JP7505980B2 - Ｃ３ｂ結合ポリペプチド - Google Patents
Ｃ３ｂ結合ポリペプチド Download PDFInfo
- Publication number
- JP7505980B2 JP7505980B2 JP2020538949A JP2020538949A JP7505980B2 JP 7505980 B2 JP7505980 B2 JP 7505980B2 JP 2020538949 A JP2020538949 A JP 2020538949A JP 2020538949 A JP2020538949 A JP 2020538949A JP 7505980 B2 JP7505980 B2 JP 7505980B2
- Authority
- JP
- Japan
- Prior art keywords
- polypeptide
- seq
- amino acid
- cell
- pharmaceutical composition
- 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.)
- Active
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims description 585
- 102000004196 processed proteins & peptides Human genes 0.000 title claims description 574
- 229920001184 polypeptide Polymers 0.000 title claims description 571
- 101000901154 Homo sapiens Complement C3 Proteins 0.000 title description 291
- 102100022133 Complement C3 Human genes 0.000 title description 290
- 150000007523 nucleic acids Chemical class 0.000 claims description 145
- 239000013598 vector Substances 0.000 claims description 144
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 139
- 108020004707 nucleic acids Proteins 0.000 claims description 134
- 102000039446 nucleic acids Human genes 0.000 claims description 134
- 208000002780 macular degeneration Diseases 0.000 claims description 111
- 206010064930 age-related macular degeneration Diseases 0.000 claims description 106
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 104
- 201000010099 disease Diseases 0.000 claims description 101
- 238000000034 method Methods 0.000 claims description 64
- 239000008194 pharmaceutical composition Substances 0.000 claims description 61
- 230000000694 effects Effects 0.000 claims description 55
- 238000011282 treatment Methods 0.000 claims description 42
- 238000006243 chemical reaction Methods 0.000 claims description 36
- 238000003776 cleavage reaction Methods 0.000 claims description 34
- 230000037361 pathway Effects 0.000 claims description 34
- 230000007017 scission Effects 0.000 claims description 34
- 239000003814 drug Substances 0.000 claims description 32
- 230000003248 secreting effect Effects 0.000 claims description 31
- 238000004519 manufacturing process Methods 0.000 claims description 30
- 230000024203 complement activation Effects 0.000 claims description 29
- 239000000203 mixture Substances 0.000 claims description 28
- 208000033530 early-onset macular degeneration Diseases 0.000 claims description 18
- 208000022873 Ocular disease Diseases 0.000 claims description 17
- 208000005590 Choroidal Neovascularization Diseases 0.000 claims description 15
- 206010060823 Choroidal neovascularisation Diseases 0.000 claims description 15
- 230000002265 prevention Effects 0.000 claims description 10
- 208000008069 Geographic Atrophy Diseases 0.000 claims description 9
- 125000000539 amino acid group Chemical group 0.000 claims description 9
- 206010012689 Diabetic retinopathy Diseases 0.000 claims description 7
- 208000010412 Glaucoma Diseases 0.000 claims description 7
- 201000004982 autoimmune uveitis Diseases 0.000 claims description 7
- 239000013603 viral vector Substances 0.000 claims description 7
- 230000003612 virological effect Effects 0.000 claims description 6
- 239000000790 retinal pigment Substances 0.000 claims description 5
- 241000702423 Adeno-associated virus - 2 Species 0.000 claims description 4
- 230000001177 retroviral effect Effects 0.000 claims description 4
- 241000175212 Herpesvirales Species 0.000 claims description 2
- 206010046865 Vaccinia virus infection Diseases 0.000 claims description 2
- 208000007089 vaccinia Diseases 0.000 claims description 2
- 210000004027 cell Anatomy 0.000 description 281
- 235000001014 amino acid Nutrition 0.000 description 129
- 108090000044 Complement Factor I Proteins 0.000 description 111
- 102100035431 Complement factor I Human genes 0.000 description 111
- 150000001413 amino acids Chemical class 0.000 description 110
- 210000001775 bruch membrane Anatomy 0.000 description 97
- 210000003583 retinal pigment epithelium Anatomy 0.000 description 66
- 230000000295 complement effect Effects 0.000 description 62
- 108090000623 proteins and genes Proteins 0.000 description 60
- 102000004169 proteins and genes Human genes 0.000 description 56
- 235000018102 proteins Nutrition 0.000 description 52
- 239000012634 fragment Substances 0.000 description 45
- 230000014509 gene expression Effects 0.000 description 43
- 239000000047 product Substances 0.000 description 35
- 101710184994 Complement control protein Proteins 0.000 description 32
- 102100035432 Complement factor H Human genes 0.000 description 26
- 238000009792 diffusion process Methods 0.000 description 25
- 230000015556 catabolic process Effects 0.000 description 23
- 239000002609 medium Substances 0.000 description 22
- 238000003556 assay Methods 0.000 description 21
- 238000006731 degradation reaction Methods 0.000 description 21
- 230000001404 mediated effect Effects 0.000 description 21
- 102000016574 Complement C3-C5 Convertases Human genes 0.000 description 20
- 108010067641 Complement C3-C5 Convertases Proteins 0.000 description 20
- 102000001708 Protein Isoforms Human genes 0.000 description 19
- 108010029485 Protein Isoforms Proteins 0.000 description 19
- 108010052926 complement C3d,g Proteins 0.000 description 19
- 239000000523 sample Substances 0.000 description 19
- 230000009467 reduction Effects 0.000 description 18
- 108010053085 Complement Factor H Proteins 0.000 description 17
- 210000001525 retina Anatomy 0.000 description 16
- 206010025421 Macule Diseases 0.000 description 15
- 210000003161 choroid Anatomy 0.000 description 14
- 108010047295 complement receptors Proteins 0.000 description 14
- 102000006834 complement receptors Human genes 0.000 description 14
- 210000001519 tissue Anatomy 0.000 description 14
- 108010076504 Protein Sorting Signals Proteins 0.000 description 13
- 230000001965 increasing effect Effects 0.000 description 13
- 101000737574 Homo sapiens Complement factor H Proteins 0.000 description 12
- 238000004458 analytical method Methods 0.000 description 12
- 238000002474 experimental method Methods 0.000 description 11
- 230000037417 hyperactivation Effects 0.000 description 11
- 230000003993 interaction Effects 0.000 description 11
- 230000006337 proteolytic cleavage Effects 0.000 description 11
- 241000894007 species Species 0.000 description 11
- 238000006467 substitution reaction Methods 0.000 description 11
- 241000283984 Rodentia Species 0.000 description 10
- 210000004204 blood vessel Anatomy 0.000 description 10
- 238000002347 injection Methods 0.000 description 10
- 239000007924 injection Substances 0.000 description 10
- 229940124597 therapeutic agent Drugs 0.000 description 10
- 201000004569 Blindness Diseases 0.000 description 9
- 238000012575 bio-layer interferometry Methods 0.000 description 9
- 239000003795 chemical substances by application Substances 0.000 description 9
- 230000006870 function Effects 0.000 description 9
- BTCSSZJGUNDROE-UHFFFAOYSA-N gamma-aminobutyric acid Chemical compound NCCCC(O)=O BTCSSZJGUNDROE-UHFFFAOYSA-N 0.000 description 9
- 230000002068 genetic effect Effects 0.000 description 9
- 239000010410 layer Substances 0.000 description 9
- 229920002451 polyvinyl alcohol Polymers 0.000 description 9
- 238000009825 accumulation Methods 0.000 description 8
- 239000002671 adjuvant Substances 0.000 description 8
- 239000003085 diluting agent Substances 0.000 description 8
- 210000003527 eukaryotic cell Anatomy 0.000 description 8
- 239000000546 pharmaceutical excipient Substances 0.000 description 8
- 210000000608 photoreceptor cell Anatomy 0.000 description 8
- 230000002207 retinal effect Effects 0.000 description 8
- 230000001225 therapeutic effect Effects 0.000 description 8
- 239000013607 AAV vector Substances 0.000 description 7
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 7
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 7
- 101000727061 Homo sapiens Complement receptor type 1 Proteins 0.000 description 7
- 108091028043 Nucleic acid sequence Proteins 0.000 description 7
- 230000015572 biosynthetic process Effects 0.000 description 7
- 230000006378 damage Effects 0.000 description 7
- 230000003247 decreasing effect Effects 0.000 description 7
- 238000001514 detection method Methods 0.000 description 7
- 239000003937 drug carrier Substances 0.000 description 7
- 230000004064 dysfunction Effects 0.000 description 7
- 210000005260 human cell Anatomy 0.000 description 7
- 238000000338 in vitro Methods 0.000 description 7
- 238000001727 in vivo Methods 0.000 description 7
- 210000004379 membrane Anatomy 0.000 description 7
- 239000012528 membrane Substances 0.000 description 7
- 239000013642 negative control Substances 0.000 description 7
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 description 7
- 238000002560 therapeutic procedure Methods 0.000 description 7
- 108091035707 Consensus sequence Proteins 0.000 description 6
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 6
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 6
- 241001465754 Metazoa Species 0.000 description 6
- 108700022034 Opsonin Proteins Proteins 0.000 description 6
- 241000700159 Rattus Species 0.000 description 6
- 238000012258 culturing Methods 0.000 description 6
- 238000011161 development Methods 0.000 description 6
- 230000018109 developmental process Effects 0.000 description 6
- 229940079593 drug Drugs 0.000 description 6
- 210000002744 extracellular matrix Anatomy 0.000 description 6
- 102000046508 human CR1 Human genes 0.000 description 6
- 210000000987 immune system Anatomy 0.000 description 6
- 238000011065 in-situ storage Methods 0.000 description 6
- 235000015097 nutrients Nutrition 0.000 description 6
- 238000012545 processing Methods 0.000 description 6
- 230000001105 regulatory effect Effects 0.000 description 6
- FVAUCKIRQBBSSJ-UHFFFAOYSA-M sodium iodide Chemical compound [Na+].[I-] FVAUCKIRQBBSSJ-UHFFFAOYSA-M 0.000 description 6
- 238000001890 transfection Methods 0.000 description 6
- 230000004393 visual impairment Effects 0.000 description 6
- 241000894006 Bacteria Species 0.000 description 5
- 102220592822 Complement factor H_Y402H_mutation Human genes 0.000 description 5
- 108020004414 DNA Proteins 0.000 description 5
- 230000008901 benefit Effects 0.000 description 5
- 230000001413 cellular effect Effects 0.000 description 5
- 239000012091 fetal bovine serum Substances 0.000 description 5
- 239000000499 gel Substances 0.000 description 5
- 230000013595 glycosylation Effects 0.000 description 5
- 238000006206 glycosylation reaction Methods 0.000 description 5
- 238000011534 incubation Methods 0.000 description 5
- 238000001802 infusion Methods 0.000 description 5
- 230000004048 modification Effects 0.000 description 5
- 238000012986 modification Methods 0.000 description 5
- 230000007170 pathology Effects 0.000 description 5
- 239000013612 plasmid Substances 0.000 description 5
- 230000028327 secretion Effects 0.000 description 5
- 238000010361 transduction Methods 0.000 description 5
- 230000026683 transduction Effects 0.000 description 5
- 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 4
- 108010034753 Complement Membrane Attack Complex Proteins 0.000 description 4
- 102000004190 Enzymes Human genes 0.000 description 4
- 108090000790 Enzymes Proteins 0.000 description 4
- 229920002683 Glycosaminoglycan Polymers 0.000 description 4
- 241001529936 Murinae Species 0.000 description 4
- 241000699670 Mus sp. Species 0.000 description 4
- 101710118538 Protease Proteins 0.000 description 4
- 210000004369 blood Anatomy 0.000 description 4
- 239000008280 blood Substances 0.000 description 4
- 230000004154 complement system Effects 0.000 description 4
- 230000034994 death Effects 0.000 description 4
- UQLDLKMNUJERMK-UHFFFAOYSA-L di(octadecanoyloxy)lead Chemical compound [Pb+2].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O UQLDLKMNUJERMK-UHFFFAOYSA-L 0.000 description 4
- 238000010586 diagram Methods 0.000 description 4
- 238000010494 dissociation reaction Methods 0.000 description 4
- 230000005593 dissociations Effects 0.000 description 4
- 239000013604 expression vector Substances 0.000 description 4
- 238000000855 fermentation Methods 0.000 description 4
- 230000004151 fermentation Effects 0.000 description 4
- 238000009472 formulation Methods 0.000 description 4
- 239000001963 growth medium Substances 0.000 description 4
- -1 iC3b Proteins 0.000 description 4
- 238000007913 intrathecal administration Methods 0.000 description 4
- 239000007788 liquid Substances 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 230000035772 mutation Effects 0.000 description 4
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 4
- 238000001262 western blot Methods 0.000 description 4
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 3
- 241000283690 Bos taurus Species 0.000 description 3
- 101150030967 CFH gene Proteins 0.000 description 3
- 229920000045 Dermatan sulfate Polymers 0.000 description 3
- 239000004471 Glycine Substances 0.000 description 3
- 229920002971 Heparan sulfate Polymers 0.000 description 3
- 101000737565 Homo sapiens Complement factor I Proteins 0.000 description 3
- 241000282567 Macaca fascicularis Species 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 230000004988 N-glycosylation Effects 0.000 description 3
- 102000035195 Peptidases Human genes 0.000 description 3
- 108091005804 Peptidases Proteins 0.000 description 3
- 206010057249 Phagocytosis Diseases 0.000 description 3
- 108020005038 Terminator Codon Proteins 0.000 description 3
- 230000004075 alteration Effects 0.000 description 3
- 238000004873 anchoring Methods 0.000 description 3
- 239000000427 antigen Substances 0.000 description 3
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 3
- 230000033228 biological regulation Effects 0.000 description 3
- 239000002299 complementary DNA Substances 0.000 description 3
- AVJBPWGFOQAPRH-FWMKGIEWSA-L dermatan sulfate Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@H](OS([O-])(=O)=O)[C@@H]1O[C@H]1[C@H](O)[C@@H](O)[C@H](O)[C@H](C([O-])=O)O1 AVJBPWGFOQAPRH-FWMKGIEWSA-L 0.000 description 3
- 229940051593 dermatan sulfate Drugs 0.000 description 3
- 208000035475 disorder Diseases 0.000 description 3
- 239000003623 enhancer Substances 0.000 description 3
- 239000003889 eye drop Substances 0.000 description 3
- 229940012356 eye drops Drugs 0.000 description 3
- 239000012530 fluid Substances 0.000 description 3
- 102000057666 human CFI Human genes 0.000 description 3
- 230000002779 inactivation Effects 0.000 description 3
- 230000001939 inductive effect Effects 0.000 description 3
- 230000002401 inhibitory effect Effects 0.000 description 3
- 238000001990 intravenous administration Methods 0.000 description 3
- 210000004962 mammalian cell Anatomy 0.000 description 3
- 238000002156 mixing Methods 0.000 description 3
- 239000002773 nucleotide Substances 0.000 description 3
- 125000003729 nucleotide group Chemical group 0.000 description 3
- 210000000056 organ Anatomy 0.000 description 3
- 229910052760 oxygen Inorganic materials 0.000 description 3
- 239000001301 oxygen Substances 0.000 description 3
- 244000052769 pathogen Species 0.000 description 3
- 230000008782 phagocytosis Effects 0.000 description 3
- 239000013641 positive control Substances 0.000 description 3
- 238000001556 precipitation Methods 0.000 description 3
- 230000008569 process Effects 0.000 description 3
- 210000001236 prokaryotic cell Anatomy 0.000 description 3
- 230000004044 response Effects 0.000 description 3
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 3
- 238000003756 stirring Methods 0.000 description 3
- 239000003104 tissue culture media Substances 0.000 description 3
- 238000012546 transfer Methods 0.000 description 3
- 230000014616 translation Effects 0.000 description 3
- 230000032258 transport Effects 0.000 description 3
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- WLCZTRVUXYALDD-IBGZPJMESA-N 7-[[(2s)-2,6-bis(2-methoxyethoxycarbonylamino)hexanoyl]amino]heptoxy-methylphosphinic acid Chemical compound COCCOC(=O)NCCCC[C@H](NC(=O)OCCOC)C(=O)NCCCCCCCOP(C)(O)=O WLCZTRVUXYALDD-IBGZPJMESA-N 0.000 description 2
- 208000035913 Atypical hemolytic uremic syndrome Diseases 0.000 description 2
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
- 108091033409 CRISPR Proteins 0.000 description 2
- 241000283707 Capra Species 0.000 description 2
- 102000016550 Complement Factor H Human genes 0.000 description 2
- 101710137943 Complement control protein C3 Proteins 0.000 description 2
- 108090000056 Complement factor B Proteins 0.000 description 2
- 241000701022 Cytomegalovirus Species 0.000 description 2
- 241000702421 Dependoparvovirus Species 0.000 description 2
- 238000002965 ELISA Methods 0.000 description 2
- 238000012286 ELISA Assay Methods 0.000 description 2
- 241000283073 Equus caballus Species 0.000 description 2
- 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 2
- 102000005744 Glycoside Hydrolases Human genes 0.000 description 2
- 108010031186 Glycoside Hydrolases Proteins 0.000 description 2
- 101000670189 Homo sapiens Ribulose-phosphate 3-epimerase Proteins 0.000 description 2
- HEFNNWSXXWATRW-UHFFFAOYSA-N Ibuprofen Chemical compound CC(C)CC1=CC=C(C(C)C(O)=O)C=C1 HEFNNWSXXWATRW-UHFFFAOYSA-N 0.000 description 2
- 206010061218 Inflammation Diseases 0.000 description 2
- 241000124008 Mammalia Species 0.000 description 2
- 208000004451 Membranoproliferative Glomerulonephritis Diseases 0.000 description 2
- 241000714177 Murine leukemia virus Species 0.000 description 2
- 208000000733 Paroxysmal Hemoglobinuria Diseases 0.000 description 2
- 102000000447 Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Human genes 0.000 description 2
- 108010055817 Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Proteins 0.000 description 2
- 102100036050 Phosphatidylinositol N-acetylglucosaminyltransferase subunit A Human genes 0.000 description 2
- 229920002873 Polyethylenimine Polymers 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
- 201000007737 Retinal degeneration Diseases 0.000 description 2
- 208000017442 Retinal disease Diseases 0.000 description 2
- 102000012479 Serine Proteases Human genes 0.000 description 2
- 108010022999 Serine Proteases Proteins 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 241000723792 Tobacco etch virus Species 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
- 230000002159 abnormal effect Effects 0.000 description 2
- 108010081667 aflibercept Proteins 0.000 description 2
- 238000013019 agitation Methods 0.000 description 2
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 2
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 2
- 235000011130 ammonium sulphate Nutrition 0.000 description 2
- 230000003321 amplification Effects 0.000 description 2
- 239000012491 analyte Substances 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
- 108091007433 antigens Proteins 0.000 description 2
- 230000004888 barrier function Effects 0.000 description 2
- 229960002685 biotin Drugs 0.000 description 2
- 235000020958 biotin Nutrition 0.000 description 2
- 239000011616 biotin Substances 0.000 description 2
- OWMVSZAMULFTJU-UHFFFAOYSA-N bis-tris Chemical compound OCCN(CCO)C(CO)(CO)CO OWMVSZAMULFTJU-UHFFFAOYSA-N 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 235000018417 cysteine Nutrition 0.000 description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
- 230000022811 deglycosylation Effects 0.000 description 2
- 239000007857 degradation product Substances 0.000 description 2
- 230000000593 degrading effect Effects 0.000 description 2
- 238000002716 delivery method Methods 0.000 description 2
- 230000008021 deposition Effects 0.000 description 2
- 230000006862 enzymatic digestion Effects 0.000 description 2
- 210000000981 epithelium Anatomy 0.000 description 2
- 108020001507 fusion proteins Proteins 0.000 description 2
- 102000037865 fusion proteins Human genes 0.000 description 2
- 238000001415 gene therapy Methods 0.000 description 2
- 238000010353 genetic engineering Methods 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 230000012010 growth Effects 0.000 description 2
- 238000010438 heat treatment Methods 0.000 description 2
- 102000057770 human C3 Human genes 0.000 description 2
- 230000002209 hydrophobic effect Effects 0.000 description 2
- 208000015181 infectious disease Diseases 0.000 description 2
- 230000002757 inflammatory effect Effects 0.000 description 2
- 230000004054 inflammatory process Effects 0.000 description 2
- 230000028709 inflammatory response Effects 0.000 description 2
- 230000002452 interceptive effect Effects 0.000 description 2
- 238000001361 intraarterial administration Methods 0.000 description 2
- 238000007918 intramuscular administration Methods 0.000 description 2
- 230000003902 lesion Effects 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 239000012669 liquid formulation Substances 0.000 description 2
- 239000012160 loading buffer Substances 0.000 description 2
- 238000001000 micrograph Methods 0.000 description 2
- 238000010369 molecular cloning Methods 0.000 description 2
- 238000003199 nucleic acid amplification method Methods 0.000 description 2
- 201000003045 paroxysmal nocturnal hemoglobinuria Diseases 0.000 description 2
- 230000000770 proinflammatory effect Effects 0.000 description 2
- 230000001737 promoting effect Effects 0.000 description 2
- 230000000069 prophylactic effect Effects 0.000 description 2
- 238000011321 prophylaxis Methods 0.000 description 2
- 235000019419 proteases Nutrition 0.000 description 2
- 235000004252 protein component Nutrition 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 238000003259 recombinant expression Methods 0.000 description 2
- 230000007115 recruitment Effects 0.000 description 2
- 230000002829 reductive effect Effects 0.000 description 2
- 230000010076 replication Effects 0.000 description 2
- 230000004258 retinal degeneration Effects 0.000 description 2
- 210000000844 retinal pigment epithelial cell Anatomy 0.000 description 2
- 230000002441 reversible effect Effects 0.000 description 2
- 102200033400 rs1085307884 Human genes 0.000 description 2
- 102200031829 rs121913056 Human genes 0.000 description 2
- 102200031710 rs121913059 Human genes 0.000 description 2
- 102220011966 rs397515734 Human genes 0.000 description 2
- 102220008957 rs398122873 Human genes 0.000 description 2
- 239000002356 single layer Substances 0.000 description 2
- 235000009518 sodium iodide Nutrition 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 238000007920 subcutaneous administration Methods 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 238000013268 sustained release Methods 0.000 description 2
- 239000012730 sustained-release form Substances 0.000 description 2
- 208000024891 symptom Diseases 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 230000009885 systemic effect Effects 0.000 description 2
- 230000000699 topical effect Effects 0.000 description 2
- 238000013519 translation Methods 0.000 description 2
- 230000007306 turnover Effects 0.000 description 2
- 230000002792 vascular Effects 0.000 description 2
- YTZALCGQUPRCGW-ZSFNYQMMSA-N verteporfin Chemical compound N1C(C=C2C(=C(CCC(O)=O)C(C=C3C(CCC(=O)OC)=C(C)C(N3)=C3)=N2)C)=C(C=C)C(C)=C1C=C1C2=CC=C(C(=O)OC)[C@@H](C(=O)OC)[C@@]2(C)C3=N1 YTZALCGQUPRCGW-ZSFNYQMMSA-N 0.000 description 2
- 230000000007 visual effect Effects 0.000 description 2
- 241001655883 Adeno-associated virus - 1 Species 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 206010003694 Atrophy Diseases 0.000 description 1
- 102100022794 Bestrophin-1 Human genes 0.000 description 1
- 241000282817 Bovidae Species 0.000 description 1
- 102100037080 C4b-binding protein beta chain Human genes 0.000 description 1
- 238000010354 CRISPR gene editing Methods 0.000 description 1
- 241000700199 Cavia porcellus Species 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 102100031609 Complement C2 Human genes 0.000 description 1
- 108090000955 Complement C2 Proteins 0.000 description 1
- 108010028780 Complement C3 Proteins 0.000 description 1
- 108010078015 Complement C3b Proteins 0.000 description 1
- 102100025680 Complement decay-accelerating factor Human genes 0.000 description 1
- 102000003712 Complement factor B Human genes 0.000 description 1
- 102100035324 Complement factor H-related protein 4 Human genes 0.000 description 1
- 102100030886 Complement receptor type 1 Human genes 0.000 description 1
- 238000005698 Diels-Alder reaction Methods 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 102000005593 Endopeptidases Human genes 0.000 description 1
- 108010059378 Endopeptidases Proteins 0.000 description 1
- 241000588921 Enterobacteriaceae Species 0.000 description 1
- 241000283074 Equus asinus Species 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- 102000004961 Furin Human genes 0.000 description 1
- 108090001126 Furin Proteins 0.000 description 1
- 101000834253 Gallus gallus Actin, cytoplasmic 1 Proteins 0.000 description 1
- 208000034826 Genetic Predisposition to Disease Diseases 0.000 description 1
- 102000051366 Glycosyltransferases Human genes 0.000 description 1
- 108700023372 Glycosyltransferases Proteins 0.000 description 1
- 208000009889 Herpes Simplex Diseases 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101000903449 Homo sapiens Bestrophin-1 Proteins 0.000 description 1
- 101000740689 Homo sapiens C4b-binding protein beta chain Proteins 0.000 description 1
- 101000856022 Homo sapiens Complement decay-accelerating factor Proteins 0.000 description 1
- 101000878133 Homo sapiens Complement factor H-related protein 4 Proteins 0.000 description 1
- 101000961414 Homo sapiens Membrane cofactor protein Proteins 0.000 description 1
- 101000702559 Homo sapiens Probable global transcription activator SNF2L2 Proteins 0.000 description 1
- 101000729271 Homo sapiens Retinoid isomerohydrolase Proteins 0.000 description 1
- 208000026350 Inborn Genetic disease Diseases 0.000 description 1
- 102000004856 Lectins Human genes 0.000 description 1
- 108090001090 Lectins Proteins 0.000 description 1
- 102100039373 Membrane cofactor protein Human genes 0.000 description 1
- 238000006957 Michael reaction Methods 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 241000009328 Perro Species 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 101710136899 Replication enhancer protein Proteins 0.000 description 1
- 102100031176 Retinoid isomerohydrolase Human genes 0.000 description 1
- 206010040047 Sepsis Diseases 0.000 description 1
- 108010090804 Streptavidin Proteins 0.000 description 1
- 241000282898 Sus scrofa Species 0.000 description 1
- 239000007984 Tris EDTA buffer Substances 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 238000005411 Van der Waals force Methods 0.000 description 1
- 208000000208 Wet Macular Degeneration Diseases 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 150000001266 acyl halides Chemical class 0.000 description 1
- 230000032683 aging Effects 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 238000003277 amino acid sequence analysis Methods 0.000 description 1
- 230000001640 apoptogenic effect Effects 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 210000001742 aqueous humor Anatomy 0.000 description 1
- 210000001367 artery Anatomy 0.000 description 1
- 210000004507 artificial chromosome Anatomy 0.000 description 1
- 210000001106 artificial yeast chromosome Anatomy 0.000 description 1
- 239000012298 atmosphere Substances 0.000 description 1
- 230000037444 atrophy Effects 0.000 description 1
- 229940120638 avastin Drugs 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 244000052616 bacterial pathogen Species 0.000 description 1
- SQVRNKJHWKZAKO-UHFFFAOYSA-N beta-N-Acetyl-D-neuraminic acid Natural products CC(=O)NC1C(O)CC(O)(C(O)=O)OC1C(O)C(O)CO SQVRNKJHWKZAKO-UHFFFAOYSA-N 0.000 description 1
- 229960000397 bevacizumab Drugs 0.000 description 1
- 239000012620 biological material Substances 0.000 description 1
- 239000012472 biological sample Substances 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- CREMABGTGYGIQB-UHFFFAOYSA-N carbon carbon Chemical compound C.C CREMABGTGYGIQB-UHFFFAOYSA-N 0.000 description 1
- 239000011203 carbon fibre reinforced carbon Substances 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 210000003986 cell retinal photoreceptor Anatomy 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 230000001684 chronic effect Effects 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 230000002860 competitive effect Effects 0.000 description 1
- 230000001010 compromised effect Effects 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 239000003636 conditioned culture medium Substances 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 210000004748 cultured cell Anatomy 0.000 description 1
- 230000002380 cytological effect Effects 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 210000005220 cytoplasmic tail Anatomy 0.000 description 1
- 235000013365 dairy product Nutrition 0.000 description 1
- 238000007405 data analysis Methods 0.000 description 1
- 230000007850 degeneration Effects 0.000 description 1
- 230000002939 deleterious effect Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 208000011325 dry age related macular degeneration Diseases 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 238000007336 electrophilic substitution reaction Methods 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 230000009881 electrostatic interaction Effects 0.000 description 1
- 150000002081 enamines Chemical class 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 210000002919 epithelial cell Anatomy 0.000 description 1
- 150000002148 esters Chemical class 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 230000029142 excretion Effects 0.000 description 1
- 229940051306 eylea Drugs 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 238000011049 filling Methods 0.000 description 1
- 238000013534 fluorescein angiography Methods 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 238000001476 gene delivery Methods 0.000 description 1
- 208000016361 genetic disease Diseases 0.000 description 1
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 230000023597 hemostasis Effects 0.000 description 1
- 230000005745 host immune response Effects 0.000 description 1
- 102000045512 human CFH Human genes 0.000 description 1
- 102000048439 human SMARCA2 Human genes 0.000 description 1
- 239000000017 hydrogel Substances 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 230000005934 immune activation Effects 0.000 description 1
- 210000002865 immune cell Anatomy 0.000 description 1
- 230000032226 immune complex clearance Effects 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 238000009169 immunotherapy Methods 0.000 description 1
- 239000007943 implant Substances 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 230000015788 innate immune response Effects 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 208000017169 kidney disease Diseases 0.000 description 1
- 150000002605 large molecules Chemical class 0.000 description 1
- 239000002523 lectin Substances 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 238000011528 liquid biopsy Methods 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 230000033001 locomotion Effects 0.000 description 1
- 208000018769 loss of vision Diseases 0.000 description 1
- 231100000864 loss of vision Toxicity 0.000 description 1
- 229940076783 lucentis Drugs 0.000 description 1
- 239000012139 lysis buffer Substances 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 229940092110 macugen Drugs 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 102000006240 membrane receptors Human genes 0.000 description 1
- 108020004084 membrane receptors Proteins 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 230000002503 metabolic effect Effects 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 238000001823 molecular biology technique Methods 0.000 description 1
- 208000028284 monogenic inheritance Diseases 0.000 description 1
- 230000004660 morphological change Effects 0.000 description 1
- 238000002887 multiple sequence alignment Methods 0.000 description 1
- 210000000822 natural killer cell Anatomy 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 238000010534 nucleophilic substitution reaction Methods 0.000 description 1
- 210000004940 nucleus Anatomy 0.000 description 1
- 230000009437 off-target effect Effects 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 230000036542 oxidative stress Effects 0.000 description 1
- 238000002888 pairwise sequence alignment Methods 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 230000008506 pathogenesis Effects 0.000 description 1
- 229960003407 pegaptanib Drugs 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 210000001539 phagocyte Anatomy 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- 238000002428 photodynamic therapy Methods 0.000 description 1
- 108091008695 photoreceptors Proteins 0.000 description 1
- 230000008488 polyadenylation Effects 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 1
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 208000011511 primary membranoproliferative glomerulonephritis Diseases 0.000 description 1
- 230000000750 progressive effect Effects 0.000 description 1
- 235000019833 protease Nutrition 0.000 description 1
- 238000000159 protein binding assay Methods 0.000 description 1
- 238000000164 protein isolation Methods 0.000 description 1
- 230000009145 protein modification Effects 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 229960003876 ranibizumab Drugs 0.000 description 1
- 239000000376 reactant Substances 0.000 description 1
- 210000003994 retinal ganglion cell Anatomy 0.000 description 1
- 210000003935 rough endoplasmic reticulum Anatomy 0.000 description 1
- 102200103620 rs121908920 Human genes 0.000 description 1
- 102220005752 rs1410996 Human genes 0.000 description 1
- 102200147378 rs398123072 Human genes 0.000 description 1
- 102200037607 rs771019366 Human genes 0.000 description 1
- 238000005070 sampling Methods 0.000 description 1
- 231100000241 scar Toxicity 0.000 description 1
- 230000037390 scarring Effects 0.000 description 1
- 230000009291 secondary effect Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- SQVRNKJHWKZAKO-OQPLDHBCSA-N sialic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)OC1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-OQPLDHBCSA-N 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 238000010532 solid phase synthesis reaction Methods 0.000 description 1
- 238000000638 solvent extraction Methods 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- 235000013599 spices Nutrition 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 230000008093 supporting effect Effects 0.000 description 1
- 230000008961 swelling Effects 0.000 description 1
- 238000007910 systemic administration Methods 0.000 description 1
- 238000002626 targeted therapy Methods 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 210000001138 tear Anatomy 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 238000010257 thawing Methods 0.000 description 1
- 238000001089 thermophoresis Methods 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 230000010474 transient expression Effects 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 108010087967 type I signal peptidase Proteins 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 210000005166 vasculature Anatomy 0.000 description 1
- 239000003981 vehicle Substances 0.000 description 1
- 210000003462 vein Anatomy 0.000 description 1
- 229960003895 verteporfin Drugs 0.000 description 1
- 229940061392 visudyne Drugs 0.000 description 1
- 210000004127 vitreous body Anatomy 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/1703—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- A61K38/1709—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P27/00—Drugs for disorders of the senses
- A61P27/02—Ophthalmic agents
-
- 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
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/70596—Molecules with a "CD"-designation not provided for elsewhere
-
- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
- C12N15/85—Vectors or expression systems specially adapted for eukaryotic hosts for animal cells
- C12N15/86—Viral vectors
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- 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
- C12N2750/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA ssDNA viruses
- C12N2750/00011—Details
- C12N2750/14011—Parvoviridae
- C12N2750/14111—Dependovirus, e.g. adenoassociated viruses
- C12N2750/14141—Use of virus, viral particle or viral elements as a vector
- C12N2750/14143—Use of virus, viral particle or viral elements as a vector viral genome or elements thereof as genetic vector
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Biophysics (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Toxicology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Immunology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Ophthalmology & Optometry (AREA)
- Wood Science & Technology (AREA)
- General Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Epidemiology (AREA)
- Marine Sciences & Fisheries (AREA)
- Virology (AREA)
- Cell Biology (AREA)
- Plant Pathology (AREA)
- Microbiology (AREA)
- Physics & Mathematics (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP2024096034A JP7858722B2 (ja) | 2018-01-15 | 2024-06-13 | Ｃ３ｂ結合ポリペプチド |
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GBGB1800620.5A GB201800620D0 (en) | 2018-01-15 | 2018-01-15 | C3b Binding Polypeptide |
| GB1800620.5 | 2018-01-15 | ||
| PCT/EP2019/050949 WO2019138137A1 (en) | 2018-01-15 | 2019-01-15 | C3b binding polypeptide |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2024096034A Division JP7858722B2 (ja) | 2018-01-15 | 2024-06-13 | Ｃ３ｂ結合ポリペプチド |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2021511030A JP2021511030A (ja) | 2021-05-06 |
| JP2021511030A5 JP2021511030A5 (enExample) | 2022-01-25 |
| JP7505980B2 true JP7505980B2 (ja) | 2024-06-25 |
Family
ID=61256254
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2020538949A Active JP7505980B2 (ja) | 2018-01-15 | 2019-01-15 | Ｃ３ｂ結合ポリペプチド |
| JP2024096034A Active JP7858722B2 (ja) | 2018-01-15 | 2024-06-13 | Ｃ３ｂ結合ポリペプチド |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2024096034A Active JP7858722B2 (ja) | 2018-01-15 | 2024-06-13 | Ｃ３ｂ結合ポリペプチド |
Country Status (8)
| Country | Link |
|---|---|
| US (3) | US11524050B2 (enExample) |
| EP (2) | EP3740498A1 (enExample) |
| JP (2) | JP7505980B2 (enExample) |
| CN (2) | CN119120483A (enExample) |
| AU (2) | AU2019207457B2 (enExample) |
| CA (1) | CA3088476A1 (enExample) |
| GB (1) | GB201800620D0 (enExample) |
| WO (1) | WO2019138137A1 (enExample) |
Families Citing this family (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB201800620D0 (en) | 2018-01-15 | 2018-02-28 | Univ Manchester | C3b Binding Polypeptide |
| GB201821082D0 (en) | 2018-12-21 | 2019-02-06 | Gyroscope Therapeutics Ltd | Combination of complement factors i and h, and vector encoding thereof |
| MX2022004939A (es) * | 2019-10-23 | 2022-08-10 | Gemini Therapeutics Sub Inc | Metodos para tratar pacientes que tienen mutaciones de cfh con proteinas de cfh recombinantes. |
| GB202006789D0 (en) | 2020-05-07 | 2020-06-24 | Univ Manchester | Detection of complement proteins |
| EP4214515A1 (en) | 2020-09-16 | 2023-07-26 | Complement Therapeutics Limited | Complementome assay |
| GB202107586D0 (en) | 2021-05-27 | 2021-07-14 | Complement Therapeutics Ltd | Inhibitory nucleic acids for Factor H family proteins |
| TWI917717B (zh) | 2021-11-19 | 2026-03-11 | 圓祥生技股份有限公司 | 針對補體途徑的雙功能融合蛋白、其醫藥組成物及其治療或預防補體相關疾病的用途 |
| GB202203627D0 (en) | 2022-03-16 | 2022-04-27 | Univ Manchester | Agents for treating complement-related disorders |
| WO2024146953A1 (en) | 2023-01-05 | 2024-07-11 | Complement Therapeutics Limited | Agents and methods for treating complement diseases |
Citations (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2011503024A (ja) | 2007-11-02 | 2011-01-27 | ノバルティス アーゲー | 補体成分を調節するための分子および方法 |
| JP2011504872A (ja) | 2007-06-07 | 2011-02-17 | ジェネンテック， インコーポレイテッド | 補体が関係している障害の予防および処置のためのｃ３ｂ抗体ならびに方法 |
| JP2015500811A (ja) | 2011-12-01 | 2015-01-08 | プロテボビオ， インコーポレイテッド | 補体経路およびｖｅｇｆ経路に対するタンパク質インヒビターおよびそれらの使用方法 |
| WO2017194912A1 (en) | 2016-05-09 | 2017-11-16 | Cambridge Enterprise Limited | Treatment of complement-mediated disorders |
| WO2018002131A1 (en) | 2016-06-28 | 2018-01-04 | Universität Ulm | Complement inhibitors and uses thereof |
| JP7341897B2 (ja) | 2017-06-09 | 2023-09-11 | コンプリメント・セラピューティクス・リミテッド | Ｃ３ｂ不活性化ポリペプチド |
Family Cites Families (92)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5981481A (en) * | 1974-12-06 | 1999-11-09 | The Johns Hopkins University | Human C3b/C4b receptor (CR1) |
| JPH0742235B2 (ja) | 1985-11-08 | 1995-05-10 | 三共株式会社 | 自己免疫性疾病の予防・治療剤 |
| DE3600368C1 (de) | 1986-01-09 | 1987-04-02 | Goldschmidt Ag Th | Trennmittel fuer Polyurethanformteile |
| IL89790A (en) | 1988-04-01 | 2002-05-23 | Johns Hopking University | Nucleic acid sequences that encode and cells that produce cr1 protein and methods of production and purification |
| US6458360B1 (en) | 1990-04-25 | 2002-10-01 | The Johns Hopkins University | Soluble complement regulatory molecules |
| CA2097825A1 (en) | 1990-12-06 | 1992-06-07 | Henry C. Marsh, Jr. | Synergistic compositions of soluble complement receptors and compounds that inhibit complement and/or suppress immune activity |
| DE69328098T2 (de) | 1992-06-24 | 2000-08-24 | Adprotech Plc, Royston | Lösliche derivate des complement type-rezeptors (cr1) |
| GB9301289D0 (en) | 1993-01-22 | 1993-03-17 | Smithkline Beecham Plc | Novel composition |
| US5679546A (en) | 1993-09-24 | 1997-10-21 | Cytomed, Inc. | Chimeric proteins which block complement activation |
| US5648244A (en) | 1993-09-27 | 1997-07-15 | President And Fellows Of Harvard College | Production, purification, cleavage and use of fusion peptides |
| WO1999044625A1 (en) | 1998-03-03 | 1999-09-10 | John Hopkins University | Smallpox inhibitor of complement enzymes (spice) protein and methods of inhibiting complement activation |
| WO2000061752A2 (en) | 1999-04-09 | 2000-10-19 | Washington University | Modified complement system regulators |
| JP2003527115A (ja) | 2000-03-13 | 2003-09-16 | セント ビンセンツ ホスピタル | 新規のｈ因子関連タンパク質５及びその抗体 |
| US20030086940A1 (en) | 2001-08-10 | 2003-05-08 | Cristina Costa | Engineered recombinant molecule that regulates humoral and cellular effector functions of the immune system |
| WO2004031733A2 (en) | 2002-10-02 | 2004-04-15 | Catalyst Biosciences | Methods of generating and screenign for porteases with altered specificity |
| AU2004216176B2 (en) | 2003-02-21 | 2008-04-03 | Genentech, Inc. | Methods for preventing and treating tissue damage associated with ischemia-reperfusion injury |
| EP1594541A4 (en) | 2003-02-21 | 2007-03-28 | Rikshospitalet Radiumhospitale | METHOD AND COMPOSITIONS FOR TREATING MECONIUM ASPIRATION SYNDROME |
| EP2266606B1 (en) | 2003-05-15 | 2014-09-10 | Genentech, Inc. | Methods and compositions for the prevention and treatment of sepsis |
| WO2005014849A2 (en) | 2003-07-03 | 2005-02-17 | Euro-Celtique, S.A. | Genes associated with responses to neuropathic pain |
| US20050214318A1 (en) | 2003-10-23 | 2005-09-29 | Nmk Research, Llc | Immunogenic composition and method of developing a vaccine based on fusion protein |
| WO2005069726A2 (en) * | 2004-01-21 | 2005-08-04 | Case Western Reserve University | Hybrid and chimeric polypeptides that regulate activation of complement |
| JP2005211063A (ja) | 2004-01-30 | 2005-08-11 | Junko Maekuroshima | ブレンドノニ茶 |
| US20050169921A1 (en) | 2004-02-03 | 2005-08-04 | Leonard Bell | Method of treating hemolytic disease |
| US20050277158A1 (en) | 2004-06-10 | 2005-12-15 | Ge Chen | Method and kit for donor specific complement-fixing antibodies crossmatch |
| WO2006012373A2 (en) | 2004-07-20 | 2006-02-02 | Critical Therapeutics, Inc. | Combination therapies of hmgb and complement inhibitors against inflammation |
| US7745389B2 (en) | 2005-02-14 | 2010-06-29 | University Of Iowa Research Foundation | Methods for treatment of age-related macular degeneration |
| JP2008540385A (ja) | 2005-05-06 | 2008-11-20 | ラボラトワール セローノ ソシエテ アノニム | 疾患を治療するための免疫グロブリンドメイン含有細胞表面認識分子の使用 |
| KR101126423B1 (ko) | 2005-10-21 | 2012-07-11 | 카탈리스트 바이오사이언시즈, 인코포레이티드 | 보체 활성화를 억제하는 변형된 프로테아제 |
| DK2500030T4 (en) | 2005-11-04 | 2018-10-29 | Genentech Inc | Use of complement pathway inhibitors for the treatment of eye diseases |
| JP5250548B2 (ja) | 2006-06-21 | 2013-07-31 | エムユーエスシー ファウンデーション フォー リサーチ ディベロップメント | 疾患の治療のための補体ｈ因子の標的化 |
| DE602007011937D1 (de) | 2006-07-03 | 2011-02-24 | Univ Johns Hopkins | Peptidantikörperdepletion und anwendung zur probenvorbereitung für massenspektrometrie |
| DK2447275T3 (en) | 2006-07-13 | 2015-06-29 | Univ Iowa Res Found | Methods and reagents for the treatment of age-related macular degeneration |
| CA2666843C (en) | 2006-10-20 | 2015-06-16 | Celldex Therapeutics, Inc. | Treatment of age-related macular degeneration and other diseases of the eye |
| CN106084055A (zh) | 2006-11-02 | 2016-11-09 | 健泰科生物技术公司 | 人源化的抗‑d因子抗体 |
| GB0701213D0 (en) | 2007-01-23 | 2007-02-28 | Univ Cardiff | Factor H polymorphisms in the diagnosis and therapy of inflammatory diseases such as age-related macular degeneration |
| MX2009009200A (es) | 2007-03-01 | 2009-10-28 | Advanced Vision Therapies Inc | Tratamiento de enfermedades caracterizadas por la inflamacion. |
| GB2447696A (en) | 2007-03-23 | 2008-09-24 | Univ Exeter | Photonic biosensor arrays |
| GB2447698A (en) | 2007-03-23 | 2008-09-24 | Univ Exeter | Fabrication of photonic biosensor arrays |
| WO2009022246A1 (en) | 2007-08-10 | 2009-02-19 | Koninklijke Philips Electronics N.V. | Sensor array for spr-based detection. |
| WO2009059317A2 (en) | 2007-11-01 | 2009-05-07 | University Of Iowa Research Foundation | Predicting amd with snps within or near c2, factor b, plekha1, htra1, prelp, or loc387715 |
| WO2009121065A2 (en) | 2008-03-28 | 2009-10-01 | Apellis Ag | Modulation and repletion/enhancement of the complement system for treatment of trauma |
| CR20170001A (es) | 2008-04-28 | 2017-08-10 | Genentech Inc | Anticuerpos anti factor d humanizados |
| WO2009151634A1 (en) | 2008-06-12 | 2009-12-17 | The Board Of Trustees Of The Leland Stanford Junior University | Complement inhibitory agents as therapeutics in posttraumatic and degenerative arthritis |
| US8476032B2 (en) | 2008-08-27 | 2013-07-02 | Children's Hospital & Research Center Oakland | Complement factor H-based assays for serum bactericidal activity against Neisseria meningitidis |
| GB0815576D0 (en) | 2008-08-28 | 2008-10-01 | Lucas & Co | Analysis of glycated proteins |
| US8937046B2 (en) | 2008-09-22 | 2015-01-20 | The Regents Of The University Of Colorado, A Body Corporate | Modulating the alternative complement pathway |
| JP6223659B2 (ja) | 2008-11-10 | 2017-11-01 | アレクシオン ファーマシューティカルズ， インコーポレイテッド | 補体関連障害を処置するための方法および組成物 |
| WO2010056399A1 (en) | 2008-11-17 | 2010-05-20 | Incode Biopharmaceutics, Inc. | Method and composition for modulating the immune system and various inflammatory conditions comprising complement depletors |
| EP3150635A3 (en) | 2009-10-16 | 2017-06-21 | Omeros Corporation | Methods for treating disseminated intravascular coagulation by inhibiting masp-2 dependent complement activation |
| CN102958535A (zh) | 2009-11-05 | 2013-03-06 | 亚力史剑桥公司 | 阵发性夜间血红蛋白尿、溶血性贫血和涉及血管内和血管外溶血的疾病状态的治疗 |
| GB0922659D0 (en) | 2009-12-24 | 2010-02-10 | Univ Edinburgh | Factor H |
| WO2011109338A1 (en) | 2010-03-01 | 2011-09-09 | Alexion Pharmaceuticals Inc. | Methods and compositions for treating degos' disease |
| AU2011222883B2 (en) | 2010-03-05 | 2016-05-26 | Omeros Corporation | Chimeric inhibitor molecules of complement activation |
| WO2011130844A1 (en) | 2010-04-22 | 2011-10-27 | Patricia Marlen Nieva | Method and apparatus for an interferometric localized surface plasmon resonance (ilspr) sensor |
| MX2012013233A (es) | 2010-05-14 | 2013-05-20 | Univ Colorado Regents | Grupos que apuntan a receptor 2 de complemento (cr2) mejorados. |
| BR112012033119A2 (pt) | 2010-06-22 | 2016-10-25 | Univ Colorado Regents | anticorpos para o fragamento c3d do componente do complemento 3. |
| JP6092776B2 (ja) | 2010-09-15 | 2017-03-08 | セルデックス セラピューティクス インコーポレイテッド | 可溶性補体受容体Ｉ型（ｓＣＲ１）を用いる慢性腎症の処置 |
| KR20130130732A (ko) | 2010-11-01 | 2013-12-02 | 제넨테크, 인크. | 다유전자 스코어를 이용한 진행성 노인성 황반 변성으로의 진행 예측 |
| WO2012095519A1 (en) | 2011-01-13 | 2012-07-19 | Leibniz-Institut Für Naturstoff-Forschung Und Infektionsbiologie | Potent inhibitors of complement activation |
| DK2694108T3 (en) | 2011-04-08 | 2018-08-20 | Univ Leicester | METHODS OF TREATING DISEASES ASSOCIATED WITH MASP-2 DEPENDENT COMPLEMENT ACTIVATION |
| WO2013151664A1 (en) * | 2012-04-02 | 2013-10-10 | modeRNA Therapeutics | Modified polynucleotides for the production of proteins |
| EA201492055A1 (ru) | 2012-06-08 | 2015-11-30 | Шир Хьюман Дженетик Терапис, Инк. | ИНГАЛЯЦИОННАЯ ДОСТАВКА мРНК В НЕЛЕГОЧНЫЕ КЛЕТКИ-МИШЕНИ |
| US20150366997A1 (en) | 2012-12-07 | 2015-12-24 | Shire Human Genetics Therapies, Inc. | COMPOSITIONS AND METHODS FOR mRNA DELIVERY |
| CA2899034A1 (en) | 2013-01-23 | 2014-07-31 | Musc Foundation For Research Development | Targeting constructs based on natural antibodies and uses thereof |
| GB201301632D0 (en) | 2013-01-30 | 2013-03-13 | Imp Innovations | Complement System |
| PT2970974T (pt) | 2013-03-14 | 2017-11-29 | Alnylam Pharmaceuticals Inc | Composições de irna de componente do complemento c5 e métodos para a sua utilização |
| WO2014194213A1 (en) | 2013-05-30 | 2014-12-04 | University Of Iowa Research Foundation | Specific complement proteins and efficacy of antibody therapy |
| EP3003372B1 (en) | 2013-06-07 | 2019-10-09 | Duke University | Inhibitors of complement factor h |
| EP3033093A1 (en) | 2013-08-16 | 2016-06-22 | Alexion Pharmaceuticals, Inc. | Treatment of graft rejection by administering a complement inhibitor to an organ prior to transplant |
| CN104231085B (zh) | 2013-09-05 | 2017-03-15 | 复旦大学附属肿瘤医院 | 靶向特异性补体系统抑制剂、其制备方法及应用 |
| GB201318170D0 (en) | 2013-10-14 | 2013-11-27 | Univ Edinburgh | Proteins with Diagnostic and Therapeutic Uses |
| ES3032935T3 (en) | 2013-10-22 | 2025-07-29 | Translate Bio Inc | Lipid formulations for delivery of messenger rna |
| FR3015484A1 (fr) * | 2013-12-20 | 2015-06-26 | Lab Francais Du Fractionnement | Proteines recombinantes possedant une activite de facteur h |
| EP3177732A4 (en) | 2014-08-08 | 2018-04-25 | ModernaTX, Inc. | Compositions and methods for the treatment of ophthalmic diseases and conditions |
| AU2015304079B2 (en) | 2014-08-20 | 2021-05-13 | Stichting Sanquin Bloedvoorziening | Factor H potentiating antibodies and uses thereof |
| KR101808762B1 (ko) | 2014-10-29 | 2017-12-14 | 차의과학대학교 산학협력단 | C3 또는 C1r 보체를 분비하는 태반 유래 세포 및 이를 포함하는 조성물 |
| US20210318287A1 (en) | 2015-02-16 | 2021-10-14 | The Regents Of The University Of Michigan | Localized surface plasmon resonance sensor systems and methods |
| AU2016239949A1 (en) | 2015-03-31 | 2017-09-07 | Sorriso Pharmaceuticals, Inc. | Peptide construct having a protease-cleavable linker |
| EP3359663A4 (en) * | 2015-09-24 | 2019-08-14 | The Trustees of The University of Pennsylvania | COMPOSITION AND METHOD FOR THE TREATMENT OF A COMPLEMENT-MEDIATED DISEASE |
| JP2019515027A (ja) | 2016-04-15 | 2019-06-06 | レジェンクスバイオ インコーポレーテッド | 翻訳後修飾された完全ヒト抗ＶＥＧＦ Ｆａｂを用いる眼疾患の治療 |
| CA3070915C (en) | 2017-07-25 | 2023-08-08 | Biocon Limited | Peptide mapping method for sequence identification of insulin & insulin analogues |
| GB201800620D0 (en) | 2018-01-15 | 2018-02-28 | Univ Manchester | C3b Binding Polypeptide |
| WO2019178280A1 (en) | 2018-03-13 | 2019-09-19 | Amgen Inc. | Sequential digestion of polypeptides for mass spectrometric analysis |
| JP7467355B2 (ja) | 2018-05-10 | 2024-04-15 | コンプリメント・セラピューティクス・リミテッド | 黄斑変性症を評価するための方法 |
| CN112118859A (zh) | 2018-05-16 | 2020-12-22 | 杰特有限公司 | 1型可溶性补体受体变体及其用途 |
| MX2021006930A (es) | 2018-12-11 | 2021-11-17 | Q32 Bio Inc | Construcciones de proteínas de fusión para enfermedades asociadas al complemento. |
| GB201821082D0 (en) | 2018-12-21 | 2019-02-06 | Gyroscope Therapeutics Ltd | Combination of complement factors i and h, and vector encoding thereof |
| KR20220019806A (ko) | 2019-06-12 | 2022-02-17 | 씨에스엘 이노베이션 피티와이 엘티디 | 가용성 보체 수용체 1형 변이체 접합체 및 이의 용도 |
| GB202006789D0 (en) | 2020-05-07 | 2020-06-24 | Univ Manchester | Detection of complement proteins |
| GB202007353D0 (en) | 2020-05-18 | 2020-07-01 | Shaw Andrew | Viral infection characterization |
| US20210373009A1 (en) | 2020-05-28 | 2021-12-02 | University Of North Texas | Plasmonic meta-surface based molecular sensors and methods for making and using them |
| KR20230088630A (ko) | 2020-10-16 | 2023-06-20 | 자이로스코프 테라퓨틱스 리미티드 | 항-vegf 엔티티 및 음성 보체 조절인자를 코딩하는 핵산 및 연령-관련 황반 변성의 치료를 위한 그의 용도 |
-
2018
- 2018-01-15 GB GBGB1800620.5A patent/GB201800620D0/en not_active Ceased
-
2019
- 2019-01-15 CA CA3088476A patent/CA3088476A1/en active Pending
- 2019-01-15 EP EP19701065.5A patent/EP3740498A1/en active Pending
- 2019-01-15 CN CN202411057957.XA patent/CN119120483A/zh active Pending
- 2019-01-15 CN CN201980016721.2A patent/CN111788219A/zh active Pending
- 2019-01-15 WO PCT/EP2019/050949 patent/WO2019138137A1/en not_active Ceased
- 2019-01-15 JP JP2020538949A patent/JP7505980B2/ja active Active
- 2019-01-15 AU AU2019207457A patent/AU2019207457B2/en active Active
- 2019-01-15 US US16/962,108 patent/US11524050B2/en active Active
- 2019-01-15 EP EP24213690.1A patent/EP4512822A3/en active Pending
-
2022
- 2022-10-20 US US18/048,303 patent/US12544423B2/en active Active
- 2022-11-04 US US18/052,768 patent/US12383600B2/en active Active
-
2024
- 2024-05-13 AU AU2024203142A patent/AU2024203142B2/en active Active
- 2024-06-13 JP JP2024096034A patent/JP7858722B2/ja active Active
Patent Citations (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2011504872A (ja) | 2007-06-07 | 2011-02-17 | ジェネンテック， インコーポレイテッド | 補体が関係している障害の予防および処置のためのｃ３ｂ抗体ならびに方法 |
| JP2011503024A (ja) | 2007-11-02 | 2011-01-27 | ノバルティス アーゲー | 補体成分を調節するための分子および方法 |
| JP2015500811A (ja) | 2011-12-01 | 2015-01-08 | プロテボビオ， インコーポレイテッド | 補体経路およびｖｅｇｆ経路に対するタンパク質インヒビターおよびそれらの使用方法 |
| WO2017194912A1 (en) | 2016-05-09 | 2017-11-16 | Cambridge Enterprise Limited | Treatment of complement-mediated disorders |
| WO2018002131A1 (en) | 2016-06-28 | 2018-01-04 | Universität Ulm | Complement inhibitors and uses thereof |
| JP7341897B2 (ja) | 2017-06-09 | 2023-09-11 | コンプリメント・セラピューティクス・リミテッド | Ｃ３ｂ不活性化ポリペプチド |
Also Published As
| Publication number | Publication date |
|---|---|
| JP2024123077A (ja) | 2024-09-10 |
| AU2024203142A1 (en) | 2024-06-06 |
| WO2019138137A1 (en) | 2019-07-18 |
| GB201800620D0 (en) | 2018-02-28 |
| AU2024203142B2 (en) | 2026-02-05 |
| EP4512822A3 (en) | 2025-04-30 |
| AU2019207457B2 (en) | 2024-02-15 |
| US20230310545A1 (en) | 2023-10-05 |
| EP3740498A1 (en) | 2020-11-25 |
| US12544423B2 (en) | 2026-02-10 |
| CN119120483A (zh) | 2024-12-13 |
| US12383600B2 (en) | 2025-08-12 |
| CA3088476A1 (en) | 2019-07-18 |
| JP7858722B2 (ja) | 2026-05-14 |
| US11524050B2 (en) | 2022-12-13 |
| JP2021511030A (ja) | 2021-05-06 |
| US20210145933A1 (en) | 2021-05-20 |
| CN111788219A (zh) | 2020-10-16 |
| EP4512822A2 (en) | 2025-02-26 |
| US20230321184A1 (en) | 2023-10-12 |
| AU2019207457A1 (en) | 2020-08-27 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP7858722B2 (ja) | Ｃ３ｂ結合ポリペプチド | |
| JP7341897B2 (ja) | Ｃ３ｂ不活性化ポリペプチド | |
| US8071745B2 (en) | Polynucleotides encoding rod-derived cone viability factor (rdcvf) and methods of using the same | |
| JP2002543837A (ja) | 組換えセトマンナン結合性レクチン | |
| CN1143386A (zh) | 转化生长因子α-H1 | |
| JP2004524821A (ja) | 疾患のイメージング、診断、及び治療 | |
| JP2003515338A (ja) | 補体結合酵素、ｍａｓｐ−３、及びその使用 | |
| JP2002506625A (ja) | サイトカインレセプター共通γ鎖様 | |
| JP4111539B2 (ja) | 膵島新生に関与するｉｎｇａｐタンパク質 | |
| JP4242128B2 (ja) | 脳アミロイドーシス予防・治療薬のスクリーニング方法 | |
| CN102336812B (zh) | 一种具有抑制血管生成活性的多肽 | |
| US20110130335A1 (en) | Therapeutic agent and test agent for disease with myocardial necrosis | |
| CN1952129B (zh) | Angptl4缺失突变体及其应用 | |
| MXPA02004241A (es) | Regulacion de la expresion de genes por agentes neurolepticos. | |
| JP2001519180A (ja) | ラミニン及びそれらの利用 | |
| NZ616479A (en) | Complement factor b analogs and their uses |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20220117 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20220117 |
|
| A711 | Notification of change in applicant |
Free format text: JAPANESE INTERMEDIATE CODE: A711 Effective date: 20220722 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20220816 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20230118 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20230414 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20230619 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20230825 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20231122 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20240226 |
|
| TRDD | Decision of grant or rejection written | ||
| A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 Effective date: 20240515 |
|
| A61 | First payment of annual fees (during grant procedure) |
Free format text: JAPANESE INTERMEDIATE CODE: A61 Effective date: 20240613 |