2
- 229920001213 Polysorbate 20 Polymers 0.000 description 2
- 241000725643 Respiratory syncytial virus Species 0.000 description 2
- 239000011542 SDS running buffer Substances 0.000 description 2
- 229920002684 Sepharose Polymers 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 101710137500 T7 RNA polymerase Proteins 0.000 description 2
- 102100033571 Tissue-type plasminogen activator Human genes 0.000 description 2
- 241000723873 Tobacco mosaic virus Species 0.000 description 2
- 108010009583 Transforming Growth Factors Proteins 0.000 description 2
- 102000009618 Transforming Growth Factors Human genes 0.000 description 2
- 108010073929 Vascular Endothelial Growth Factor A Proteins 0.000 description 2
- 102000005789 Vascular Endothelial Growth Factors Human genes 0.000 description 2
- 108010019530 Vascular Endothelial Growth Factors Proteins 0.000 description 2
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 2
- 230000001133 acceleration Effects 0.000 description 2
- ZSLZBFCDCINBPY-ZSJPKINUSA-N acetyl-CoA Chemical compound O[C@@H]1[C@H](OP(O)(O)=O)[C@@H](COP(O)(=O)OP(O)(=O)OCC(C)(C)[C@@H](O)C(=O)NCCC(=O)NCCSC(=O)C)O[C@H]1N1C2=NC=NC(N)=C2N=C1 ZSLZBFCDCINBPY-ZSJPKINUSA-N 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 230000004913 activation Effects 0.000 description 2
- 150000001408 amides Chemical class 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 238000000376 autoradiography Methods 0.000 description 2
- PHKGGXPMPXXISP-DFWYDOINSA-N azanium;(4s)-4-amino-5-hydroxy-5-oxopentanoate Chemical compound [NH4+].[O-]C(=O)[C@@H]([NH3+])CCC([O-])=O PHKGGXPMPXXISP-DFWYDOINSA-N 0.000 description 2
- 230000009286 beneficial effect Effects 0.000 description 2
- OWMVSZAMULFTJU-UHFFFAOYSA-N bis-tris Chemical compound OCCN(CCO)C(CO)(CO)CO OWMVSZAMULFTJU-UHFFFAOYSA-N 0.000 description 2
- 239000003114 blood coagulation factor Substances 0.000 description 2
- 229940112869 bone morphogenetic protein Drugs 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 235000014633 carbohydrates Nutrition 0.000 description 2
- 210000004671 cell-free system Anatomy 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 210000000349 chromosome Anatomy 0.000 description 2
- 229940047120 colony stimulating factors Drugs 0.000 description 2
- 238000010276 construction Methods 0.000 description 2
- 230000008878 coupling Effects 0.000 description 2
- 238000010168 coupling process Methods 0.000 description 2
- 238000005859 coupling reaction Methods 0.000 description 2
- 230000003247 decreasing effect Effects 0.000 description 2
- WDRWZVWLVBXVOI-QTNFYWBSSA-L dipotassium;(2s)-2-aminopentanedioate Chemical compound [K+].[K+].[O-]C(=O)[C@@H](N)CCC([O-])=O WDRWZVWLVBXVOI-QTNFYWBSSA-L 0.000 description 2
- IRXRGVFLQOSHOH-UHFFFAOYSA-L dipotassium;oxalate Chemical compound [K+].[K+].[O-]C(=O)C([O-])=O IRXRGVFLQOSHOH-UHFFFAOYSA-L 0.000 description 2
- 230000002255 enzymatic effect Effects 0.000 description 2
- 150000002148 esters Chemical class 0.000 description 2
- 210000003527 eukaryotic cell Anatomy 0.000 description 2
- 239000013604 expression vector Substances 0.000 description 2
- VVIAGPKUTFNRDU-ABLWVSNPSA-N folinic acid Chemical compound C1NC=2NC(N)=NC(=O)C=2N(C=O)C1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 VVIAGPKUTFNRDU-ABLWVSNPSA-N 0.000 description 2
- 235000008191 folinic acid Nutrition 0.000 description 2
- 239000011672 folinic acid Substances 0.000 description 2
- 239000012634 fragment Substances 0.000 description 2
- 238000002825 functional assay Methods 0.000 description 2
- 150000004676 glycans Chemical class 0.000 description 2
- 239000003102 growth factor Substances 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- 238000010438 heat treatment Methods 0.000 description 2
- 229910052739 hydrogen Inorganic materials 0.000 description 2
- 239000001257 hydrogen Substances 0.000 description 2
- 230000028993 immune response Effects 0.000 description 2
- 230000002163 immunogen Effects 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 2
- 229940047122 interleukins Drugs 0.000 description 2
- 125000000468 ketone group Chemical group 0.000 description 2
- 229960001691 leucovorin Drugs 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 239000012160 loading buffer Substances 0.000 description 2
- 230000014759 maintenance of location Effects 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 230000002503 metabolic effect Effects 0.000 description 2
- 229910052751 metal Inorganic materials 0.000 description 2
- 239000002184 metal Substances 0.000 description 2
- 238000000329 molecular dynamics simulation Methods 0.000 description 2
- 235000013917 monoammonium glutamate Nutrition 0.000 description 2
- 235000013919 monopotassium glutamate Nutrition 0.000 description 2
- 239000003900 neurotrophic factor Substances 0.000 description 2
- 229940101270 nicotinamide adenine dinucleotide (nad) Drugs 0.000 description 2
- 239000002773 nucleotide Substances 0.000 description 2
- 125000003729 nucleotide group Chemical group 0.000 description 2
- 229940116315 oxalic acid Drugs 0.000 description 2
- 230000003647 oxidation Effects 0.000 description 2
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 2
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 2
- 229920001282 polysaccharide Polymers 0.000 description 2
- 239000005017 polysaccharide Substances 0.000 description 2
- 230000002265 prevention Effects 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 230000006920 protein precipitation Effects 0.000 description 2
- 102000005962 receptors Human genes 0.000 description 2
- 108020003175 receptors Proteins 0.000 description 2
- 230000006798 recombination Effects 0.000 description 2
- 239000011347 resin Substances 0.000 description 2
- 229920005989 resin Polymers 0.000 description 2
- 210000003705 ribosome Anatomy 0.000 description 2
- 102220280159 rs779269083 Human genes 0.000 description 2
- 230000003248 secreting effect Effects 0.000 description 2
- 238000001338 self-assembly Methods 0.000 description 2
- 238000010512 small scale reaction Methods 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 238000001228 spectrum Methods 0.000 description 2
- PFNFFQXMRSDOHW-UHFFFAOYSA-N spermine Chemical compound NCCCNCCCCNCCCN PFNFFQXMRSDOHW-UHFFFAOYSA-N 0.000 description 2
- 230000000087 stabilizing effect Effects 0.000 description 2
- 238000003860 storage Methods 0.000 description 2
- 210000001519 tissue Anatomy 0.000 description 2
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 2
- 241001515965 unidentified phage Species 0.000 description 2
- 239000003981 vehicle Substances 0.000 description 2
- PPDNGMUGVMESGE-JTQLQIEISA-N (2s)-2-amino-3-(4-ethynylphenyl)propanoic acid Chemical compound OC(=O)[C@@H](N)CC1=CC=C(C#C)C=C1 PPDNGMUGVMESGE-JTQLQIEISA-N 0.000 description 1
- JSXMFBNJRFXRCX-NSHDSACASA-N (2s)-2-amino-3-(4-prop-2-ynoxyphenyl)propanoic acid Chemical compound OC(=O)[C@@H](N)CC1=CC=C(OCC#C)C=C1 JSXMFBNJRFXRCX-NSHDSACASA-N 0.000 description 1
- BZSALXKCVOJCJJ-IPEMHBBOSA-N (4s)-4-[[(2s)-2-acetamido-3-methylbutanoyl]amino]-5-[[(2s)-1-[[(2s)-1-[[(2s,3r)-1-[[(2s)-1-[[(2s)-1-[[2-[[(2s)-1-amino-1-oxo-3-phenylpropan-2-yl]amino]-2-oxoethyl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]amino]-3-hydroxy Chemical compound CC(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCC)C(=O)N[C@@H](CCCC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCN=C(N)N)C(=O)NCC(=O)N[C@H](C(N)=O)CC1=CC=CC=C1 BZSALXKCVOJCJJ-IPEMHBBOSA-N 0.000 description 1
- 102000040650 (ribonucleotides)n+m Human genes 0.000 description 1
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 1
- QXZBMSIDSOZZHK-DOPDSADYSA-N 31362-50-2 Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(N)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H]1NC(=O)CC1)C(C)C)C1=CNC=N1 QXZBMSIDSOZZHK-DOPDSADYSA-N 0.000 description 1
- 208000030507 AIDS Diseases 0.000 description 1
- 102000007469 Actins Human genes 0.000 description 1
- 108010085238 Actins Proteins 0.000 description 1
- 108010059616 Activins Proteins 0.000 description 1
- 102000005606 Activins Human genes 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 description 1
- 108010005853 Anti-Mullerian Hormone Proteins 0.000 description 1
- 108020005098 Anticodon Proteins 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 101800001288 Atrial natriuretic factor Proteins 0.000 description 1
- 102400001282 Atrial natriuretic peptide Human genes 0.000 description 1
- 101800001890 Atrial natriuretic peptide Proteins 0.000 description 1
- 108010077805 Bacterial Proteins Proteins 0.000 description 1
- 102000015081 Blood Coagulation Factors Human genes 0.000 description 1
- 108010039209 Blood Coagulation Factors Proteins 0.000 description 1
- 102000013585 Bombesin Human genes 0.000 description 1
- 108010051479 Bombesin Proteins 0.000 description 1
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 1
- 108010009575 CD55 Antigens Proteins 0.000 description 1
- 102400000113 Calcitonin Human genes 0.000 description 1
- 108060001064 Calcitonin Proteins 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- 102000001327 Chemokine CCL5 Human genes 0.000 description 1
- 108010055166 Chemokine CCL5 Proteins 0.000 description 1
- 102000019034 Chemokines Human genes 0.000 description 1
- 108010012236 Chemokines Proteins 0.000 description 1
- 102100022641 Coagulation factor IX Human genes 0.000 description 1
- 108700010070 Codon Usage Proteins 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 229910021589 Copper(I) bromide Inorganic materials 0.000 description 1
- 229910021595 Copper(I) iodide Inorganic materials 0.000 description 1
- 241000711573 Coronaviridae Species 0.000 description 1
- 239000004971 Cross linker Substances 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 241000450599 DNA viruses Species 0.000 description 1
- 208000001490 Dengue Diseases 0.000 description 1
- 206010012310 Dengue fever Diseases 0.000 description 1
- 102000016911 Deoxyribonucleases Human genes 0.000 description 1
- 108010053770 Deoxyribonucleases Proteins 0.000 description 1
- 241000702421 Dependoparvovirus Species 0.000 description 1
- 108090000204 Dipeptidase 1 Proteins 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 241001115402 Ebolavirus Species 0.000 description 1
- 108010014258 Elastin Proteins 0.000 description 1
- 102000016942 Elastin Human genes 0.000 description 1
- 241000709661 Enterovirus Species 0.000 description 1
- 241000991587 Enterovirus C Species 0.000 description 1
- 101710121417 Envelope glycoprotein Proteins 0.000 description 1
- 208000000832 Equine Encephalomyelitis Diseases 0.000 description 1
- 102000003951 Erythropoietin Human genes 0.000 description 1
- 108090000394 Erythropoietin Proteins 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 241000701959 Escherichia virus Lambda Species 0.000 description 1
- 108010076282 Factor IX Proteins 0.000 description 1
- 108010054218 Factor VIII Proteins 0.000 description 1
- 102000001690 Factor VIII Human genes 0.000 description 1
- 102000018233 Fibroblast Growth Factor Human genes 0.000 description 1
- 108050007372 Fibroblast Growth Factor Proteins 0.000 description 1
- 108090000386 Fibroblast Growth Factor 1 Proteins 0.000 description 1
- 102100031706 Fibroblast growth factor 1 Human genes 0.000 description 1
- 102000012673 Follicle Stimulating Hormone Human genes 0.000 description 1
- 108010079345 Follicle Stimulating Hormone Proteins 0.000 description 1
- VZCYOOQTPOCHFL-OWOJBTEDSA-N Fumaric acid Chemical compound OC(=O)\C=C\C(O)=O VZCYOOQTPOCHFL-OWOJBTEDSA-N 0.000 description 1
- 102400000321 Glucagon Human genes 0.000 description 1
- 108060003199 Glucagon Proteins 0.000 description 1
- 102000006771 Gonadotropins Human genes 0.000 description 1
- 108010086677 Gonadotropins Proteins 0.000 description 1
- 108010017080 Granulocyte Colony-Stimulating Factor Proteins 0.000 description 1
- 102000004269 Granulocyte Colony-Stimulating Factor Human genes 0.000 description 1
- 239000000095 Growth Hormone-Releasing Hormone Substances 0.000 description 1
- 239000007995 HEPES buffer Substances 0.000 description 1
- 208000031886 HIV Infections Diseases 0.000 description 1
- 101710154606 Hemagglutinin Proteins 0.000 description 1
- 241000711557 Hepacivirus Species 0.000 description 1
- 241000700721 Hepatitis B virus Species 0.000 description 1
- 241000709721 Hepatovirus A Species 0.000 description 1
- 208000007514 Herpes zoster Diseases 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 108010000521 Human Growth Hormone Proteins 0.000 description 1
- 102000002265 Human Growth Hormone Human genes 0.000 description 1
- 239000000854 Human Growth Hormone Substances 0.000 description 1
- 102000008100 Human Serum Albumin Human genes 0.000 description 1
- 108091006905 Human Serum Albumin Proteins 0.000 description 1
- 241000700588 Human alphaherpesvirus 1 Species 0.000 description 1
- 241000701074 Human alphaherpesvirus 2 Species 0.000 description 1
- 241000713772 Human immunodeficiency virus 1 Species 0.000 description 1
- 241000713340 Human immunodeficiency virus 2 Species 0.000 description 1
- AVXURJPOCDRRFD-UHFFFAOYSA-N Hydroxylamine Chemical compound ON AVXURJPOCDRRFD-UHFFFAOYSA-N 0.000 description 1
- 102100034349 Integrase Human genes 0.000 description 1
- 102000014150 Interferons Human genes 0.000 description 1
- 108010050904 Interferons Proteins 0.000 description 1
- 108010002352 Interleukin-1 Proteins 0.000 description 1
- 102000011782 Keratins Human genes 0.000 description 1
- 108010076876 Keratins Proteins 0.000 description 1
- 108010047294 Lamins Proteins 0.000 description 1
- 241000713666 Lentivirus Species 0.000 description 1
- 102000003960 Ligases Human genes 0.000 description 1
- 108090000364 Ligases Proteins 0.000 description 1
- 102000004895 Lipoproteins Human genes 0.000 description 1
- 108090001030 Lipoproteins Proteins 0.000 description 1
- 102000009151 Luteinizing Hormone Human genes 0.000 description 1
- 108010073521 Luteinizing Hormone Proteins 0.000 description 1
- 108090000542 Lymphotoxin-alpha Proteins 0.000 description 1
- 102000004083 Lymphotoxin-alpha Human genes 0.000 description 1
- 108010046938 Macrophage Colony-Stimulating Factor Proteins 0.000 description 1
- 102000007651 Macrophage Colony-Stimulating Factor Human genes 0.000 description 1
- 102000009571 Macrophage Inflammatory Proteins Human genes 0.000 description 1
- 108010009474 Macrophage Inflammatory Proteins Proteins 0.000 description 1
- 241000712079 Measles morbillivirus Species 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- 241000351643 Metapneumovirus Species 0.000 description 1
- 108060004795 Methyltransferase Proteins 0.000 description 1
- 241000711386 Mumps virus Species 0.000 description 1
- 102000003505 Myosin Human genes 0.000 description 1
- 108060008487 Myosin Proteins 0.000 description 1
- 108700010674 N-acetylVal-Nle(7,8)- allatotropin (5-13) Proteins 0.000 description 1
- 229910002651 NO3 Inorganic materials 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 102000003729 Neprilysin Human genes 0.000 description 1
- 108090000028 Neprilysin Proteins 0.000 description 1
- 102000015336 Nerve Growth Factor Human genes 0.000 description 1
- 108090000095 Neurotrophin-6 Proteins 0.000 description 1
- NHNBFGGVMKEFGY-UHFFFAOYSA-N Nitrate Chemical compound [O-][N+]([O-])=O NHNBFGGVMKEFGY-UHFFFAOYSA-N 0.000 description 1
- IOVCWXUNBOPUCH-UHFFFAOYSA-N Nitrous acid Chemical compound ON=O IOVCWXUNBOPUCH-UHFFFAOYSA-N 0.000 description 1
- 108020004485 Nonsense Codon Proteins 0.000 description 1
- 101710163270 Nuclease Proteins 0.000 description 1
- 102000015636 Oligopeptides Human genes 0.000 description 1
- 108010038807 Oligopeptides Proteins 0.000 description 1
- 101710093908 Outer capsid protein VP4 Proteins 0.000 description 1
- 101710135467 Outer capsid protein sigma-1 Proteins 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 208000002606 Paramyxoviridae Infections Diseases 0.000 description 1
- 102000003982 Parathyroid hormone Human genes 0.000 description 1
- 108090000445 Parathyroid hormone Proteins 0.000 description 1
- 102000001938 Plasminogen Activators Human genes 0.000 description 1
- 108010001014 Plasminogen Activators Proteins 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 239000004721 Polyphenylene oxide Substances 0.000 description 1
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
- 102100026531 Prelamin-A/C Human genes 0.000 description 1
- 108010076181 Proinsulin Proteins 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 101710176177 Protein A56 Proteins 0.000 description 1
- 101800004937 Protein C Proteins 0.000 description 1
- 102000017975 Protein C Human genes 0.000 description 1
- 108010042038 Protozoan Proteins Proteins 0.000 description 1
- 102000012751 Pyruvate Dehydrogenase Complex Human genes 0.000 description 1
- 108010090051 Pyruvate Dehydrogenase Complex Proteins 0.000 description 1
- 241000711798 Rabies lyssavirus Species 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 102400000834 Relaxin A chain Human genes 0.000 description 1
- 101800000074 Relaxin A chain Proteins 0.000 description 1
- 102400000610 Relaxin B chain Human genes 0.000 description 1
- 101710109558 Relaxin B chain Proteins 0.000 description 1
- 102100028255 Renin Human genes 0.000 description 1
- 108090000783 Renin Proteins 0.000 description 1
- 241000702263 Reovirus sp. Species 0.000 description 1
- 241000714474 Rous sarcoma virus Species 0.000 description 1
- 101800001700 Saposin-D Proteins 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- BQCADISMDOOEFD-UHFFFAOYSA-N Silver Chemical compound [Ag] BQCADISMDOOEFD-UHFFFAOYSA-N 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 208000001203 Smallpox Diseases 0.000 description 1
- 102100022831 Somatoliberin Human genes 0.000 description 1
- 101710142969 Somatoliberin Proteins 0.000 description 1
- 101710172711 Structural protein Proteins 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- 102000019197 Superoxide Dismutase Human genes 0.000 description 1
- 108010012715 Superoxide dismutase Proteins 0.000 description 1
- 108091008874 T cell receptors Proteins 0.000 description 1
- 230000005867 T cell response Effects 0.000 description 1
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 1
- DKGAVHZHDRPRBM-UHFFFAOYSA-N Tert-Butanol Chemical compound CC(C)(C)O DKGAVHZHDRPRBM-UHFFFAOYSA-N 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 108090000190 Thrombin Proteins 0.000 description 1
- 108010000499 Thromboplastin Proteins 0.000 description 1
- 102000002262 Thromboplastin Human genes 0.000 description 1
- 102000011923 Thyrotropin Human genes 0.000 description 1
- 108010061174 Thyrotropin Proteins 0.000 description 1
- 108090000373 Tissue Plasminogen Activator Proteins 0.000 description 1
- 108050006955 Tissue-type plasminogen activator Proteins 0.000 description 1
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 1
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 1
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 1
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 1
- 206010046865 Vaccinia virus infection Diseases 0.000 description 1
- 241000870995 Variola Species 0.000 description 1
- 241000700647 Variola virus Species 0.000 description 1
- 108010067390 Viral Proteins Proteins 0.000 description 1
- 241000710886 West Nile virus Species 0.000 description 1
- 241000710772 Yellow fever virus Species 0.000 description 1
- 239000000370 acceptor Substances 0.000 description 1
- 229940100228 acetyl coenzyme a Drugs 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 239000000488 activin Substances 0.000 description 1
- 125000002252 acyl group Chemical group 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 150000001299 aldehydes Chemical class 0.000 description 1
- 125000003342 alkenyl group Chemical group 0.000 description 1
- 125000002355 alkine group Chemical group 0.000 description 1
- 125000000217 alkyl group Chemical group 0.000 description 1
- 102000015395 alpha 1-Antitrypsin Human genes 0.000 description 1
- 108010050122 alpha 1-Antitrypsin Proteins 0.000 description 1
- 229940024142 alpha 1-antitrypsin Drugs 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 230000000689 aminoacylating effect Effects 0.000 description 1
- 230000001455 anti-clotting effect Effects 0.000 description 1
- 239000000868 anti-mullerian hormone Substances 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 125000004429 atom Chemical group 0.000 description 1
- 150000001540 azides Chemical class 0.000 description 1
- 125000000852 azido group Chemical group *N=[N+]=[N-] 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- 102000006635 beta-lactamase Human genes 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- 210000000988 bone and bone Anatomy 0.000 description 1
- ZADPBFCGQRWHPN-UHFFFAOYSA-N boronic acid Chemical compound OBO ZADPBFCGQRWHPN-UHFFFAOYSA-N 0.000 description 1
- 108010006025 bovine growth hormone Proteins 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- BBBFJLBPOGFECG-VJVYQDLKSA-N calcitonin Chemical compound N([C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(N)=O)C(C)C)C(=O)[C@@H]1CSSC[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1 BBBFJLBPOGFECG-VJVYQDLKSA-N 0.000 description 1
- 229960004015 calcitonin Drugs 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- NSQLIUXCMFBZME-MPVJKSABSA-N carperitide Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CSSC[C@@H](C(=O)N1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)=O)[C@@H](C)CC)C1=CC=CC=C1 NSQLIUXCMFBZME-MPVJKSABSA-N 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 238000006555 catalytic reaction Methods 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 239000012707 chemical precursor Substances 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- NKNDPYCGAZPOFS-UHFFFAOYSA-M copper(i) bromide Chemical compound Br[Cu] NKNDPYCGAZPOFS-UHFFFAOYSA-M 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 125000004093 cyano group Chemical group *C#N 0.000 description 1
- 208000025729 dengue disease Diseases 0.000 description 1
- 108700001680 des-(1-3)- insulin-like growth factor 1 Proteins 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 230000006334 disulfide bridging Effects 0.000 description 1
- 238000012377 drug delivery Methods 0.000 description 1
- 241001492478 dsDNA viruses, no RNA stage Species 0.000 description 1
- 229920002549 elastin Polymers 0.000 description 1
- 230000027721 electron transport chain Effects 0.000 description 1
- 230000009881 electrostatic interaction Effects 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 239000008393 encapsulating agent Substances 0.000 description 1
- 229940105423 erythropoietin Drugs 0.000 description 1
- 238000002270 exclusion chromatography Methods 0.000 description 1
- 229960004222 factor ix Drugs 0.000 description 1
- 108060002895 fibrillin Proteins 0.000 description 1
- 102000013370 fibrillin Human genes 0.000 description 1
- 229940126864 fibroblast growth factor Drugs 0.000 description 1
- 229940028334 follicle stimulating hormone Drugs 0.000 description 1
- 230000008014 freezing Effects 0.000 description 1
- 238000007710 freezing Methods 0.000 description 1
- 125000000524 functional group Chemical group 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 102000034356 gene-regulatory proteins Human genes 0.000 description 1
- 108091006104 gene-regulatory proteins Proteins 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- MASNOZXLGMXCHN-ZLPAWPGGSA-N glucagon Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC=1NC=NC=1)[C@@H](C)O)[C@@H](C)O)C1=CC=CC=C1 MASNOZXLGMXCHN-ZLPAWPGGSA-N 0.000 description 1
- 229960004666 glucagon Drugs 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 239000002622 gonadotropin Substances 0.000 description 1
- 230000005484 gravity Effects 0.000 description 1
- 239000000122 growth hormone Substances 0.000 description 1
- 125000001475 halogen functional group Chemical group 0.000 description 1
- 239000000185 hemagglutinin Substances 0.000 description 1
- 230000002607 hemopoietic effect Effects 0.000 description 1
- 208000005252 hepatitis A Diseases 0.000 description 1
- 125000000623 heterocyclic group Chemical group 0.000 description 1
- 235000014304 histidine Nutrition 0.000 description 1
- 150000002411 histidines Chemical class 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- XMBWDFGMSWQBCA-UHFFFAOYSA-N hydrogen iodide Chemical compound I XMBWDFGMSWQBCA-UHFFFAOYSA-N 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 238000003384 imaging method Methods 0.000 description 1
- 150000002466 imines Chemical class 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 230000016784 immunoglobulin production Effects 0.000 description 1
- 238000012744 immunostaining Methods 0.000 description 1
- 230000002637 immunotoxin Effects 0.000 description 1
- 229940051026 immunotoxin Drugs 0.000 description 1
- 239000002596 immunotoxin Substances 0.000 description 1
- 231100000608 immunotoxin Toxicity 0.000 description 1
- 230000001976 improved effect Effects 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 206010022000 influenza Diseases 0.000 description 1
- 239000000893 inhibin Substances 0.000 description 1
- ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 102000028416 insulin-like growth factor binding Human genes 0.000 description 1
- 108091022911 insulin-like growth factor binding Proteins 0.000 description 1
- 102000006495 integrins Human genes 0.000 description 1
- 108010044426 integrins Proteins 0.000 description 1
- 229940079322 interferon Drugs 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- JEIPFZHSYJVQDO-UHFFFAOYSA-N iron(III) oxide Inorganic materials O=[Fe]O[Fe]=O JEIPFZHSYJVQDO-UHFFFAOYSA-N 0.000 description 1
- YOBAEOGBNPPUQV-UHFFFAOYSA-N iron;trihydrate Chemical compound O.O.O.[Fe].[Fe] YOBAEOGBNPPUQV-UHFFFAOYSA-N 0.000 description 1
- 210000005053 lamin Anatomy 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 229940066294 lung surfactant Drugs 0.000 description 1
- 239000003580 lung surfactant Substances 0.000 description 1
- 229940040129 luteinizing hormone Drugs 0.000 description 1
- 210000001165 lymph node Anatomy 0.000 description 1
- 108010026228 mRNA guanylyltransferase Proteins 0.000 description 1
- 159000000003 magnesium salts Chemical class 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- WPBNNNQJVZRUHP-UHFFFAOYSA-L manganese(2+);methyl n-[[2-(methoxycarbonylcarbamothioylamino)phenyl]carbamothioyl]carbamate;n-[2-(sulfidocarbothioylamino)ethyl]carbamodithioate Chemical compound [Mn+2].[S-]C(=S)NCCNC([S-])=S.COC(=O)NC(=S)NC1=CC=CC=C1NC(=S)NC(=O)OC WPBNNNQJVZRUHP-UHFFFAOYSA-L 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 239000004005 microsphere Substances 0.000 description 1
- 108091005601 modified peptides Proteins 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 229940053128 nerve growth factor Drugs 0.000 description 1
- 229940032018 neurotrophin 3 Drugs 0.000 description 1
- BOPGDPNILDQYTO-NNYOXOHSSA-N nicotinamide-adenine dinucleotide Chemical compound C1=CCC(C(=O)N)=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OC[C@@H]2[C@H]([C@@H](O)[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)O)O1 BOPGDPNILDQYTO-NNYOXOHSSA-N 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 210000003463 organelle Anatomy 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 230000002138 osteoinductive effect Effects 0.000 description 1
- PSWJVKKJYCAPTI-UHFFFAOYSA-N oxido-oxo-phosphonophosphanylphosphanium Chemical compound OP(O)(=O)PP(=O)=O PSWJVKKJYCAPTI-UHFFFAOYSA-N 0.000 description 1
- 239000000199 parathyroid hormone Substances 0.000 description 1
- 229960001319 parathyroid hormone Drugs 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 230000035515 penetration Effects 0.000 description 1
- 230000002572 peristaltic effect Effects 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 229960005190 phenylalanine Drugs 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 230000000704 physical effect Effects 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 229940127126 plasminogen activator Drugs 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 230000008488 polyadenylation Effects 0.000 description 1
- 229920000570 polyether Polymers 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- 239000011591 potassium Substances 0.000 description 1
- OXCMYAYHXIHQOA-UHFFFAOYSA-N potassium;[2-butyl-5-chloro-3-[[4-[2-(1,2,4-triaza-3-azanidacyclopenta-1,4-dien-5-yl)phenyl]phenyl]methyl]imidazol-4-yl]methanol Chemical compound [K+].CCCCC1=NC(Cl)=C(CO)N1CC1=CC=C(C=2C(=CC=CC=2)C2=N[N-]N=N2)C=C1 OXCMYAYHXIHQOA-UHFFFAOYSA-N 0.000 description 1
- 108010087851 prorelaxin Proteins 0.000 description 1
- 229960000856 protein c Drugs 0.000 description 1
- 230000035484 reaction time Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 238000007634 remodeling Methods 0.000 description 1
- 230000003362 replicative effect Effects 0.000 description 1
- 238000004366 reverse phase liquid chromatography Methods 0.000 description 1
- 102220032030 rs72554328 Human genes 0.000 description 1
- 201000005404 rubella Diseases 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 150000003354 serine derivatives Chemical class 0.000 description 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
- 229910052709 silver Inorganic materials 0.000 description 1
- 239000004332 silver Substances 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 229940063675 spermine Drugs 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 125000000472 sulfonyl group Chemical group *S(*)(=O)=O 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 238000010189 synthetic method Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 229940126585 therapeutic drug Drugs 0.000 description 1
- 150000003568 thioethers Chemical class 0.000 description 1
- 150000003573 thiols Chemical class 0.000 description 1
- 229960004072 thrombin Drugs 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- VZCYOOQTPOCHFL-UHFFFAOYSA-N trans-butenedioic acid Natural products OC(=O)C=CC(O)=O VZCYOOQTPOCHFL-UHFFFAOYSA-N 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- 230000032258 transport Effects 0.000 description 1
- 201000008827 tuberculosis Diseases 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 241000701161 unidentified adenovirus Species 0.000 description 1
- 241001529453 unidentified herpesvirus Species 0.000 description 1
- 241000712461 unidentified influenza virus Species 0.000 description 1
- 241001430294 unidentified retrovirus Species 0.000 description 1
- 239000002691 unilamellar liposome Substances 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- VBEQCZHXXJYVRD-GACYYNSASA-N uroanthelone Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C(C)C)[C@@H](C)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CS)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O)C(C)C)[C@@H](C)CC)C1=CC=C(O)C=C1 VBEQCZHXXJYVRD-GACYYNSASA-N 0.000 description 1
- 229960005356 urokinase Drugs 0.000 description 1
- 208000007089 vaccinia Diseases 0.000 description 1
- 210000000605 viral structure Anatomy 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 238000009736 wetting Methods 0.000 description 1
- 239000000080 wetting agent Substances 0.000 description 1
- 229940051021 yellow-fever virus Drugs 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
- C07K14/01—DNA viruses
- C07K14/02—Hepadnaviridae, e.g. hepatitis B virus
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/12—Viral antigens
- A61K39/29—Hepatitis virus
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2730/00—Reverse transcribing DNA viruses
- C12N2730/00011—Details
- C12N2730/10011—Hepadnaviridae
- C12N2730/10111—Orthohepadnavirus, e.g. hepatitis B virus
- C12N2730/10122—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2730/00—Reverse transcribing DNA viruses
- C12N2730/00011—Details
- C12N2730/10011—Hepadnaviridae
- C12N2730/10111—Orthohepadnavirus, e.g. hepatitis B virus
- C12N2730/10123—Virus like particles [VLP]
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2770/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA ssRNA viruses positive-sense
- C12N2770/00011—Details
- C12N2770/32011—Picornaviridae
- C12N2770/32411—Hepatovirus, i.e. hepatitis A virus
- C12N2770/32423—Virus like particles [VLP]
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2770/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA ssRNA viruses positive-sense
- C12N2770/00011—Details
- C12N2770/32011—Picornaviridae
- C12N2770/32411—Hepatovirus, i.e. hepatitis A virus
- C12N2770/32434—Use of virus or viral component as vaccine, e.g. live-attenuated or inactivated virus, VLP, viral protein
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Virology (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Engineering & Computer Science (AREA)
- Biophysics (AREA)
- Medicinal Chemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- General Chemical & Material Sciences (AREA)
- Communicable Diseases (AREA)
- Microbiology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Biotechnology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201361755850P | 2013-01-23 | 2013-01-23 | |
| US61/755,850 | 2013-01-23 | ||
| US201361901243P | 2013-11-07 | 2013-11-07 | |
| US61/901,243 | 2013-11-07 | ||
| PCT/US2014/012586 WO2014116730A2 (en) | 2013-01-23 | 2014-01-22 | Stabilized hepatitis b core polypeptide |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2936092A1 true CA2936092A1 (en) | 2014-07-31 |
Family
ID=51228185
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA2936092A Abandoned CA2936092A1 (en) | 2013-01-23 | 2014-01-22 | Stabilized hepatitis b core polypeptide |
Country Status (5)
| Country | Link |
|---|---|
| US (1) | US9896483B2 (enExample) |
| EP (1) | EP2948469A4 (enExample) |
| JP (1) | JP2016507520A (enExample) |
| CA (1) | CA2936092A1 (enExample) |
| WO (1) | WO2014116730A2 (enExample) |
Families Citing this family (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CA2936092A1 (en) | 2013-01-23 | 2014-07-31 | The Board Of Trustees Of The Leland Stanford Junior University | Stabilized hepatitis b core polypeptide |
| HK1246654A1 (zh) | 2015-01-15 | 2018-09-14 | University Of Copenhagen | 具有有效表位显示的病毒样颗粒 |
| EP3368068B1 (en) | 2015-10-30 | 2020-11-18 | University of Copenhagen | Virus like particle with efficient epitope display |
| CN106636016B (zh) * | 2017-02-24 | 2020-03-17 | 天津大学 | 一种通过正负电荷引入辅助病毒样颗粒自组装的方法和应用 |
| EP3723796A1 (en) * | 2017-12-13 | 2020-10-21 | CureVac AG | Flavivirus vaccine |
| US11261216B2 (en) * | 2018-12-28 | 2022-03-01 | The Board Of Trustees Of The Leland Stanford Junior University | Engineered hepatitis B core polypeptide |
| CN109666067A (zh) * | 2019-01-07 | 2019-04-23 | 中国科学院过程工程研究所 | 一种重组病毒样颗粒及其制备方法和用途 |
| WO2020145901A1 (en) * | 2019-01-11 | 2020-07-16 | Agency For Science, Technology And Research | Use of hla-a*11:01-restricted hepatitis b virus (hbv) peptides for identifying hbv-specific cd8+ t cells |
Family Cites Families (56)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6099846A (en) | 1992-10-14 | 2000-08-08 | The Board Of Trustees Of The Leland Stanford Junior University | Enhancement of B cell lymphoma and tumor resistance using idiotype/cytokine conjugates |
| US6239116B1 (en) | 1994-07-15 | 2001-05-29 | University Of Iowa Research Foundation | Immunostimulatory nucleic acid molecules |
| US6429199B1 (en) | 1994-07-15 | 2002-08-06 | University Of Iowa Research Foundation | Immunostimulatory nucleic acid molecules for activating dendritic cells |
| ES2366201T3 (es) | 1994-07-15 | 2011-10-18 | University Of Iowa Research Foundation | Oligonucleótidos inmunmoduladores. |
| US6207646B1 (en) | 1994-07-15 | 2001-03-27 | University Of Iowa Research Foundation | Immunostimulatory nucleic acid molecules |
| US5968767A (en) | 1996-06-07 | 1999-10-19 | Genentech, Inc. | Methods for in vitro protein synthesis |
| WO1998035062A1 (en) | 1997-02-07 | 1998-08-13 | Lingappa Jaisri R | Multistep, atp-dependent cell-free system for the assembly of human immunodeficiency virus capsids |
| US6406705B1 (en) | 1997-03-10 | 2002-06-18 | University Of Iowa Research Foundation | Use of nucleic acids containing unmethylated CpG dinucleotide as an adjuvant |
| ATE252596T1 (de) | 1997-06-06 | 2003-11-15 | Dynavax Tech Corp | Immunstimulierende oligonucleotide, zusammensetzungen davon, und verfahren zur verwendung davon |
| TR200002338T2 (tr) * | 1998-02-12 | 2002-06-21 | Immune Complex Corporation | Stratejik olarak yenilenmiş hepatit B çekirdek proteinler. |
| WO2000023955A1 (en) | 1998-10-21 | 2000-04-27 | The Government Of The United States Of America, Represented By The Secretary, Department Of Health And Human Services | Virus-like particles for the induction of autoantibodies |
| EP2360174B1 (en) * | 1998-12-04 | 2014-04-09 | Biogen Idec MA Inc. | HBV core antigen particles with multiple immunogenic components attached via peptide ligands |
| US6994986B2 (en) | 1999-03-17 | 2006-02-07 | The Board Of Trustees Of The Leland Stanford University | In vitro synthesis of polypeptides by optimizing amino acid metabolism |
| US6168931B1 (en) | 1999-03-17 | 2001-01-02 | The Board Of Trustees Of The Leland Stanford Junior University | Enhanced in vitro synthesis of biological macromolecules using a novel ATP regeneration system |
| US6337191B1 (en) | 1999-03-22 | 2002-01-08 | The Board Of Trustees Of The Leland Stanford Junior University | Vitro protein synthesis using glycolytic intermediates as an energy source |
| US6586207B2 (en) | 2000-05-26 | 2003-07-01 | California Institute Of Technology | Overexpression of aminoacyl-tRNA synthetases for efficient production of engineered proteins containing amino acid analogues |
| US6548276B2 (en) | 2000-09-06 | 2003-04-15 | The Board Of Trustees Of The Leland Stanford Junior University | Enhanced in vitro synthesis of active proteins containing disulfide bonds |
| US7041479B2 (en) | 2000-09-06 | 2006-05-09 | The Board Of Trustess Of The Leland Stanford Junior University | Enhanced in vitro synthesis of active proteins containing disulfide bonds |
| JP2005502322A (ja) | 2001-04-19 | 2005-01-27 | ザ スクリップス リサーチ インスティテュート | 非天然アミノ酸のインビボ組込み |
| US20030099668A1 (en) | 2001-09-14 | 2003-05-29 | Cytos Biotechnology Ag | Packaging of immunostimulatory substances into virus-like particles: method of preparation and use |
| AU2002366710A1 (en) | 2001-12-20 | 2003-07-09 | The Government Of The United States Of America As Represented By The Secretary Of The Department Of | USE OF CpG OLIGODEOXYNUCLEOTIDES TO INDUCE ANGIOGENESIS |
| US8466116B2 (en) | 2001-12-20 | 2013-06-18 | The Unites States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Use of CpG oligodeoxynucleotides to induce epithelial cell growth |
| JP4638225B2 (ja) | 2002-05-30 | 2011-02-23 | ザ スクリプス リサーチ インスティテュート | 銅を触媒とするアジドとアセチレンのライゲーション |
| AU2003259912B2 (en) | 2002-08-19 | 2008-10-23 | The Board Of Trustees Of The Leland Stanford Junior University | Improved methods of in vitro protein synthesis |
| WO2004022585A1 (ja) * | 2002-09-06 | 2004-03-18 | Advanced Life Science Institute, Inc. | 粒子形成能を有するhbvプレコア蛋白質 |
| AU2004217526B2 (en) | 2003-02-28 | 2010-02-04 | St. Jude Children's Research Hospital Inc. | T cell regulation |
| WO2004084940A1 (en) | 2003-03-26 | 2004-10-07 | Cytos Biotechnology Ag | Packaging of immunostimulatory oligonucleotides into virus-like particles: method of preparation and use |
| US7888063B2 (en) | 2003-06-18 | 2011-02-15 | The Scripps Research Institute | Unnatural reactive amino acid genetic code additions |
| WO2005005614A2 (en) * | 2003-07-03 | 2005-01-20 | Pecos Labs, Inc. | Combined b-cell and t-cell epitopes on vlp for improved vaccines |
| US7341852B2 (en) | 2003-07-18 | 2008-03-11 | The Board Of Trustees Of The Leland Stanford Junior University | Methods of decoupling reaction scale and protein synthesis yield in batch mode |
| US20050054044A1 (en) | 2003-07-18 | 2005-03-10 | The Board Of Trustees Of The Leland Stanford Junior University | Method of alleviating nucleotide limitations for in vitro protein synthesis |
| JP2007510622A (ja) | 2003-10-08 | 2007-04-26 | ザ・フェインスタイン・インスティチュート・フォー・メディカル・リサーチ | Ｂ細胞慢性リンパ性白血病の診断及び治療のための方法及び組成物 |
| ES2532608T3 (es) | 2003-11-20 | 2015-03-30 | The Board Of Trustees Of The Leland Stanford Junior University | Métodos mejorados de síntesis proteica in vitro |
| US20050170551A1 (en) | 2004-02-04 | 2005-08-04 | Strip David R. | Manufacture of flat panel light emitting devices |
| EP1773303A2 (en) * | 2004-05-25 | 2007-04-18 | Chimeracore, Inc. | Self-assembling nanoparticle drug delivery system |
| ES2666693T3 (es) | 2004-09-21 | 2018-05-07 | The Scripps Research Institute | Incorporación in vivo de alquinil aminoácidos a proteínas en eubacterias |
| WO2006065751A2 (en) | 2004-12-13 | 2006-06-22 | Government Of The United States Of America, Represented By The Secretary, Department Of Health And Human Services | Cpg oligonucleotide prodrugs, compositions thereof and associated therapeutic methods |
| US8067011B2 (en) * | 2006-04-07 | 2011-11-29 | Chimeros, Inc. | Compositions and methods for treating B-cell malignancies |
| US20080096819A1 (en) | 2006-05-02 | 2008-04-24 | Allozyne, Inc. | Amino acid substituted molecules |
| WO2008002663A2 (en) | 2006-06-28 | 2008-01-03 | The Board Of Trustees Of The Leland Stanford Junior University | Immunogenic protein constructs |
| EP2035554B1 (en) | 2006-06-29 | 2013-04-24 | The Board of Trustees of The Leland Stanford Junior University | Cell-free synthesis of proteins containing unnatural amino acids |
| WO2008002673A2 (en) | 2006-06-29 | 2008-01-03 | The Board Of Trustees Of The Leland Stanford Junior University | Cell-free synthesis of virus like particles |
| ES2465473T3 (es) | 2006-09-08 | 2014-06-05 | Ambrx, Inc. | Transcripción de arnt supresor en células de vertebrado |
| CA2673765A1 (en) | 2007-01-18 | 2008-07-24 | The Board Of Trustees Of The Leland Stanford Junior University | Enhanced cell-free synthesis of active proteins containing disulfide bonds |
| CA2707840A1 (en) | 2007-08-20 | 2009-02-26 | Allozyne, Inc. | Amino acid substituted molecules |
| US8445706B2 (en) | 2008-09-05 | 2013-05-21 | Board Of Trustees Of Northern Illinois University | Unnatural amino acids capable of covalently modifying protein phosphatases and their use as general and specific inhibitors and probes |
| WO2010042755A2 (en) * | 2008-10-08 | 2010-04-15 | Chimeros Inc. | Chimeric therapeutics, compositions, and methods for using same |
| US20100168402A1 (en) | 2008-11-14 | 2010-07-01 | Bundy Bradley C | Direct Attachment of Polypeptides to Virus Like Particles |
| US8324149B2 (en) | 2008-11-18 | 2012-12-04 | The Board Of Trustees Of The Leland Stanford Junior University | Encapsidation of heterologous entities into virus-like particles |
| WO2011057134A1 (en) | 2009-11-05 | 2011-05-12 | Novici Biotech Llc | Generation of antigenic virus-like particles through protein-protein linkages |
| US8685416B2 (en) | 2010-03-02 | 2014-04-01 | The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Compositions and methods for the treatment of cancer |
| EP2747774A4 (en) * | 2011-09-09 | 2015-02-11 | Biomed Realty L P | METHOD AND COMPOSITIONS FOR CONTROLLING VIRUS PROTECTION |
| EP3520809B1 (en) | 2012-02-03 | 2025-08-06 | Emory University | Immunostimulatory compositions. |
| CA2936092A1 (en) | 2013-01-23 | 2014-07-31 | The Board Of Trustees Of The Leland Stanford Junior University | Stabilized hepatitis b core polypeptide |
| WO2014145932A2 (en) | 2013-03-15 | 2014-09-18 | Bullet Biotechnology, Inc. | Specific multivalent virus-like particle vaccines and uses thereof |
| US20170035864A1 (en) | 2013-12-09 | 2017-02-09 | Bullet Biotechnology, Inc. | SPECIFIC VIRUS-LIKE PARTICLE-CpG OLIGONUCLEOTIDE VACCINES AND USES THEREOF |
-
2014
- 2014-01-22 CA CA2936092A patent/CA2936092A1/en not_active Abandoned
- 2014-01-22 JP JP2015555242A patent/JP2016507520A/ja active Pending
- 2014-01-22 EP EP14743102.7A patent/EP2948469A4/en not_active Withdrawn
- 2014-01-22 WO PCT/US2014/012586 patent/WO2014116730A2/en not_active Ceased
-
2015
- 2015-07-23 US US14/807,787 patent/US9896483B2/en active Active
Also Published As
| Publication number | Publication date |
|---|---|
| EP2948469A2 (en) | 2015-12-02 |
| US9896483B2 (en) | 2018-02-20 |
| WO2014116730A3 (en) | 2014-10-23 |
| WO2014116730A2 (en) | 2014-07-31 |
| JP2016507520A (ja) | 2016-03-10 |
| EP2948469A4 (en) | 2016-11-02 |
| US20150329598A1 (en) | 2015-11-19 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CA2936092A1 (en) | Stabilized hepatitis b core polypeptide | |
| Patel et al. | Surface functionalization of virus-like particles by direct conjugation using azide− alkyne click chemistry | |
| Bundy et al. | Escherichia coli‐based cell‐free synthesis of virus‐like particles | |
| AU2007325952B8 (en) | Cell-free synthesis of proteins containing unnatural amino acids | |
| US20090317861A1 (en) | Cell-free synthesis of virus like particles | |
| CA2405438A1 (en) | Hepatitis b core antigen fusion proteins | |
| CA3094859A1 (en) | Proteolipid vesicles formulated with fusion associated small transmembrane proteins | |
| EP2852396A2 (en) | Influenza vaccine constructs | |
| US20230201337A1 (en) | Vaccine compositions comprising endogenous gag polypeptides | |
| US20100168402A1 (en) | Direct Attachment of Polypeptides to Virus Like Particles | |
| JP2021193893A (ja) | 改変型ｐｉｇｇｙＢａｃトランスポゼースのポリペプチド、それをコードするポリヌクレオチド、導入キャリア、キット、細胞のゲノムに目的配列を組込む方法及び細胞製造方法 | |
| US9550813B2 (en) | Disulfide stabilized foldon polypeptides | |
| WO2018074558A1 (ja) | 複合ポリペプチド単量体、細胞浸透機能を有する当該複合ポリペプチドの単量体の会合体、及び、当該会合体を有効成分とする皮下、皮内、経皮又は筋肉内投与用ノロウイルスコンポーネントワクチン | |
| US9255255B2 (en) | Synthesis of linear and branched polymers of polypeptides through direct conjugation | |
| US20220281924A1 (en) | Engineered hepatitis b core polypeptide | |
| US9296792B2 (en) | Ordered flagellin array as an immunostimulant | |
| FR3113288A1 (fr) | Approche vaccinale basée sur des antigènes viraux trimériques | |
| JP7609793B2 (ja) | バイオコンジュゲーションのために操作されたｃｄ４７の細胞外ドメイン | |
| ES2789073T3 (es) | Método de fabricación de una proteína terapéutica | |
| Kumar et al. | Unveiling Fundamentals and Research Opportunities of mRNA Technology | |
| Fogarty | Development of a Modular Virus-like Particle Vaccine Platform | |
| Brown | Bacteriophage Qβ: a versatile platform for Nanoengineering |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FZDE | Discontinued |
Effective date: 20190122 |