JPH10500298A - 三量体化ポリペプチド、その製造及び使用 - Google Patents
三量体化ポリペプチド、その製造及び使用Info
- Publication number
- JPH10500298A JPH10500298A JP7529462A JP52946295A JPH10500298A JP H10500298 A JPH10500298 A JP H10500298A JP 7529462 A JP7529462 A JP 7529462A JP 52946295 A JP52946295 A JP 52946295A JP H10500298 A JPH10500298 A JP H10500298A
- Authority
- JP
- Japan
- Prior art keywords
- polypeptide
- amino acid
- neck region
- sequence
- trimer
- 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- Withdrawn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 303
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 185
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 161
- 238000004519 manufacturing process Methods 0.000 title claims abstract description 12
- 150000001413 amino acids Chemical class 0.000 claims abstract description 112
- 238000000034 method Methods 0.000 claims abstract description 69
- 102000008186 Collagen Human genes 0.000 claims abstract description 53
- 108010035532 Collagen Proteins 0.000 claims abstract description 53
- 229920001436 collagen Polymers 0.000 claims abstract description 52
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 35
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 35
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 35
- 108090000909 Collectins Proteins 0.000 claims abstract description 25
- 102000004405 Collectins Human genes 0.000 claims abstract description 25
- 238000005829 trimerization reaction Methods 0.000 claims abstract description 21
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract description 15
- 108020001580 protein domains Proteins 0.000 claims abstract description 9
- 108060003951 Immunoglobulin Proteins 0.000 claims abstract description 5
- 102000018358 immunoglobulin Human genes 0.000 claims abstract description 5
- 239000013638 trimer Substances 0.000 claims description 74
- 230000014509 gene expression Effects 0.000 claims description 39
- 210000004027 cell Anatomy 0.000 claims description 27
- 108010007127 Pulmonary Surfactant-Associated Protein D Proteins 0.000 claims description 23
- 239000000126 substance Substances 0.000 claims description 14
- 239000013598 vector Substances 0.000 claims description 14
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims description 13
- 210000004899 c-terminal region Anatomy 0.000 claims description 9
- 239000000047 product Substances 0.000 claims description 9
- 101710193968 Collectin-43 Proteins 0.000 claims description 6
- 239000002253 acid Substances 0.000 claims description 6
- 108010018927 conglutinin Proteins 0.000 claims description 6
- QCUFYOBGGZSFHY-UHFFFAOYSA-N depsidomycin Chemical compound O=C1C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(NC=O)C(C)CC)C(C)OC(=O)C2CCCNN2C(=O)C(CC(C)C)NC(=O)C2CCCNN21 QCUFYOBGGZSFHY-UHFFFAOYSA-N 0.000 claims description 6
- 230000001105 regulatory effect Effects 0.000 claims description 6
- 108091026890 Coding region Proteins 0.000 claims description 4
- 230000002209 hydrophobic effect Effects 0.000 claims description 4
- 238000002955 isolation Methods 0.000 claims description 4
- 239000002773 nucleotide Substances 0.000 claims description 4
- 125000003729 nucleotide group Chemical group 0.000 claims description 4
- 238000012258 culturing Methods 0.000 claims description 3
- 239000007861 trimeric product Substances 0.000 claims 1
- 238000001816 cooling Methods 0.000 abstract description 12
- 238000010438 heat treatment Methods 0.000 abstract description 10
- -1 for example Chemical class 0.000 abstract description 4
- 238000011081 inoculation Methods 0.000 abstract 1
- 229920001542 oligosaccharide Polymers 0.000 abstract 1
- 150000002482 oligosaccharides Chemical group 0.000 abstract 1
- 235000001014 amino acid Nutrition 0.000 description 80
- 108090000623 proteins and genes Proteins 0.000 description 50
- 239000002523 lectin Substances 0.000 description 46
- 102000004169 proteins and genes Human genes 0.000 description 44
- 235000018102 proteins Nutrition 0.000 description 35
- 108020004414 DNA Proteins 0.000 description 33
- 102000037865 fusion proteins Human genes 0.000 description 32
- 108020001507 fusion proteins Proteins 0.000 description 32
- 101000632467 Homo sapiens Pulmonary surfactant-associated protein D Proteins 0.000 description 22
- 239000012634 fragment Substances 0.000 description 22
- 102000004856 Lectins Human genes 0.000 description 21
- 108090001090 Lectins Proteins 0.000 description 21
- 238000006243 chemical reaction Methods 0.000 description 20
- 239000013612 plasmid Substances 0.000 description 20
- 238000004458 analytical method Methods 0.000 description 19
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 19
- 102000004190 Enzymes Human genes 0.000 description 17
- 108090000790 Enzymes Proteins 0.000 description 17
- 230000027455 binding Effects 0.000 description 17
- 230000015572 biosynthetic process Effects 0.000 description 17
- 229940088598 enzyme Drugs 0.000 description 17
- 239000000243 solution Substances 0.000 description 17
- 102000005720 Glutathione transferase Human genes 0.000 description 16
- 108010070675 Glutathione transferase Proteins 0.000 description 16
- 238000004132 cross linking Methods 0.000 description 14
- 102000029816 Collagenase Human genes 0.000 description 13
- 108060005980 Collagenase Proteins 0.000 description 13
- 102100027845 Pulmonary surfactant-associated protein D Human genes 0.000 description 13
- 108090000190 Thrombin Proteins 0.000 description 13
- 229960002424 collagenase Drugs 0.000 description 13
- 229960004072 thrombin Drugs 0.000 description 13
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 12
- 239000004971 Cross linker Substances 0.000 description 10
- 102000003930 C-Type Lectins Human genes 0.000 description 9
- 108090000342 C-Type Lectins Proteins 0.000 description 9
- 230000001580 bacterial effect Effects 0.000 description 9
- 239000000872 buffer Substances 0.000 description 9
- 230000029087 digestion Effects 0.000 description 9
- 230000004927 fusion Effects 0.000 description 9
- 239000002953 phosphate buffered saline Substances 0.000 description 9
- 239000003153 chemical reaction reagent Substances 0.000 description 8
- 238000002474 experimental method Methods 0.000 description 8
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 8
- 238000010899 nucleation Methods 0.000 description 8
- 108091008146 restriction endonucleases Proteins 0.000 description 8
- 206010039509 Scab Diseases 0.000 description 7
- 238000003776 cleavage reaction Methods 0.000 description 7
- 239000013604 expression vector Substances 0.000 description 7
- 238000000746 purification Methods 0.000 description 7
- 239000011347 resin Substances 0.000 description 7
- 229920005989 resin Polymers 0.000 description 7
- 230000007017 scission Effects 0.000 description 7
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 6
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 6
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 6
- 125000000539 amino acid group Chemical group 0.000 description 6
- VYLDEYYOISNGST-UHFFFAOYSA-N bissulfosuccinimidyl suberate Chemical compound O=C1C(S(=O)(=O)O)CC(=O)N1OC(=O)CCCCCCC(=O)ON1C(=O)C(S(O)(=O)=O)CC1=O VYLDEYYOISNGST-UHFFFAOYSA-N 0.000 description 6
- NKLPQNGYXWVELD-UHFFFAOYSA-M coomassie brilliant blue Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=C1 NKLPQNGYXWVELD-UHFFFAOYSA-M 0.000 description 6
- 230000001965 increasing effect Effects 0.000 description 6
- 239000003446 ligand Substances 0.000 description 6
- 230000006911 nucleation Effects 0.000 description 6
- 239000011780 sodium chloride Substances 0.000 description 6
- 238000005119 centrifugation Methods 0.000 description 5
- 150000001875 compounds Chemical class 0.000 description 5
- 239000000539 dimer Substances 0.000 description 5
- 238000011160 research Methods 0.000 description 5
- 238000001542 size-exclusion chromatography Methods 0.000 description 5
- 238000010186 staining Methods 0.000 description 5
- 238000006467 substitution reaction Methods 0.000 description 5
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 4
- 229920000936 Agarose Polymers 0.000 description 4
- 241000894006 Bacteria Species 0.000 description 4
- 108010087870 Mannose-Binding Lectin Proteins 0.000 description 4
- 102000009112 Mannose-Binding Lectin Human genes 0.000 description 4
- 108091034117 Oligonucleotide Proteins 0.000 description 4
- 108700026244 Open Reading Frames Proteins 0.000 description 4
- 125000003277 amino group Chemical group 0.000 description 4
- 230000006399 behavior Effects 0.000 description 4
- 230000008901 benefit Effects 0.000 description 4
- 238000006555 catalytic reaction Methods 0.000 description 4
- 230000008859 change Effects 0.000 description 4
- 210000000349 chromosome Anatomy 0.000 description 4
- 239000002299 complementary DNA Substances 0.000 description 4
- 239000003431 cross linking reagent Substances 0.000 description 4
- 238000004925 denaturation Methods 0.000 description 4
- 230000036425 denaturation Effects 0.000 description 4
- 238000010586 diagram Methods 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 229930195733 hydrocarbon Natural products 0.000 description 4
- 150000002430 hydrocarbons Chemical class 0.000 description 4
- 125000001165 hydrophobic group Chemical group 0.000 description 4
- 230000003993 interaction Effects 0.000 description 4
- 230000004048 modification Effects 0.000 description 4
- 238000012986 modification Methods 0.000 description 4
- 238000006384 oligomerization reaction Methods 0.000 description 4
- 230000002829 reductive effect Effects 0.000 description 4
- 241000894007 species Species 0.000 description 4
- ZPEILGDXTSIWFX-UHFFFAOYSA-N 2-[[1,3-dihydroxy-2-(hydroxymethyl)propan-2-yl]amino]acetic acid propane-1,2,3-triol prop-2-enamide Chemical compound NC(=O)C=C.OCC(O)CO.OCC(CO)(CO)NCC(O)=O.OCC(CO)(CO)NCC(O)=O.OCC(CO)(CO)NCC(O)=O ZPEILGDXTSIWFX-UHFFFAOYSA-N 0.000 description 3
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 3
- 241000672609 Escherichia coli BL21 Species 0.000 description 3
- 239000004471 Glycine Substances 0.000 description 3
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 3
- 239000004472 Lysine Substances 0.000 description 3
- 238000007792 addition Methods 0.000 description 3
- 238000010367 cloning Methods 0.000 description 3
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 3
- 238000010828 elution Methods 0.000 description 3
- VWWQXMAJTJZDQX-UYBVJOGSSA-N flavin adenine dinucleotide Chemical compound C1=NC2=C(N)N=CN=C2N1[C@@H]([C@H](O)[C@@H]1O)O[C@@H]1CO[P@](O)(=O)O[P@@](O)(=O)OC[C@@H](O)[C@@H](O)[C@@H](O)CN1C2=NC(=O)NC(=O)C2=NC2=C1C=C(C)C(C)=C2 VWWQXMAJTJZDQX-UYBVJOGSSA-N 0.000 description 3
- 235000019162 flavin adenine dinucleotide Nutrition 0.000 description 3
- 239000011714 flavin adenine dinucleotide Substances 0.000 description 3
- 239000011768 flavin mononucleotide Substances 0.000 description 3
- FVTCRASFADXXNN-SCRDCRAPSA-N flavin mononucleotide Chemical compound OP(=O)(O)OC[C@@H](O)[C@@H](O)[C@@H](O)CN1C=2C=C(C)C(C)=CC=2N=C2C1=NC(=O)NC2=O FVTCRASFADXXNN-SCRDCRAPSA-N 0.000 description 3
- 229940013640 flavin mononucleotide Drugs 0.000 description 3
- FVTCRASFADXXNN-UHFFFAOYSA-N flavin mononucleotide Natural products OP(=O)(O)OCC(O)C(O)C(O)CN1C=2C=C(C)C(C)=CC=2N=C2C1=NC(=O)NC2=O FVTCRASFADXXNN-UHFFFAOYSA-N 0.000 description 3
- 229940093632 flavin-adenine dinucleotide Drugs 0.000 description 3
- 125000000524 functional group Chemical group 0.000 description 3
- 125000000404 glutamine group Chemical group N[C@@H](CCC(N)=O)C(=O)* 0.000 description 3
- 230000006698 induction Effects 0.000 description 3
- 239000012139 lysis buffer Substances 0.000 description 3
- 239000011159 matrix material Substances 0.000 description 3
- 238000005259 measurement Methods 0.000 description 3
- 238000002156 mixing Methods 0.000 description 3
- 239000000178 monomer Substances 0.000 description 3
- 230000002441 reversible effect Effects 0.000 description 3
- 235000019231 riboflavin-5'-phosphate Nutrition 0.000 description 3
- 102220201851 rs143406017 Human genes 0.000 description 3
- 238000012163 sequencing technique Methods 0.000 description 3
- 238000001228 spectrum Methods 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- 239000004215 Carbon black (E152) Substances 0.000 description 2
- 241000588724 Escherichia coli Species 0.000 description 2
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 2
- 108091028043 Nucleic acid sequence Proteins 0.000 description 2
- 108010007100 Pulmonary Surfactant-Associated Protein A Proteins 0.000 description 2
- 102000007615 Pulmonary Surfactant-Associated Protein A Human genes 0.000 description 2
- 101100163901 Rattus norvegicus Asic2 gene Proteins 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 108091081024 Start codon Proteins 0.000 description 2
- 238000002835 absorbance Methods 0.000 description 2
- 238000005571 anion exchange chromatography Methods 0.000 description 2
- 239000000427 antigen Substances 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
- 108091007433 antigens Proteins 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 description 2
- RYYVLZVUVIJVGH-UHFFFAOYSA-N caffeine Chemical compound CN1C(=O)N(C)C(=O)C2=C1N=CN2C RYYVLZVUVIJVGH-UHFFFAOYSA-N 0.000 description 2
- 125000000837 carbohydrate group Chemical group 0.000 description 2
- 230000006037 cell lysis Effects 0.000 description 2
- 238000007385 chemical modification Methods 0.000 description 2
- 238000000978 circular dichroism spectroscopy Methods 0.000 description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Chemical group SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
- 235000018417 cysteine Nutrition 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 238000001976 enzyme digestion Methods 0.000 description 2
- 239000013613 expression plasmid Substances 0.000 description 2
- 125000004072 flavinyl group Chemical group 0.000 description 2
- 230000006870 function Effects 0.000 description 2
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 2
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 2
- LEQAOMBKQFMDFZ-UHFFFAOYSA-N glyoxal Chemical group O=CC=O LEQAOMBKQFMDFZ-UHFFFAOYSA-N 0.000 description 2
- 238000003505 heat denaturation Methods 0.000 description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 2
- 210000004408 hybridoma Anatomy 0.000 description 2
- 238000007901 in situ hybridization Methods 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 238000010348 incorporation Methods 0.000 description 2
- 238000003780 insertion Methods 0.000 description 2
- 230000037431 insertion Effects 0.000 description 2
- 239000002502 liposome Substances 0.000 description 2
- 239000006166 lysate Substances 0.000 description 2
- 210000004962 mammalian cell Anatomy 0.000 description 2
- 238000002844 melting Methods 0.000 description 2
- 230000008018 melting Effects 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- BQJCRHHNABKAKU-KBQPJGBKSA-N morphine Chemical compound O([C@H]1[C@H](C=C[C@H]23)O)C4=C5[C@@]12CCN(C)[C@@H]3CC5=CC=C4O BQJCRHHNABKAKU-KBQPJGBKSA-N 0.000 description 2
- 150000002894 organic compounds Chemical class 0.000 description 2
- 238000012856 packing Methods 0.000 description 2
- 230000004962 physiological condition Effects 0.000 description 2
- 238000003752 polymerase chain reaction Methods 0.000 description 2
- 239000002244 precipitate Substances 0.000 description 2
- 150000003141 primary amines Chemical class 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 230000017854 proteolysis Effects 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 230000008929 regeneration Effects 0.000 description 2
- 238000011069 regeneration method Methods 0.000 description 2
- 125000006853 reporter group Chemical group 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- MPLHNVLQVRSVEE-UHFFFAOYSA-N texas red Chemical compound [O-]S(=O)(=O)C1=CC(S(Cl)(=O)=O)=CC=C1C(C1=CC=2CCCN3CCCC(C=23)=C1O1)=C2C1=C(CCC1)C3=[N+]1CCCC3=C2 MPLHNVLQVRSVEE-UHFFFAOYSA-N 0.000 description 2
- 238000001890 transfection Methods 0.000 description 2
- 238000012546 transfer Methods 0.000 description 2
- 230000007704 transition Effects 0.000 description 2
- 241000701447 unidentified baculovirus Species 0.000 description 2
- 230000003612 virological effect Effects 0.000 description 2
- 229910052727 yttrium Inorganic materials 0.000 description 2
- VZQHRKZCAZCACO-PYJNHQTQSA-N (2s)-2-[[(2s)-2-[2-[[(2s)-2-[[(2s)-2-amino-5-(diaminomethylideneamino)pentanoyl]amino]propanoyl]amino]prop-2-enoylamino]-3-methylbutanoyl]amino]propanoic acid Chemical group OC(=O)[C@H](C)NC(=O)[C@H](C(C)C)NC(=O)C(=C)NC(=O)[C@H](C)NC(=O)[C@@H](N)CCCNC(N)=N VZQHRKZCAZCACO-PYJNHQTQSA-N 0.000 description 1
- OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 description 1
- QEQDLKUMPUDNPG-UHFFFAOYSA-N 2-(7-amino-4-methyl-2-oxochromen-3-yl)acetic acid Chemical compound C1=C(N)C=CC2=C1OC(=O)C(CC(O)=O)=C2C QEQDLKUMPUDNPG-UHFFFAOYSA-N 0.000 description 1
- GOLORTLGFDVFDW-UHFFFAOYSA-N 3-(1h-benzimidazol-2-yl)-7-(diethylamino)chromen-2-one Chemical compound C1=CC=C2NC(C3=CC4=CC=C(C=C4OC3=O)N(CC)CC)=NC2=C1 GOLORTLGFDVFDW-UHFFFAOYSA-N 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 108010017384 Blood Proteins Proteins 0.000 description 1
- 102000004506 Blood Proteins Human genes 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 102000001187 Collagen Type III Human genes 0.000 description 1
- 108010069502 Collagen Type III Proteins 0.000 description 1
- RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 0.000 description 1
- 241000699800 Cricetinae Species 0.000 description 1
- 102000018832 Cytochromes Human genes 0.000 description 1
- 108010052832 Cytochromes Proteins 0.000 description 1
- 108020003215 DNA Probes Proteins 0.000 description 1
- 239000003298 DNA probe Substances 0.000 description 1
- 238000007900 DNA-DNA hybridization Methods 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 108700024394 Exon Proteins 0.000 description 1
- 102000009842 Fibril-Associated Collagens Human genes 0.000 description 1
- 108010020305 Fibril-Associated Collagens Proteins 0.000 description 1
- 108700028146 Genetic Enhancer Elements Proteins 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 108010024636 Glutathione Proteins 0.000 description 1
- ABPRMMYHROQBLY-NKWVEPMBSA-N Gly-Ser-Pro Chemical compound C1C[C@@H](N(C1)C(=O)[C@H](CO)NC(=O)CN)C(=O)O ABPRMMYHROQBLY-NKWVEPMBSA-N 0.000 description 1
- 101710154606 Hemagglutinin Proteins 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 102000015696 Interleukins Human genes 0.000 description 1
- 108010063738 Interleukins Proteins 0.000 description 1
- LPHGQDQBBGAPDZ-UHFFFAOYSA-N Isocaffeine Natural products CN1C(=O)N(C)C(=O)C2=C1N(C)C=N2 LPHGQDQBBGAPDZ-UHFFFAOYSA-N 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical group SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 1
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 description 1
- 238000005481 NMR spectroscopy Methods 0.000 description 1
- 108090000189 Neuropeptides 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
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
- 108010004729 Phycoerythrin Proteins 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 101710176177 Protein A56 Proteins 0.000 description 1
- 108010041520 Pulmonary Surfactant-Associated Proteins Proteins 0.000 description 1
- 102000000528 Pulmonary Surfactant-Associated Proteins Human genes 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- MEFKEPWMEQBLKI-AIRLBKTGSA-N S-adenosyl-L-methioninate Chemical compound O[C@@H]1[C@H](O)[C@@H](C[S+](CC[C@H](N)C([O-])=O)C)O[C@H]1N1C2=NC=NC(N)=C2N=C1 MEFKEPWMEQBLKI-AIRLBKTGSA-N 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 101150052859 Slc9a1 gene Proteins 0.000 description 1
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 1
- 108010019965 Spectrin Proteins 0.000 description 1
- 102000005890 Spectrin Human genes 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- 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 1
- 108060008539 Transglutaminase Proteins 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 206010046865 Vaccinia virus infection Diseases 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 description 1
- LPQOADBMXVRBNX-UHFFFAOYSA-N ac1ldcw0 Chemical compound Cl.C1CN(C)CCN1C1=C(F)C=C2C(=O)C(C(O)=O)=CN3CCSC1=C32 LPQOADBMXVRBNX-UHFFFAOYSA-N 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 125000002252 acyl group Chemical group 0.000 description 1
- 229960001570 ademetionine Drugs 0.000 description 1
- 238000000137 annealing Methods 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 230000009141 biological interaction Effects 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 108700007873 bovine collectin-43 Proteins 0.000 description 1
- 229960001948 caffeine Drugs 0.000 description 1
- VJEONQKOZGKCAK-UHFFFAOYSA-N caffeine Natural products CN1C(=O)N(C)C(=O)C2=C1C=CN2C VJEONQKOZGKCAK-UHFFFAOYSA-N 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 239000001506 calcium phosphate Substances 0.000 description 1
- 229910000389 calcium phosphate Inorganic materials 0.000 description 1
- 235000011010 calcium phosphates Nutrition 0.000 description 1
- 150000001718 carbodiimides Chemical group 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 150000007942 carboxylates Chemical group 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 238000010382 chemical cross-linking Methods 0.000 description 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
- 229960005091 chloramphenicol Drugs 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 238000002983 circular dichroism Methods 0.000 description 1
- 239000007979 citrate buffer Substances 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 229910052802 copper Inorganic materials 0.000 description 1
- 239000010949 copper Substances 0.000 description 1
- 238000012937 correction Methods 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000001212 derivatisation Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 238000009792 diffusion process Methods 0.000 description 1
- 238000006471 dimerization reaction Methods 0.000 description 1
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 150000002019 disulfides Chemical class 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 238000001493 electron microscopy Methods 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 150000002148 esters Chemical class 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 102000013373 fibrillar collagen Human genes 0.000 description 1
- 108060002894 fibrillar collagen Proteins 0.000 description 1
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 102000034238 globular proteins Human genes 0.000 description 1
- 108091005896 globular proteins Proteins 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- 229940015043 glyoxal Drugs 0.000 description 1
- 150000003278 haem Chemical group 0.000 description 1
- 239000000185 hemagglutinin Substances 0.000 description 1
- 125000005842 heteroatom Chemical group 0.000 description 1
- 125000004051 hexyl group Chemical group [H]C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])* 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 230000033444 hydroxylation Effects 0.000 description 1
- 238000005805 hydroxylation reaction Methods 0.000 description 1
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Substances C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 1
- 230000003100 immobilizing effect Effects 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 238000000099 in vitro assay Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 210000003000 inclusion body Anatomy 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 239000000411 inducer Substances 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 206010022000 influenza Diseases 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000001948 isotopic labelling Methods 0.000 description 1
- 210000003292 kidney cell Anatomy 0.000 description 1
- 229910021644 lanthanide ion Inorganic materials 0.000 description 1
- 150000002605 large molecules Chemical class 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- 238000004989 laser desorption mass spectroscopy Methods 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 239000012160 loading buffer Substances 0.000 description 1
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 230000009456 molecular mechanism Effects 0.000 description 1
- 229960005181 morphine Drugs 0.000 description 1
- 238000010995 multi-dimensional NMR spectroscopy Methods 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 210000004897 n-terminal region Anatomy 0.000 description 1
- 238000000655 nuclear magnetic resonance spectrum Methods 0.000 description 1
- 230000000269 nucleophilic effect Effects 0.000 description 1
- 210000004940 nucleus Anatomy 0.000 description 1
- 125000000962 organic group Chemical group 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 108010091748 peptide A Proteins 0.000 description 1
- NMHMNPHRMNGLLB-UHFFFAOYSA-N phloretic acid Chemical compound OC(=O)CCC1=CC=C(O)C=C1 NMHMNPHRMNGLLB-UHFFFAOYSA-N 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 230000008488 polyadenylation Effects 0.000 description 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
- QLNJFJADRCOGBJ-UHFFFAOYSA-N propionamide Chemical compound CCC(N)=O QLNJFJADRCOGBJ-UHFFFAOYSA-N 0.000 description 1
- 229940080818 propionamide Drugs 0.000 description 1
- 230000004853 protein function Effects 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 239000010453 quartz Substances 0.000 description 1
- 239000000376 reactant Substances 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000006479 redox reaction Methods 0.000 description 1
- 238000007634 remodeling Methods 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000004366 reverse phase liquid chromatography Methods 0.000 description 1
- 239000000523 sample Substances 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N silicon dioxide Inorganic materials O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- 239000001509 sodium citrate Substances 0.000 description 1
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 230000010512 thermal transition Effects 0.000 description 1
- 125000003396 thiol group Chemical group [H]S* 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 238000006276 transfer reaction Methods 0.000 description 1
- 102000003601 transglutaminase Human genes 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
- 238000009966 trimming Methods 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 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
- 241001430294 unidentified retrovirus Species 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 208000007089 vaccinia Diseases 0.000 description 1
- 125000002987 valine group Chemical group [H]N([H])C([H])(C(*)=O)C([H])(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 239000003643 water by type Substances 0.000 description 1
- 229910052725 zinc Inorganic materials 0.000 description 1
- 239000011701 zinc Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K19/00—Hybrid peptides, i.e. peptides covalently bound to nucleic acids, or non-covalently bound protein-protein complexes
-
- 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
- C07K14/4726—Lectins
-
- 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
- C07K14/785—Alveolar surfactant peptides; Pulmonary surfactant peptides
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- Zoology (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Pulmonology (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Materials For Medical Uses (AREA)
Abstract
Description
Claims (1)
- 【特許請求の範囲】 1.コレクチンのネック領域であるアミノ酸の一次配列、あるいはそのアミノ 酸配列変異体又はその誘導体を包含し、三量体を生成可能な非天然ポリペプチド 。 2.アミノ酸の一次配列がコレクチンSP−Dのネック領域、あるいはその変 異体又は誘導体である請求項1記載のポリペプチド。 3.一次アミノ酸配列が図1に示されるネック領域アミノ酸配列である請求項 2記載のポリペプチド。 4.一次アミノ酸配列がコレクチン−43又はコングルチニンのネック領域、 あるいはこれらの一方の変異体又は誘導体である請求項1記載のポリペプチド。 5.コレクチンSP−Dのネック領域と同一又は同様のアミノ酸パターン及び /又は疎水性プロフィールを有するアミノ酸の一次配列を包含し、三量体を生成 し得るポリペプチド。 6.アミノ酸の上記一次配列が1つ又はそれ以上の異種アミノ酸と融合される 請求項1〜5のいずれかに記載のポリペプチド。 7.異種アミノ酸がタンパク質ドメインを包含する請求項6記載のポリペプチ ド。 8.異種アミノ酸がイムノグロブリン由来の配列を包含する請求項6又は7記 載のポリペプチド。 9.一次アミノ酸配列が異種アミノ酸と連結されるか又はペプチドリンカーを 介してアミノ酸と連結される請求項6、7又は8のいずれかに記載のポリペプチ ド。 10.単数又は複数の異種アミノ酸が化学的部分の付着のために誘導可能であ るアミノ酸を包含する請求項6〜9のいずれかに記載のポリペプチド。 11.非ペプチド部分と連結される前記請求項のいずれかに記載のポリペプチ ド。 12.アミノ酸の一次配列に対する上記異種アミノ酸(単数又は複数)N末端 及びアミノ酸の一次配列に対する1つ又はそれ以上のアミノ酸C末端、あるいは アミノ酸の一次配列に対する上記異種アミノ酸(単数又は複数)C末端及びアミ ノ酸の一次配列に対する1つ又はそれ以上のアミノ酸N末端を包含する請求項6 〜10のいずれかに記載のポリペプチド。 13.コレクチンC型レクチンドメインを包含する請求項1〜12のいずれか に記載のポリペプチド。 14.前記請求項のいずれかに記載のポリペプチドをコードするヌクレオチド の配列を包含する核酸。 15.ベクターである請求項14記載の核酸。 16.請求項14又は15記載の核酸を含有する宿主細胞。 17.コード配列がポリペプチドの発現のための調節配列に操作可能的に連結 される請求項14又は15記載の核酸。 18.請求項17記載の核酸を含有する宿主細胞。 19.コード化ポリペプチドの請求項14記載の核酸からの発現を含む方法。 20.上記ポリペプチドの発現のための条件下で請求項18記載の宿主細胞を 培養することから成る方法。 21.請求項19又は20に記載の方法によるその発現後にポリペプチドを包 含する三量体を生成することから成る方法。 22.上記三量体がホモ三量体である請求項21記載の方法。 23.上記三量体がヘテロ三量体である請求項21記載の方法。 24.請求項19又は20記載の方法によるその発現後にポリペプチドを単離 することを含む方法。 25.請求項24記載の方法によるその単離後にポリペプチドを包含する三量 体を生成することから成る方法。 26.上記三量体がホモ三量体である請求項25記載の方法。 27.上記三量体がヘテロ三量体である請求項25記載の方法。 28.請求項1〜13のいずれかに記載のポリペプチドを包含する三量体を生 成することから成る方法。 29.請求項1〜13のいずれかに記載のポリペプチドを包含する三量体。 30.ホモ三量体である請求項29記載の三量体。 31.ヘテロ三量体である請求項29記載の三量体。 32.非天然ポリペプチドを提供することから成るするコラーゲン三重らせん の生成方法であって、各ポリペプチドがコレクチンのネック領域、あるいはその アミノ酸配列変異体又はその誘導体であるアミノ酸の一次配列に対する一連のコ ラーゲントリプレットN末端を包含し、三量体を生成可能であって、上記ポリペ プチドにさりたを生成させるか又は生成可能にさせる方法。 33.アミノ酸の一次配列がコレクチンSP−Dのネック領域、あるいはその 変異体又は誘導体である請求項32記載の方法。 34.一次アミノ酸配列が図1に示されるネック領域アミノ酸配列である請求 項33記載の方法。 35.一次アミノ酸配列がコレクチン−43又はコングルチニンのネック領域 、あるいはこれらの一方の変異体又は誘導体である請求項32記載の方法。 36.アミノ酸の上記一次配列がポリペプチドのC末端にあるか、あるいは上 記ポリペプチドが上記一次配列に対する1つ又はそれ以上の異種アミノ酸C末端 を包含する請求項32〜35記載の方法。 37.非天然ポリペプチドを提供することから成るコラーゲン三重らせんの生 成方法であって、各ポリペプチドがコレクチンSP−Dのネック領域と同一又は 同様のアミノ酸パターン及び/又は疎水性プロフィールを有するアミノ酸の一次 配列に対する一連のコラーゲントリプレットN末端を包含し、三量体を生成し得 るポリペプチドであって、上記ポリペプチドに三量体を生成させるか又は生成可 能にする方法。 38.上記ポリペプチドがそのコード化核酸からの発現により提供される請求 項32〜37のいずれかに記載の方法。 39.上記三量体が三量体化後に単離される請求項38記載の方法。
Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
GB9409768.0 | 1994-05-16 | ||
GB9409768A GB9409768D0 (en) | 1994-05-16 | 1994-05-16 | Trimerising polypeptides |
PCT/GB1995/001104 WO1995031540A1 (en) | 1994-05-16 | 1995-05-16 | Trimerising polypeptides, their manufacture and use |
Related Child Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2005230930A Division JP3836865B2 (ja) | 1994-05-16 | 2005-08-09 | 三量体化ポリペプチド、その製造及び使用 |
Publications (1)
Publication Number | Publication Date |
---|---|
JPH10500298A true JPH10500298A (ja) | 1998-01-13 |
Family
ID=10755201
Family Applications (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP7529462A Withdrawn JPH10500298A (ja) | 1994-05-16 | 1995-05-16 | 三量体化ポリペプチド、その製造及び使用 |
JP2005230930A Expired - Fee Related JP3836865B2 (ja) | 1994-05-16 | 2005-08-09 | 三量体化ポリペプチド、その製造及び使用 |
Family Applications After (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2005230930A Expired - Fee Related JP3836865B2 (ja) | 1994-05-16 | 2005-08-09 | 三量体化ポリペプチド、その製造及び使用 |
Country Status (12)
Country | Link |
---|---|
US (1) | US6190886B1 (ja) |
EP (1) | EP0757720B1 (ja) |
JP (2) | JPH10500298A (ja) |
AT (1) | ATE227341T1 (ja) |
AU (1) | AU2451995A (ja) |
CA (1) | CA2190264A1 (ja) |
DE (1) | DE69528761T2 (ja) |
DK (1) | DK0757720T3 (ja) |
ES (1) | ES2186718T3 (ja) |
GB (1) | GB9409768D0 (ja) |
PT (1) | PT757720E (ja) |
WO (1) | WO1995031540A1 (ja) |
Cited By (8)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2005078085A1 (ja) * | 2004-02-16 | 2005-08-25 | Techno Network Shikoku Co., Ltd. | コラーゲン様構造を有するポリペプチド |
WO2010074081A1 (ja) * | 2008-12-22 | 2010-07-01 | 国立大学法人北海道大学 | 三重螺旋構造を有するタンパク質、およびその製造方法 |
JP2010532978A (ja) * | 2007-07-10 | 2010-10-21 | アポゲニクス ゲゼルシャフト ミット ベシュレンクテル ハフツング | Tnfスーパーファミリーコレクチン融合タンパク質 |
JP2011217760A (ja) * | 2005-12-15 | 2011-11-04 | Ind Technol Res Inst | 組み換え三重足場ベースポリペプチド |
JP2012514616A (ja) * | 2009-01-09 | 2012-06-28 | アポゲニクス ゲゼルシャフト ミット ベシュレンクテル ハフツング | 三量体形成融合タンパク質 |
JP2014218510A (ja) * | 2014-08-11 | 2014-11-20 | アポゲニクスゲゼルシャフト ミット ベシュレンクテルハフツングApogenix GmbH | 三量体形成融合タンパク質 |
JP2016210791A (ja) * | 2016-08-03 | 2016-12-15 | アポゲニクス アーゲー | 三量体形成融合タンパク質 |
US10183986B2 (en) | 2005-12-15 | 2019-01-22 | Industrial Technology Research Institute | Trimeric collagen scaffold antibodies |
Families Citing this family (32)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
AUPO591797A0 (en) | 1997-03-27 | 1997-04-24 | Commonwealth Scientific And Industrial Research Organisation | High avidity polyvalent and polyspecific reagents |
EP0938571B8 (en) * | 1996-10-28 | 2008-07-02 | University of Lausanne | Method for the oligomerisation of peptides |
EP0950098B1 (en) * | 1996-10-29 | 2008-09-03 | Commonwealth Scientific And Industrial Research Organisation | Stable expression of triple helical proteins |
EP1012280B1 (en) | 1997-06-11 | 2004-11-10 | Borean Pharma A/S | Trimerising module |
US7914814B2 (en) * | 1997-09-17 | 2011-03-29 | Strategic Science & Technologies, Llc | Topical delivery of arginine of cause beneficial effects |
ATE293994T1 (de) * | 1997-12-01 | 2005-05-15 | Fang Fang | Multivalente rekombinante antikörper zur behandlung von hrv infektionen |
US20030035798A1 (en) * | 2000-08-16 | 2003-02-20 | Fang Fang | Humanized antibodies |
US7300774B1 (en) * | 1999-12-09 | 2007-11-27 | The Regents Of The University Of California | Multimeric fusion proteins of the TNF superfamily ligands |
CA2372198A1 (en) * | 1999-05-14 | 2000-11-23 | Medical Research Council | Protein scaffold and its use to multimerise monomeric polypeptides |
CN1268641C (zh) | 2000-11-10 | 2006-08-09 | 普罗蒂奥制药公司 | 载脂蛋白类似物 |
WO2002070725A1 (en) * | 2001-03-06 | 2002-09-12 | Mustapha Abdelouahed | Carrier chimeric proteins, targeted carrier chimeric proteins and preparation thereof |
JP2005522192A (ja) | 2001-07-19 | 2005-07-28 | パーラン セラピューティクス, インコーポレイテッド | マルチマータンパク質およびマルチマータンパク質を作製および使用する方法 |
DK1440083T3 (da) | 2001-10-25 | 2013-03-25 | Medical Res Council | Molekyler |
EP1463755B1 (en) * | 2001-12-21 | 2008-06-25 | Immunex Corporation | Recombinant polypeptides |
CN101899106A (zh) | 2002-10-29 | 2010-12-01 | 阿纳福公司 | 三聚细胞因子的三聚结合蛋白 |
WO2005037852A2 (en) * | 2003-08-22 | 2005-04-28 | Barnes-Jewish Hospital | Trimerizing polypeptides and their uses |
US7268116B2 (en) * | 2003-10-02 | 2007-09-11 | Genhunter Corp. | Methods and compositions for producing secreted trimeric receptor analogs and biologically active fusion proteins |
EP1824878A1 (en) | 2004-11-22 | 2007-08-29 | Borean Pharma A/S | Tnf antagonists |
ES2415890T3 (es) * | 2005-09-09 | 2013-07-29 | Zymogenetics, Inc. | Procedimiento de preparación de proteínas triméricas |
EP2674440B1 (en) | 2005-12-16 | 2019-07-03 | IBC Pharmaceuticals, Inc. | Multivalent immunoglobulin-based bioactive assemblies |
CN103159857B (zh) * | 2007-05-21 | 2014-11-05 | 财团法人工业技术研究院 | 以重组的三股螺旋支架为基础的复合物 |
KR20100087344A (ko) | 2007-10-29 | 2010-08-04 | 버지니아 테크 인터렉추얼 프라퍼티스, 인크. | 돼지 DC-SIGN, ICAM-3 및 LSECtin 및 이의 용도 |
CN102089432A (zh) | 2008-07-08 | 2011-06-08 | 麦迪卡格公司 | 可溶性重组流感抗原 |
CA2739663A1 (en) | 2008-10-10 | 2010-05-15 | Anaphore, Inc. | Polypeptides that bind trail-r1 and trail-r2 |
WO2010122181A1 (es) * | 2009-04-20 | 2010-10-28 | Universidad Autónoma de Madrid | Proteínas oligoméricas y sus aplicaciones |
US20110086806A1 (en) * | 2009-10-09 | 2011-04-14 | Anaphore, Inc. | Polypeptides that Bind IL-23R |
JP2013507124A (ja) * | 2009-10-09 | 2013-03-04 | アナフォア インコーポレイテッド | Il−23rを結合するポリペプチド |
WO2014145355A1 (en) | 2013-03-15 | 2014-09-18 | Stone Geoffrey W | Composition comprised of antigen linked to a tnf superfamily ligand |
KR20180070709A (ko) | 2015-11-13 | 2018-06-26 | 스파이버 테크놀러지스 에이비 | 전하 역전 n-말단 거미줄 단백질 도메인 및 이의 용도 |
GB201522610D0 (en) * | 2015-12-22 | 2016-02-03 | Univ Southampton | Protein |
US11377490B2 (en) | 2017-05-31 | 2022-07-05 | Sichuan Clover Biopharmaceuticals, Inc | Method for treating cancer using disulfide-linked trimeric 4-1BBL |
WO2021249116A1 (en) | 2020-06-10 | 2021-12-16 | Sichuan Clover Biopharmaceuticals, Inc. | Coronavirus vaccine compositions, methods, and uses thereof |
Family Cites Families (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5716805A (en) * | 1991-10-25 | 1998-02-10 | Immunex Corporation | Methods of preparing soluble, oligomeric proteins |
-
1994
- 1994-05-16 GB GB9409768A patent/GB9409768D0/en active Pending
-
1995
- 1995-05-16 WO PCT/GB1995/001104 patent/WO1995031540A1/en active IP Right Grant
- 1995-05-16 US US08/737,629 patent/US6190886B1/en not_active Expired - Lifetime
- 1995-05-16 CA CA002190264A patent/CA2190264A1/en not_active Abandoned
- 1995-05-16 DK DK95918689T patent/DK0757720T3/da active
- 1995-05-16 EP EP95918689A patent/EP0757720B1/en not_active Expired - Lifetime
- 1995-05-16 ES ES95918689T patent/ES2186718T3/es not_active Expired - Lifetime
- 1995-05-16 AT AT95918689T patent/ATE227341T1/de not_active IP Right Cessation
- 1995-05-16 JP JP7529462A patent/JPH10500298A/ja not_active Withdrawn
- 1995-05-16 PT PT95918689T patent/PT757720E/pt unknown
- 1995-05-16 DE DE69528761T patent/DE69528761T2/de not_active Expired - Lifetime
- 1995-05-16 AU AU24519/95A patent/AU2451995A/en not_active Abandoned
-
2005
- 2005-08-09 JP JP2005230930A patent/JP3836865B2/ja not_active Expired - Fee Related
Cited By (17)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US8030448B2 (en) | 2004-02-16 | 2011-10-04 | Techno Network Shikoku Co., Ltd. | Polypeptide having collagen-like structure |
WO2005078085A1 (ja) * | 2004-02-16 | 2005-08-25 | Techno Network Shikoku Co., Ltd. | コラーゲン様構造を有するポリペプチド |
JP2011217760A (ja) * | 2005-12-15 | 2011-11-04 | Ind Technol Res Inst | 組み換え三重足場ベースポリペプチド |
US10183986B2 (en) | 2005-12-15 | 2019-01-22 | Industrial Technology Research Institute | Trimeric collagen scaffold antibodies |
JP2015057442A (ja) * | 2007-07-10 | 2015-03-26 | アポゲニクス ゲゼルシャフト ミット ベシュレンクテル ハフツングApogenix GmbH | Tnfスーパーファミリーコレクチン融合タンパク質 |
US10000550B2 (en) | 2007-07-10 | 2018-06-19 | Apogenix Ag | GITRL-collectin fusion proteins and encoding nucleic acids |
JP2010532978A (ja) * | 2007-07-10 | 2010-10-21 | アポゲニクス ゲゼルシャフト ミット ベシュレンクテル ハフツング | Tnfスーパーファミリーコレクチン融合タンパク質 |
US9527897B2 (en) | 2007-07-10 | 2016-12-27 | Apogenix Ag | CD40L collectin fusion proteins and encoding nucleic acid molecules |
US10519217B2 (en) | 2007-07-10 | 2019-12-31 | Apogenix Ag | CD27L collectin fusion proteins and encoding nucleic acids |
US9212211B2 (en) | 2007-07-10 | 2015-12-15 | Apogenix Gmbh | Trail collectin fusion proteins |
JP5645187B2 (ja) * | 2008-12-22 | 2014-12-24 | 国立大学法人北海道大学 | 三重螺旋構造を有するタンパク質、およびその製造方法 |
US8470555B2 (en) | 2008-12-22 | 2013-06-25 | National University Corporation Hokkaido University | Protein substance having triple helix structure and manufacturing method therefor |
KR20110119650A (ko) * | 2008-12-22 | 2011-11-02 | 국립대학법인 홋가이도 다이가쿠 | 3중 나선구조를 갖는 단백질 및 그의 제조방법 |
WO2010074081A1 (ja) * | 2008-12-22 | 2010-07-01 | 国立大学法人北海道大学 | 三重螺旋構造を有するタンパク質、およびその製造方法 |
JP2012514616A (ja) * | 2009-01-09 | 2012-06-28 | アポゲニクス ゲゼルシャフト ミット ベシュレンクテル ハフツング | 三量体形成融合タンパク質 |
JP2014218510A (ja) * | 2014-08-11 | 2014-11-20 | アポゲニクスゲゼルシャフト ミット ベシュレンクテルハフツングApogenix GmbH | 三量体形成融合タンパク質 |
JP2016210791A (ja) * | 2016-08-03 | 2016-12-15 | アポゲニクス アーゲー | 三量体形成融合タンパク質 |
Also Published As
Publication number | Publication date |
---|---|
GB9409768D0 (en) | 1994-07-06 |
DE69528761D1 (de) | 2002-12-12 |
DE69528761T2 (de) | 2003-07-17 |
DK0757720T3 (da) | 2003-03-17 |
AU2451995A (en) | 1995-12-05 |
JP2005328851A (ja) | 2005-12-02 |
EP0757720A1 (en) | 1997-02-12 |
CA2190264A1 (en) | 1995-11-23 |
PT757720E (pt) | 2003-03-31 |
ES2186718T3 (es) | 2003-05-16 |
JP3836865B2 (ja) | 2006-10-25 |
WO1995031540A1 (en) | 1995-11-23 |
EP0757720B1 (en) | 2002-11-06 |
ATE227341T1 (de) | 2002-11-15 |
US6190886B1 (en) | 2001-02-20 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
JP3836865B2 (ja) | 三量体化ポリペプチド、その製造及び使用 | |
WO1995031540A9 (en) | Trimerising polypeptides, their manufacture and use | |
US10247727B2 (en) | Peptide tag system that spontaneously form an irreversible link to protein partners via isopeptide bonds | |
CN110582566B (zh) | 肽连接酶及其用途 | |
CA1339208C (en) | Fusion proteins containing a hinge region for enhanced cleavage | |
WO2009016043A2 (en) | New albumin binding compositions, methods and uses | |
AU2005216126A1 (en) | Binding peptidomimetics and uses of the same | |
JPH06510434A (ja) | 組換えコア・ストレプトアビジン | |
JP2003501064A (ja) | シャペロンポリペプチドのフラグメントを含む融合タンパク質 | |
Crabb et al. | Structural and functional characterization of recombinant human cellular retinaldehyde‐binding protein | |
JP2003527561A (ja) | 蛋白の部位特異的標識化方法およびそのための使用 | |
US5888775A (en) | Peptide synthesis and purification by fusion to penI protein or precipitation effective portion thereof | |
US20090023185A1 (en) | Avidin Mutants | |
King et al. | Isolation, expression, and characterization of fully functional nontoxic BiP/GRP78 mutants | |
US20130157257A1 (en) | Compositions Comprising the NC2 Domain of Collagen IX and Methods of Using Same | |
JP2000247999A (ja) | 固定化蛋白質の製造法 | |
Xu et al. | Cloning, expression, and purification of a highly immunogenic recombinant gonadotropin-releasing hormone (GnRH) chimeric peptide | |
KR20190114550A (ko) | 단백질-단백질 결합체를 형성 매개 펩타이드 및 이를 이용한 단백질-단백질 결합체 형성 방법 | |
Jha et al. | Overexpression and rapid purification of rabbit fast skeletal troponin I from Escherichia coli: effect of different promoters, host strains, and culture conditions | |
JPH05317050A (ja) | Pzp−4遺伝子及び避妊ワクチン | |
KR101598581B1 (ko) | 광활성 메티오닌 모사체 도입 단백질 g 변이체 | |
JPH07126297A (ja) | カルモジュリン融合蛋白質 | |
JP2813370B2 (ja) | ヒトインターロイキン5の生産方法 | |
JP2000044597A (ja) | 組み換え梅毒47kDa抗原の製造方法 | |
JPH04234988A (ja) | ヒトプロラクチン−プロテインa融合蛋白発現遺伝子 |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20040914 |
|
A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20041210 |
|
A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20050131 |
|
A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20050314 |
|
A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20050426 |
|
A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20050725 |
|
A761 | Written withdrawal of application |
Free format text: JAPANESE INTERMEDIATE CODE: A761 Effective date: 20050823 |