EA019370B1 - Пептиды fviii и их применение для индукции толерантности у больных гемофилией - Google Patents
Пептиды fviii и их применение для индукции толерантности у больных гемофилией Download PDFInfo
- Publication number
- EA019370B1 EA019370B1 EA201070681A EA201070681A EA019370B1 EA 019370 B1 EA019370 B1 EA 019370B1 EA 201070681 A EA201070681 A EA 201070681A EA 201070681 A EA201070681 A EA 201070681A EA 019370 B1 EA019370 B1 EA 019370B1
- Authority
- EA
- Eurasian Patent Office
- Prior art keywords
- peptide
- peptides
- hemophilia
- cells
- factor viii
- Prior art date
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 194
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 91
- 101000911390 Homo sapiens Coagulation factor VIII Proteins 0.000 claims abstract description 23
- 201000003542 Factor VIII deficiency Diseases 0.000 claims abstract description 22
- 208000013633 acquired hemophilia Diseases 0.000 claims abstract description 19
- 230000015572 biosynthetic process Effects 0.000 claims abstract description 19
- 108010054218 Factor VIII Proteins 0.000 claims description 51
- 102000001690 Factor VIII Human genes 0.000 claims description 48
- 208000009292 Hemophilia A Diseases 0.000 claims description 46
- 229960000301 factor viii Drugs 0.000 claims description 46
- 239000000203 mixture Substances 0.000 claims description 38
- 238000011282 treatment Methods 0.000 claims description 25
- 208000031220 Hemophilia Diseases 0.000 claims description 24
- 102100026735 Coagulation factor VIII Human genes 0.000 claims description 18
- 201000010099 disease Diseases 0.000 claims description 12
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 12
- 238000009256 replacement therapy Methods 0.000 claims description 10
- 239000003112 inhibitor Substances 0.000 abstract description 23
- 230000030741 antigen processing and presentation Effects 0.000 abstract description 7
- 230000001629 suppression Effects 0.000 abstract description 5
- 102000018713 Histocompatibility Antigens Class II Human genes 0.000 abstract description 4
- 108010027412 Histocompatibility Antigens Class II Proteins 0.000 abstract description 4
- 102000057593 human F8 Human genes 0.000 abstract description 4
- 230000002265 prevention Effects 0.000 abstract 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 54
- 241000699670 Mus sp. Species 0.000 description 41
- 210000004027 cell Anatomy 0.000 description 29
- 108091007433 antigens Proteins 0.000 description 25
- 102000036639 antigens Human genes 0.000 description 25
- 150000001413 amino acids Chemical class 0.000 description 24
- 239000000427 antigen Substances 0.000 description 23
- 230000028993 immune response Effects 0.000 description 23
- 230000004044 response Effects 0.000 description 21
- 238000000034 method Methods 0.000 description 20
- 210000004408 hybridoma Anatomy 0.000 description 18
- 208000032843 Hemorrhage Diseases 0.000 description 15
- 210000000612 antigen-presenting cell Anatomy 0.000 description 15
- 230000002401 inhibitory effect Effects 0.000 description 14
- 102000015081 Blood Coagulation Factors Human genes 0.000 description 13
- 108010039209 Blood Coagulation Factors Proteins 0.000 description 13
- 239000003114 blood coagulation factor Substances 0.000 description 13
- 238000004519 manufacturing process Methods 0.000 description 12
- 238000012545 processing Methods 0.000 description 12
- 208000034158 bleeding Diseases 0.000 description 11
- 230000000740 bleeding effect Effects 0.000 description 11
- 108090000623 proteins and genes Proteins 0.000 description 11
- 102000043131 MHC class II family Human genes 0.000 description 10
- 108091054438 MHC class II family Proteins 0.000 description 10
- 238000006243 chemical reaction Methods 0.000 description 10
- 210000001165 lymph node Anatomy 0.000 description 10
- 238000006467 substitution reaction Methods 0.000 description 10
- 239000002671 adjuvant Substances 0.000 description 9
- 230000015271 coagulation Effects 0.000 description 9
- 238000005345 coagulation Methods 0.000 description 9
- 230000007423 decrease Effects 0.000 description 9
- 230000000694 effects Effects 0.000 description 8
- 230000006698 induction Effects 0.000 description 8
- 210000003719 b-lymphocyte Anatomy 0.000 description 7
- WQAQPCDUOCURKW-UHFFFAOYSA-N butanethiol Chemical compound CCCCS WQAQPCDUOCURKW-UHFFFAOYSA-N 0.000 description 7
- 239000003814 drug Substances 0.000 description 7
- 208000009429 hemophilia B Diseases 0.000 description 7
- 102000004169 proteins and genes Human genes 0.000 description 7
- 208000023275 Autoimmune disease Diseases 0.000 description 6
- 102100022641 Coagulation factor IX Human genes 0.000 description 6
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 6
- 229940079593 drug Drugs 0.000 description 6
- 210000004698 lymphocyte Anatomy 0.000 description 6
- 230000001225 therapeutic effect Effects 0.000 description 6
- 210000004369 blood Anatomy 0.000 description 5
- 239000008280 blood Substances 0.000 description 5
- 238000001415 gene therapy Methods 0.000 description 5
- 210000001503 joint Anatomy 0.000 description 5
- 230000007774 longterm Effects 0.000 description 5
- 230000035772 mutation Effects 0.000 description 5
- 206010011968 Decreased immune responsiveness Diseases 0.000 description 4
- 238000003776 cleavage reaction Methods 0.000 description 4
- 239000012141 concentrate Substances 0.000 description 4
- 230000006378 damage Effects 0.000 description 4
- 230000007812 deficiency Effects 0.000 description 4
- 230000002950 deficient Effects 0.000 description 4
- 210000000987 immune system Anatomy 0.000 description 4
- 238000012986 modification Methods 0.000 description 4
- 230000004048 modification Effects 0.000 description 4
- 230000035935 pregnancy Effects 0.000 description 4
- 230000035755 proliferation Effects 0.000 description 4
- 230000002829 reductive effect Effects 0.000 description 4
- 230000007017 scission Effects 0.000 description 4
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 3
- AHLPHDHHMVZTML-BYPYZUCNSA-N L-Ornithine Chemical compound NCCC[C@H](N)C(O)=O AHLPHDHHMVZTML-BYPYZUCNSA-N 0.000 description 3
- 102000043129 MHC class I family Human genes 0.000 description 3
- 108091054437 MHC class I family Proteins 0.000 description 3
- 241001465754 Metazoa Species 0.000 description 3
- 241000699660 Mus musculus Species 0.000 description 3
- AHLPHDHHMVZTML-UHFFFAOYSA-N Orn-delta-NH2 Natural products NCCCC(N)C(O)=O AHLPHDHHMVZTML-UHFFFAOYSA-N 0.000 description 3
- UTJLXEIPEHZYQJ-UHFFFAOYSA-N Ornithine Natural products OC(=O)C(C)CCCN UTJLXEIPEHZYQJ-UHFFFAOYSA-N 0.000 description 3
- 108010043958 Peptoids Proteins 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 230000005867 T cell response Effects 0.000 description 3
- 208000027418 Wounds and injury Diseases 0.000 description 3
- 125000000539 amino acid group Chemical group 0.000 description 3
- 206010003246 arthritis Diseases 0.000 description 3
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 3
- 229960000900 human factor viii Drugs 0.000 description 3
- 230000001939 inductive effect Effects 0.000 description 3
- 238000002347 injection Methods 0.000 description 3
- 239000007924 injection Substances 0.000 description 3
- 150000002632 lipids Chemical class 0.000 description 3
- 239000012528 membrane Substances 0.000 description 3
- 210000003205 muscle Anatomy 0.000 description 3
- 229960003104 ornithine Drugs 0.000 description 3
- 230000002093 peripheral effect Effects 0.000 description 3
- 239000008194 pharmaceutical composition Substances 0.000 description 3
- 239000000546 pharmaceutical excipient Substances 0.000 description 3
- 230000000069 prophylactic effect Effects 0.000 description 3
- 230000001105 regulatory effect Effects 0.000 description 3
- 230000000638 stimulation Effects 0.000 description 3
- 238000007920 subcutaneous administration Methods 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 238000003786 synthesis reaction Methods 0.000 description 3
- 229940104230 thymidine Drugs 0.000 description 3
- 210000001519 tissue Anatomy 0.000 description 3
- 238000011830 transgenic mouse model Methods 0.000 description 3
- PTOAARAWEBMLNO-KVQBGUIXSA-N Cladribine Chemical compound C1=NC=2C(N)=NC(Cl)=NC=2N1[C@H]1C[C@H](O)[C@@H](CO)O1 PTOAARAWEBMLNO-KVQBGUIXSA-N 0.000 description 2
- CMSMOCZEIVJLDB-UHFFFAOYSA-N Cyclophosphamide Chemical compound ClCCN(CCCl)P1(=O)NCCCO1 CMSMOCZEIVJLDB-UHFFFAOYSA-N 0.000 description 2
- PMATZTZNYRCHOR-CGLBZJNRSA-N Cyclosporin A Chemical compound CC[C@@H]1NC(=O)[C@H]([C@H](O)[C@H](C)C\C=C\C)N(C)C(=O)[C@H](C(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)N(C)C(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)N(C)C(=O)CN(C)C1=O PMATZTZNYRCHOR-CGLBZJNRSA-N 0.000 description 2
- 108010036949 Cyclosporine Proteins 0.000 description 2
- 229940124135 Factor VIII inhibitor Drugs 0.000 description 2
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
- 206010020751 Hypersensitivity Diseases 0.000 description 2
- 208000002193 Pain Diseases 0.000 description 2
- 229930040373 Paraformaldehyde Natural products 0.000 description 2
- 229930182555 Penicillin Natural products 0.000 description 2
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 2
- 108010033276 Peptide Fragments Proteins 0.000 description 2
- 102000007079 Peptide Fragments Human genes 0.000 description 2
- 239000002202 Polyethylene glycol Substances 0.000 description 2
- 102000001708 Protein Isoforms Human genes 0.000 description 2
- 108010029485 Protein Isoforms Proteins 0.000 description 2
- 208000026552 Severe hemophilia A Diseases 0.000 description 2
- 108091008874 T cell receptors Proteins 0.000 description 2
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 2
- 241000700605 Viruses Species 0.000 description 2
- 230000002378 acidificating effect Effects 0.000 description 2
- 230000004913 activation Effects 0.000 description 2
- 239000004480 active ingredient Substances 0.000 description 2
- 230000033289 adaptive immune response Effects 0.000 description 2
- 238000007792 addition Methods 0.000 description 2
- 208000026935 allergic disease Diseases 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 230000000890 antigenic effect Effects 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 125000004429 atom Chemical group 0.000 description 2
- UCMIRNVEIXFBKS-UHFFFAOYSA-N beta-alanine Chemical compound NCCC(O)=O UCMIRNVEIXFBKS-UHFFFAOYSA-N 0.000 description 2
- 230000023555 blood coagulation Effects 0.000 description 2
- 229960001265 ciclosporin Drugs 0.000 description 2
- 238000011109 contamination Methods 0.000 description 2
- 230000000139 costimulatory effect Effects 0.000 description 2
- 238000012258 culturing Methods 0.000 description 2
- 229960004397 cyclophosphamide Drugs 0.000 description 2
- 229930182912 cyclosporin Natural products 0.000 description 2
- 230000007547 defect Effects 0.000 description 2
- 238000012217 deletion Methods 0.000 description 2
- 230000037430 deletion Effects 0.000 description 2
- 210000004443 dendritic cell Anatomy 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 238000004108 freeze drying Methods 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 102000054766 genetic haplotypes Human genes 0.000 description 2
- 230000012010 growth Effects 0.000 description 2
- 230000001900 immune effect Effects 0.000 description 2
- 230000002163 immunogen Effects 0.000 description 2
- 230000016784 immunoglobulin production Effects 0.000 description 2
- 230000001506 immunosuppresive effect Effects 0.000 description 2
- 230000001976 improved effect Effects 0.000 description 2
- 238000001802 infusion Methods 0.000 description 2
- 208000014674 injury Diseases 0.000 description 2
- 238000001990 intravenous administration Methods 0.000 description 2
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 2
- 239000002502 liposome Substances 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 230000003211 malignant effect Effects 0.000 description 2
- 230000007246 mechanism Effects 0.000 description 2
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 2
- 201000006417 multiple sclerosis Diseases 0.000 description 2
- 238000006386 neutralization reaction Methods 0.000 description 2
- 229920002866 paraformaldehyde Polymers 0.000 description 2
- 230000036961 partial effect Effects 0.000 description 2
- 230000001575 pathological effect Effects 0.000 description 2
- 229940049954 penicillin Drugs 0.000 description 2
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 2
- 150000003904 phospholipids Chemical class 0.000 description 2
- 229920001223 polyethylene glycol Polymers 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- -1 pyriylalanine Chemical compound 0.000 description 2
- 229960004641 rituximab Drugs 0.000 description 2
- 230000003248 secreting effect Effects 0.000 description 2
- 210000004989 spleen cell Anatomy 0.000 description 2
- 230000002269 spontaneous effect Effects 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 229940124530 sulfonamide Drugs 0.000 description 2
- 150000003456 sulfonamides Chemical class 0.000 description 2
- 210000001541 thymus gland Anatomy 0.000 description 2
- 238000009966 trimming Methods 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- HDTRYLNUVZCQOY-UHFFFAOYSA-N α-D-glucopyranosyl-α-D-glucopyranoside Natural products OC1C(O)C(O)C(CO)OC1OC1C(O)C(O)C(O)C(CO)O1 HDTRYLNUVZCQOY-UHFFFAOYSA-N 0.000 description 1
- ABIFUJNCKIMWRZ-JGVFFNPUSA-N (2r,4s)-4-(3-phosphonopropyl)piperidine-2-carboxylic acid Chemical compound OC(=O)[C@H]1C[C@@H](CCCP(O)(O)=O)CCN1 ABIFUJNCKIMWRZ-JGVFFNPUSA-N 0.000 description 1
- IYKLZBIWFXPUCS-VIFPVBQESA-N (2s)-2-(naphthalen-1-ylamino)propanoic acid Chemical compound C1=CC=C2C(N[C@@H](C)C(O)=O)=CC=CC2=C1 IYKLZBIWFXPUCS-VIFPVBQESA-N 0.000 description 1
- BWKMGYQJPOAASG-UHFFFAOYSA-N 1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid Chemical compound C1=CC=C2CNC(C(=O)O)CC2=C1 BWKMGYQJPOAASG-UHFFFAOYSA-N 0.000 description 1
- IQFYYKKMVGJFEH-OFKYTIFKSA-N 1-[(2r,4s,5r)-4-hydroxy-5-(tritiooxymethyl)oxolan-2-yl]-5-methylpyrimidine-2,4-dione Chemical compound C1[C@H](O)[C@@H](CO[3H])O[C@H]1N1C(=O)NC(=O)C(C)=C1 IQFYYKKMVGJFEH-OFKYTIFKSA-N 0.000 description 1
- BLCJBICVQSYOIF-UHFFFAOYSA-N 2,2-diaminobutanoic acid Chemical compound CCC(N)(N)C(O)=O BLCJBICVQSYOIF-UHFFFAOYSA-N 0.000 description 1
- WTOFYLAWDLQMBZ-UHFFFAOYSA-N 2-azaniumyl-3-thiophen-2-ylpropanoate Chemical compound OC(=O)C(N)CC1=CC=CS1 WTOFYLAWDLQMBZ-UHFFFAOYSA-N 0.000 description 1
- XDOLZJYETYVRKV-UHFFFAOYSA-N 7-Aminoheptanoic acid Chemical compound NCCCCCCC(O)=O XDOLZJYETYVRKV-UHFFFAOYSA-N 0.000 description 1
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
- 241000766754 Agra Species 0.000 description 1
- 101710141722 Arylsulfatase Proteins 0.000 description 1
- 208000032116 Autoimmune Experimental Encephalomyelitis Diseases 0.000 description 1
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
- 241000699800 Cricetinae Species 0.000 description 1
- 229930105110 Cyclosporin A Natural products 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 1
- 108020004414 DNA Proteins 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- 108010076282 Factor IX Proteins 0.000 description 1
- 206010016077 Factor IX deficiency Diseases 0.000 description 1
- 108010014173 Factor X Proteins 0.000 description 1
- 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 1
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 208000028782 Hereditary disease Diseases 0.000 description 1
- 241000725303 Human immunodeficiency virus Species 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 206010062016 Immunosuppression Diseases 0.000 description 1
- 208000026350 Inborn Genetic disease Diseases 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- ZGUNAGUHMKGQNY-ZETCQYMHSA-N L-alpha-phenylglycine zwitterion Chemical compound OC(=O)[C@@H](N)C1=CC=CC=C1 ZGUNAGUHMKGQNY-ZETCQYMHSA-N 0.000 description 1
- 150000008575 L-amino acids Chemical class 0.000 description 1
- LRQKBLKVPFOOQJ-YFKPBYRVSA-N L-norleucine Chemical compound CCCC[C@H]([NH3+])C([O-])=O LRQKBLKVPFOOQJ-YFKPBYRVSA-N 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- DZLNHFMRPBPULJ-VKHMYHEASA-N L-thioproline Chemical compound OC(=O)[C@@H]1CSCN1 DZLNHFMRPBPULJ-VKHMYHEASA-N 0.000 description 1
- 102100037611 Lysophospholipase Human genes 0.000 description 1
- 108700018351 Major Histocompatibility Complex Proteins 0.000 description 1
- 229930195725 Mannitol Natural products 0.000 description 1
- 208000024556 Mendelian disease Diseases 0.000 description 1
- 239000004909 Moisturizer Substances 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 108020004485 Nonsense Codon Proteins 0.000 description 1
- 208000001388 Opportunistic Infections Diseases 0.000 description 1
- PEMUHKUIQHFMTH-UHFFFAOYSA-N P-Bromo-DL-phenylalanine Chemical compound OC(=O)C(N)CC1=CC=C(Br)C=C1 PEMUHKUIQHFMTH-UHFFFAOYSA-N 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 241000219098 Parthenocissus Species 0.000 description 1
- 108010058864 Phospholipases A2 Proteins 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 241000125945 Protoparvovirus Species 0.000 description 1
- 208000010378 Pulmonary Embolism Diseases 0.000 description 1
- 206010037437 Pulmonary thrombosis Diseases 0.000 description 1
- 208000035977 Rare disease Diseases 0.000 description 1
- 108020004511 Recombinant DNA Proteins 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
- 230000006044 T cell activation Effects 0.000 description 1
- 230000017274 T cell anergy Effects 0.000 description 1
- 208000024770 Thyroid neoplasm Diseases 0.000 description 1
- 206010052779 Transplant rejections Diseases 0.000 description 1
- HDTRYLNUVZCQOY-WSWWMNSNSA-N Trehalose Natural products O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-WSWWMNSNSA-N 0.000 description 1
- YZCKVEUIGOORGS-NJFSPNSNSA-N Tritium Chemical compound [3H] YZCKVEUIGOORGS-NJFSPNSNSA-N 0.000 description 1
- 208000037386 Typhoid Diseases 0.000 description 1
- 208000027276 Von Willebrand disease Diseases 0.000 description 1
- 206010052428 Wound Diseases 0.000 description 1
- 210000001766 X chromosome Anatomy 0.000 description 1
- 230000005856 abnormality Effects 0.000 description 1
- 238000005299 abrasion Methods 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 206010000891 acute myocardial infarction Diseases 0.000 description 1
- 208000005298 acute pain Diseases 0.000 description 1
- 210000005006 adaptive immune system Anatomy 0.000 description 1
- 230000007815 allergy Effects 0.000 description 1
- HDTRYLNUVZCQOY-LIZSDCNHSA-N alpha,alpha-trehalose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-LIZSDCNHSA-N 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 238000011091 antibody purification Methods 0.000 description 1
- 230000007503 antigenic stimulation Effects 0.000 description 1
- 239000002246 antineoplastic agent Substances 0.000 description 1
- 230000006907 apoptotic process Effects 0.000 description 1
- 230000003190 augmentative effect Effects 0.000 description 1
- LMEKQMALGUDUQG-UHFFFAOYSA-N azathioprine Chemical compound CN1C=NC([N+]([O-])=O)=C1SC1=NC=NC2=C1NC=N2 LMEKQMALGUDUQG-UHFFFAOYSA-N 0.000 description 1
- 229960002170 azathioprine Drugs 0.000 description 1
- 239000003659 bee venom Substances 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- 229940000635 beta-alanine Drugs 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 230000005540 biological transmission Effects 0.000 description 1
- 238000009534 blood test Methods 0.000 description 1
- 230000037396 body weight Effects 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 239000000337 buffer salt Substances 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 230000001684 chronic effect Effects 0.000 description 1
- 230000001112 coagulating effect Effects 0.000 description 1
- 229940105774 coagulation factor ix Drugs 0.000 description 1
- 229940105778 coagulation factor viii Drugs 0.000 description 1
- 239000003246 corticosteroid Substances 0.000 description 1
- 229960001334 corticosteroids Drugs 0.000 description 1
- 230000004940 costimulation Effects 0.000 description 1
- 231100000433 cytotoxic Toxicity 0.000 description 1
- 229940127089 cytotoxic agent Drugs 0.000 description 1
- 230000001472 cytotoxic effect Effects 0.000 description 1
- 230000034994 death Effects 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000006735 deficit Effects 0.000 description 1
- 238000000586 desensitisation Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- 206010012601 diabetes mellitus Diseases 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
- 150000002016 disaccharides Chemical class 0.000 description 1
- 208000009190 disseminated intravascular coagulation Diseases 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 230000003828 downregulation Effects 0.000 description 1
- 230000000857 drug effect Effects 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 208000012997 experimental autoimmune encephalomyelitis Diseases 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 238000009093 first-line therapy Methods 0.000 description 1
- 238000000684 flow cytometry Methods 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 238000001476 gene delivery Methods 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 235000011187 glycerol Nutrition 0.000 description 1
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 1
- 150000004820 halides Chemical class 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 208000014951 hematologic disease Diseases 0.000 description 1
- 230000002008 hemorrhagic effect Effects 0.000 description 1
- 230000023597 hemostasis Effects 0.000 description 1
- 208000006454 hepatitis Diseases 0.000 description 1
- 231100000283 hepatitis Toxicity 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 229960002591 hydroxyproline Drugs 0.000 description 1
- 230000009610 hypersensitivity Effects 0.000 description 1
- 230000002519 immonomodulatory effect Effects 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 230000007233 immunological mechanism Effects 0.000 description 1
- 239000003018 immunosuppressive agent Substances 0.000 description 1
- 229940124589 immunosuppressive drug Drugs 0.000 description 1
- 238000002650 immunosuppressive therapy Methods 0.000 description 1
- 230000001024 immunotherapeutic effect Effects 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 238000002513 implantation Methods 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 239000012678 infectious agent Substances 0.000 description 1
- 208000027866 inflammatory disease Diseases 0.000 description 1
- 230000002757 inflammatory effect Effects 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- FZWBNHMXJMCXLU-BLAUPYHCSA-N isomaltotriose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1OC[C@@H]1[C@@H](O)[C@H](O)[C@@H](O)[C@@H](OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C=O)O1 FZWBNHMXJMCXLU-BLAUPYHCSA-N 0.000 description 1
- 125000001449 isopropyl group Chemical group [H]C([H])([H])C([H])(*)C([H])([H])[H] 0.000 description 1
- 210000003292 kidney cell Anatomy 0.000 description 1
- 239000004310 lactic acid Substances 0.000 description 1
- 235000014655 lactic acid Nutrition 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 239000006193 liquid solution Substances 0.000 description 1
- 239000006194 liquid suspension Substances 0.000 description 1
- 230000033001 locomotion Effects 0.000 description 1
- 230000001589 lymphoproliferative effect Effects 0.000 description 1
- 238000012792 lyophilization process Methods 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 235000010355 mannitol Nutrition 0.000 description 1
- 239000000594 mannitol Substances 0.000 description 1
- 230000003228 microsomal effect Effects 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 108091005601 modified peptides Proteins 0.000 description 1
- 230000001333 moisturizer Effects 0.000 description 1
- 230000003039 myelosuppressive effect Effects 0.000 description 1
- 210000005036 nerve Anatomy 0.000 description 1
- 230000003472 neutralizing effect Effects 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 125000004433 nitrogen atom Chemical group N* 0.000 description 1
- 230000037434 nonsense mutation Effects 0.000 description 1
- 231100000862 numbness Toxicity 0.000 description 1
- 239000006179 pH buffering agent Substances 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 239000002953 phosphate buffered saline Substances 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 238000002616 plasmapheresis Methods 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 235000015277 pork Nutrition 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- XOFYZVNMUHMLCC-ZPOLXVRWSA-N prednisone Chemical compound O=C1C=C[C@]2(C)[C@H]3C(=O)C[C@](C)([C@@](CC4)(O)C(=O)CO)[C@@H]4[C@@H]3CCC2=C1 XOFYZVNMUHMLCC-ZPOLXVRWSA-N 0.000 description 1
- 229960004618 prednisone Drugs 0.000 description 1
- 208000012113 pregnancy disease Diseases 0.000 description 1
- 238000002953 preparative HPLC Methods 0.000 description 1
- 230000008742 procoagulation Effects 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 108010012557 prothrombin complex concentrates Proteins 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 206010039073 rheumatoid arthritis Diseases 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 210000004872 soft tissue Anatomy 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 230000006641 stabilisation Effects 0.000 description 1
- 238000011105 stabilization Methods 0.000 description 1
- 150000003431 steroids Chemical class 0.000 description 1
- 230000004936 stimulating effect Effects 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 125000001424 substituent group Chemical group 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 239000000829 suppository Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 208000008732 thymoma Diseases 0.000 description 1
- 201000002510 thyroid cancer Diseases 0.000 description 1
- 230000003614 tolerogenic effect Effects 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 229910052722 tritium Inorganic materials 0.000 description 1
- 201000008297 typhoid fever Diseases 0.000 description 1
- 239000006200 vaporizer Substances 0.000 description 1
- 208000034280 venom allergy Diseases 0.000 description 1
- 244000052613 viral pathogen Species 0.000 description 1
- 230000003253 viricidal effect Effects 0.000 description 1
- 108010047303 von Willebrand Factor Proteins 0.000 description 1
- 208000012137 von Willebrand disease (hereditary or acquired) Diseases 0.000 description 1
- 102100036537 von Willebrand factor Human genes 0.000 description 1
- 229960001134 von willebrand factor Drugs 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/745—Blood coagulation or fibrinolysis factors
- C07K14/755—Factors VIII, e.g. factor VIII C (AHF), factor VIII Ag (VWF)
-
- 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
- A61K38/36—Blood coagulation or fibrinolysis factors
- A61K38/37—Factors VIII
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/06—Immunosuppressants, e.g. drugs for graft rejection
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
- A61P7/04—Antihaemorrhagics; Procoagulants; Haemostatic agents; Antifibrinolytic agents
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Hematology (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Pharmacology & Pharmacy (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Animal Behavior & Ethology (AREA)
- Immunology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Biophysics (AREA)
- Toxicology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Biochemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- General Chemical & Material Sciences (AREA)
- Transplantation (AREA)
- Diabetes (AREA)
- Epidemiology (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GBGB0723712.6A GB0723712D0 (en) | 2007-12-04 | 2007-12-04 | Peptides |
| PCT/GB2008/003996 WO2009071886A1 (en) | 2007-12-04 | 2008-12-03 | Fviii peptides and their use in tolerising haemophiliacs |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| EA201070681A1 EA201070681A1 (ru) | 2010-10-29 |
| EA019370B1 true EA019370B1 (ru) | 2014-03-31 |
Family
ID=38982965
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| EA201070681A EA019370B1 (ru) | 2007-12-04 | 2008-12-03 | Пептиды fviii и их применение для индукции толерантности у больных гемофилией |
Country Status (25)
| Country | Link |
|---|---|
| US (1) | US8445448B2 (enExample) |
| EP (1) | EP2227488B3 (enExample) |
| JP (2) | JP5501245B2 (enExample) |
| KR (1) | KR101519840B1 (enExample) |
| CN (2) | CN103709234B (enExample) |
| AU (1) | AU2008332968B2 (enExample) |
| BR (1) | BRPI0820143A2 (enExample) |
| CA (2) | CA3005013C (enExample) |
| CY (1) | CY1115168T1 (enExample) |
| DK (1) | DK2227488T6 (enExample) |
| EA (1) | EA019370B1 (enExample) |
| EC (1) | ECSP10010327A (enExample) |
| ES (1) | ES2458315T7 (enExample) |
| GB (1) | GB0723712D0 (enExample) |
| HR (1) | HRP20140344T4 (enExample) |
| IL (1) | IL205780A (enExample) |
| MX (1) | MX2010006084A (enExample) |
| MY (1) | MY150995A (enExample) |
| NZ (1) | NZ585217A (enExample) |
| PL (1) | PL2227488T6 (enExample) |
| PT (1) | PT2227488E (enExample) |
| SI (1) | SI2227488T1 (enExample) |
| UA (1) | UA101003C2 (enExample) |
| WO (1) | WO2009071886A1 (enExample) |
| ZA (1) | ZA201002997B (enExample) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2698392C2 (ru) * | 2008-06-24 | 2019-08-26 | Октафарма Аг | Способ очистки фактора свертывания крови viii |
Families Citing this family (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SI1311542T1 (sl) | 2000-08-21 | 2009-02-28 | Apitope Technology Bristol Ltd | Tolerogenski peptidi |
| GB0801513D0 (en) * | 2008-01-28 | 2008-03-05 | Circassia Ltd | Peptides from factor VIII |
| GB0908515D0 (en) * | 2009-05-18 | 2009-06-24 | Apitope Technology Bristol Ltd | Peptide |
| US20120135917A1 (en) * | 2009-06-16 | 2012-05-31 | Eisaku Yoshihara | Anti-Gram Negative Bacteria Agent |
| DK2632479T3 (en) * | 2010-10-27 | 2017-08-07 | Baxalta GmbH | FVIII PEPTIDES FOR IMMUNT TOLERANCE INDUCTION AND IMMUNODIAGNOSTICS |
| PL3453402T3 (pl) | 2012-01-12 | 2022-03-21 | Bioverativ Therapeutics Inc. | Zmniejszenie immunogenności przeciwko czynnikowi viii u osób poddawanych terapii czynnikiem viii |
| PL2917232T3 (pl) * | 2012-11-12 | 2017-09-29 | Apitope International Nv | Pochodzące od czynnika VIII peptydy do zastosowania w leczeniu hemofilii A |
| GB201314052D0 (en) | 2013-08-06 | 2013-09-18 | Apitope Int Nv | Peptides |
| WO2017096329A1 (en) | 2015-12-03 | 2017-06-08 | Juno Therapeutics, Inc. | Modified chimeric receptors and related compositions and methods |
| BR112019011198A2 (pt) | 2016-12-02 | 2019-12-17 | Bioverativ Therapeutics Inc | métodos de indução de tolerância imune a fatores de coagulação |
| US12077607B2 (en) * | 2021-09-23 | 2024-09-03 | University Of Utah Research Foundation | Functional and therapeutic effects of PAR4 cleavage by cathepsin G |
Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1990015615A1 (en) * | 1989-06-20 | 1990-12-27 | Scripps Clinic And Research Foundation | The phospholipid binding domain of factor viii |
| WO2002016410A2 (en) * | 2000-08-21 | 2002-02-28 | Apitope Technology (Bristol) Limited | Peptide selection method |
| WO2002060917A2 (en) * | 2000-12-01 | 2002-08-08 | Regents Of The University Of Minnesota | Method to treat hemophilia |
| WO2002098454A2 (en) * | 2001-05-31 | 2002-12-12 | D. Collen Research Foundation Vzw Onderwijsen Navorsing Campus Gasthuisberg K.U. Leuven | Recombinant molecules with reduced immunogenicity, methods and intermediates for obtaining them and their use in pharmaceutical compositions and diagnostic tools |
| WO2003087161A1 (en) * | 2002-04-18 | 2003-10-23 | Merck Patent Gmbh | Modified factor viii |
Family Cites Families (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| BR9806793A (pt) * | 1997-01-22 | 2000-05-16 | Univ Texas | Processos e composições de fator tissular para coagulação e tratamento de tumores. |
| AU2002233340B2 (en) * | 2001-02-19 | 2008-05-22 | Merck Patent Gmbh | Artificial fusion proteins with reduced immunogenicity |
| SI1729795T1 (sl) * | 2004-02-09 | 2016-04-29 | Human Genome Sciences, Inc. | Albuminski fuzijski proteini |
| WO2006003183A1 (de) | 2004-07-02 | 2006-01-12 | Alois Jungbauer | Peptide zur blockierung von fviii-inhibitoren |
| IL229645A0 (en) * | 2013-11-26 | 2014-03-31 | Omrix Biopharmaceuticals Ltd | A dry bandage containing thrombin and pectin |
-
2007
- 2007-12-04 GB GBGB0723712.6A patent/GB0723712D0/en not_active Ceased
-
2008
- 2008-03-12 UA UAA201008194A patent/UA101003C2/uk unknown
- 2008-12-03 SI SI200831186T patent/SI2227488T1/sl unknown
- 2008-12-03 CN CN201310392152.6A patent/CN103709234B/zh not_active Expired - Fee Related
- 2008-12-03 NZ NZ585217A patent/NZ585217A/xx not_active IP Right Cessation
- 2008-12-03 EA EA201070681A patent/EA019370B1/ru not_active IP Right Cessation
- 2008-12-03 KR KR1020107011743A patent/KR101519840B1/ko not_active Expired - Fee Related
- 2008-12-03 US US12/746,141 patent/US8445448B2/en not_active Expired - Fee Related
- 2008-12-03 HR HRP20140344TT patent/HRP20140344T4/hr unknown
- 2008-12-03 AU AU2008332968A patent/AU2008332968B2/en not_active Ceased
- 2008-12-03 PT PT88557723T patent/PT2227488E/pt unknown
- 2008-12-03 ES ES08855772.3T patent/ES2458315T7/es active Active
- 2008-12-03 PL PL08855772T patent/PL2227488T6/pl unknown
- 2008-12-03 CN CN200880119313.1A patent/CN101889024B/zh not_active Expired - Fee Related
- 2008-12-03 CA CA3005013A patent/CA3005013C/en active Active
- 2008-12-03 DK DK08855772.3T patent/DK2227488T6/en active
- 2008-12-03 WO PCT/GB2008/003996 patent/WO2009071886A1/en not_active Ceased
- 2008-12-03 EP EP08855772.3A patent/EP2227488B3/en active Active
- 2008-12-03 JP JP2010536523A patent/JP5501245B2/ja active Active
- 2008-12-03 MY MYPI20102567 patent/MY150995A/en unknown
- 2008-12-03 CA CA2707559A patent/CA2707559C/en active Active
- 2008-12-03 MX MX2010006084A patent/MX2010006084A/es active IP Right Grant
- 2008-12-03 BR BRPI0820143 patent/BRPI0820143A2/pt not_active Application Discontinuation
-
2010
- 2010-04-29 ZA ZA2010/02997A patent/ZA201002997B/en unknown
- 2010-05-13 IL IL205780A patent/IL205780A/en active IP Right Grant
- 2010-07-02 EC EC2010010327A patent/ECSP10010327A/es unknown
-
2014
- 2014-02-10 JP JP2014023217A patent/JP6063402B2/ja not_active Expired - Fee Related
- 2014-04-15 CY CY20141100281T patent/CY1115168T1/el unknown
Patent Citations (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1990015615A1 (en) * | 1989-06-20 | 1990-12-27 | Scripps Clinic And Research Foundation | The phospholipid binding domain of factor viii |
| WO2002016410A2 (en) * | 2000-08-21 | 2002-02-28 | Apitope Technology (Bristol) Limited | Peptide selection method |
| WO2002060917A2 (en) * | 2000-12-01 | 2002-08-08 | Regents Of The University Of Minnesota | Method to treat hemophilia |
| WO2002098454A2 (en) * | 2001-05-31 | 2002-12-12 | D. Collen Research Foundation Vzw Onderwijsen Navorsing Campus Gasthuisberg K.U. Leuven | Recombinant molecules with reduced immunogenicity, methods and intermediates for obtaining them and their use in pharmaceutical compositions and diagnostic tools |
| WO2003087161A1 (en) * | 2002-04-18 | 2003-10-23 | Merck Patent Gmbh | Modified factor viii |
Non-Patent Citations (2)
| Title |
|---|
| JONES T. D. ET AL.: "Identification and removal of a promiscuous CD4+ T cell epitope from the C1 domain of factor VIII'', JOURNAL OF THROMBOSIS AND HAEMOSTASIS: JTH MAY 2005, vol. 3, no. 5, May 2005 (2005-05), pages 991-1000, XP002518538, ISSN: 1538-7933, table 1 * |
| SUGIHARA T. ET AL.: "IDENTIFICATION OF PLASMA ANTIBODY EPITOPES AND GENE ABNORMALITIES IN JAPANESE HEMOPHILIA A PATIENTS WITH FACTOR VIII INHIBITOR", NAGOYA JOURNAL OF MEDICAL SCIENCE, NAGOYA DAIGAKU IGAKUBU, NAGOYA, JP, vol. 63, no. 1/02, 1 May 2000 (2000-05-01), pages 25-39, XP008014431, ISSN: 0027-7622, table 2 * |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| RU2698392C2 (ru) * | 2008-06-24 | 2019-08-26 | Октафарма Аг | Способ очистки фактора свертывания крови viii |
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| EA019370B1 (ru) | Пептиды fviii и их применение для индукции толерантности у больных гемофилией | |
| US20210346476A1 (en) | Modified FVIII Apitope Peptides | |
| CA2762020C (en) | Mhc-ii-binding fviii peptides | |
| AU2014200237B2 (en) | FVIII peptides and their use in tolerising haemophiliacs | |
| HK1172240B (en) | Fviii-derived peptides and their use in tolerising haemophiliacs | |
| HK1172240A (en) | Fviii-derived peptides and their use in tolerising haemophiliacs | |
| HK1144292B (en) | Fviii peptides and their use in tolerising haemophiliacs | |
| HK1209138B (en) | Factor viii-derived peptides for use in the treatment of haemophilia a | |
| HK1173358B (en) | Fviii-derived peptides |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MM4A | Lapse of a eurasian patent due to non-payment of renewal fees within the time limit in the following designated state(s) |
Designated state(s): AM AZ BY KZ KG MD TJ TM |
|
| MM4A | Lapse of a eurasian patent due to non-payment of renewal fees within the time limit in the following designated state(s) |
Designated state(s): RU |