ES2842105T3 - Polipéptidos estables que se unen a C5 de complemento humano - Google Patents
Polipéptidos estables que se unen a C5 de complemento humano Download PDFInfo
- Publication number
- ES2842105T3 ES2842105T3 ES14765883T ES14765883T ES2842105T3 ES 2842105 T3 ES2842105 T3 ES 2842105T3 ES 14765883 T ES14765883 T ES 14765883T ES 14765883 T ES14765883 T ES 14765883T ES 2842105 T3 ES2842105 T3 ES 2842105T3
- Authority
- ES
- Spain
- Prior art keywords
- seq
- binding
- polypeptide
- amino acid
- acid sequence
- 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 abstract description 124
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 122
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 121
- 101000941598 Homo sapiens Complement C5 Proteins 0.000 title description 13
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract description 54
- 230000000295 complement effect Effects 0.000 claims abstract description 11
- 150000001875 compounds Chemical class 0.000 claims description 76
- 238000000034 method Methods 0.000 claims description 15
- 102000009027 Albumins Human genes 0.000 claims description 14
- 108010088751 Albumins Proteins 0.000 claims description 14
- 150000001413 amino acids Chemical class 0.000 claims description 7
- 201000010099 disease Diseases 0.000 claims description 7
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 7
- 208000000733 Paroxysmal Hemoglobinuria Diseases 0.000 claims description 6
- 102100036050 Phosphatidylinositol N-acetylglucosaminyltransferase subunit A Human genes 0.000 claims description 6
- 201000003045 paroxysmal nocturnal hemoglobinuria Diseases 0.000 claims description 6
- 238000011282 treatment Methods 0.000 claims description 6
- 208000023275 Autoimmune disease Diseases 0.000 claims description 4
- 108091006027 G proteins Proteins 0.000 claims description 4
- 102000030782 GTP binding Human genes 0.000 claims description 4
- 108091000058 GTP-Binding Proteins 0.000 claims description 4
- 230000006378 damage Effects 0.000 claims description 4
- 208000030533 eye disease Diseases 0.000 claims description 3
- 208000014951 hematologic disease Diseases 0.000 claims description 3
- 238000011321 prophylaxis Methods 0.000 claims description 3
- 238000002560 therapeutic procedure Methods 0.000 claims description 3
- 208000024172 Cardiovascular disease Diseases 0.000 claims description 2
- 208000035473 Communicable disease Diseases 0.000 claims description 2
- 208000019693 Lung disease Diseases 0.000 claims description 2
- 208000027418 Wounds and injury Diseases 0.000 claims description 2
- 208000026935 allergic disease Diseases 0.000 claims description 2
- 208000027866 inflammatory disease Diseases 0.000 claims description 2
- 208000014674 injury Diseases 0.000 claims description 2
- 208000017169 kidney disease Diseases 0.000 claims description 2
- 208000015122 neurodegenerative disease Diseases 0.000 claims description 2
- 238000006467 substitution reaction Methods 0.000 description 37
- 108090000623 proteins and genes Proteins 0.000 description 19
- 102000004169 proteins and genes Human genes 0.000 description 18
- 238000013112 stability test Methods 0.000 description 18
- 235000018102 proteins Nutrition 0.000 description 17
- 239000000872 buffer Substances 0.000 description 14
- 238000004007 reversed phase HPLC Methods 0.000 description 14
- 239000000499 gel Substances 0.000 description 13
- 102100031506 Complement C5 Human genes 0.000 description 12
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 12
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 11
- 210000004027 cell Anatomy 0.000 description 11
- 102220097833 rs876660426 Human genes 0.000 description 10
- 101100440311 Homo sapiens C5 gene Proteins 0.000 description 9
- 125000000539 amino acid group Chemical group 0.000 description 8
- 238000003776 cleavage reaction Methods 0.000 description 8
- 230000024203 complement activation Effects 0.000 description 8
- 102200016465 rs104894275 Human genes 0.000 description 8
- 102200029475 rs200313585 Human genes 0.000 description 8
- 239000000523 sample Substances 0.000 description 8
- 230000007017 scission Effects 0.000 description 8
- 102000008100 Human Serum Albumin Human genes 0.000 description 7
- 108091006905 Human Serum Albumin Proteins 0.000 description 7
- 230000004154 complement system Effects 0.000 description 7
- 230000004048 modification Effects 0.000 description 7
- 238000012986 modification Methods 0.000 description 7
- 230000037361 pathway Effects 0.000 description 7
- 238000001228 spectrum Methods 0.000 description 7
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 6
- 230000004071 biological effect Effects 0.000 description 6
- 230000005764 inhibitory process Effects 0.000 description 6
- 239000011780 sodium chloride Substances 0.000 description 6
- 108700012439 CA9 Proteins 0.000 description 5
- 102100024423 Carbonic anhydrase 9 Human genes 0.000 description 5
- 206010018910 Haemolysis Diseases 0.000 description 5
- 101001012157 Homo sapiens Receptor tyrosine-protein kinase erbB-2 Proteins 0.000 description 5
- 102100026120 IgG receptor FcRn large subunit p51 Human genes 0.000 description 5
- 102100026547 Platelet-derived growth factor receptor beta Human genes 0.000 description 5
- 101710164680 Platelet-derived growth factor receptor beta Proteins 0.000 description 5
- 102100030086 Receptor tyrosine-protein kinase erbB-2 Human genes 0.000 description 5
- 238000007792 addition Methods 0.000 description 5
- 238000006243 chemical reaction Methods 0.000 description 5
- 229960002224 eculizumab Drugs 0.000 description 5
- 239000002953 phosphate buffered saline Substances 0.000 description 5
- 108010028773 Complement C5 Proteins 0.000 description 4
- 108010034753 Complement Membrane Attack Complex Proteins 0.000 description 4
- 102000000989 Complement System Proteins Human genes 0.000 description 4
- 101710177940 IgG receptor FcRn large subunit p51 Proteins 0.000 description 4
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 4
- 230000033228 biological regulation Effects 0.000 description 4
- 230000008878 coupling Effects 0.000 description 4
- 238000010168 coupling process Methods 0.000 description 4
- 238000005859 coupling reaction Methods 0.000 description 4
- 238000011156 evaluation Methods 0.000 description 4
- 239000012634 fragment Substances 0.000 description 4
- 230000006870 function Effects 0.000 description 4
- 230000008588 hemolysis Effects 0.000 description 4
- 238000011534 incubation Methods 0.000 description 4
- JJWLVOIRVHMVIS-UHFFFAOYSA-N isopropylamine Chemical compound CC(C)N JJWLVOIRVHMVIS-UHFFFAOYSA-N 0.000 description 4
- 239000003446 ligand Substances 0.000 description 4
- 125000005647 linker group Chemical group 0.000 description 4
- 244000052769 pathogen Species 0.000 description 4
- 210000002966 serum Anatomy 0.000 description 4
- 201000000596 systemic lupus erythematosus Diseases 0.000 description 4
- 230000008685 targeting Effects 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- 108010069112 Complement System Proteins Proteins 0.000 description 3
- 241000588724 Escherichia coli Species 0.000 description 3
- 102220470986 Histone deacetylase 8_S39E_mutation Human genes 0.000 description 3
- 102220597878 Ketimine reductase mu-crystallin_D36R_mutation Human genes 0.000 description 3
- 206010049567 Miller Fisher syndrome Diseases 0.000 description 3
- 241001494479 Pecora Species 0.000 description 3
- 241000194017 Streptococcus Species 0.000 description 3
- 230000009471 action Effects 0.000 description 3
- 230000004913 activation Effects 0.000 description 3
- 150000001412 amines Chemical class 0.000 description 3
- 238000003556 assay Methods 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 230000000903 blocking effect Effects 0.000 description 3
- 239000003153 chemical reaction reagent Substances 0.000 description 3
- 238000001142 circular dichroism spectrum Methods 0.000 description 3
- 210000003743 erythrocyte Anatomy 0.000 description 3
- 239000003112 inhibitor Substances 0.000 description 3
- 230000002401 inhibitory effect Effects 0.000 description 3
- 230000003993 interaction Effects 0.000 description 3
- 238000004519 manufacturing process Methods 0.000 description 3
- 230000035772 mutation Effects 0.000 description 3
- 239000013612 plasmid Substances 0.000 description 3
- 230000008569 process Effects 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 230000008929 regeneration Effects 0.000 description 3
- 238000011069 regeneration method Methods 0.000 description 3
- 206010039073 rheumatoid arthritis Diseases 0.000 description 3
- 238000012430 stability testing Methods 0.000 description 3
- 208000003343 Antiphospholipid Syndrome Diseases 0.000 description 2
- 208000035913 Atypical hemolytic uremic syndrome Diseases 0.000 description 2
- 241000283707 Capra Species 0.000 description 2
- 102100035432 Complement factor H Human genes 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 208000035895 Guillain-Barré syndrome Diseases 0.000 description 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
- 102000009112 Mannose-Binding Lectin Human genes 0.000 description 2
- 108010087870 Mannose-Binding Lectin Proteins 0.000 description 2
- 229920001213 Polysorbate 20 Polymers 0.000 description 2
- 208000034841 Thrombotic Microangiopathies Diseases 0.000 description 2
- 206010052779 Transplant rejections Diseases 0.000 description 2
- 102220469588 Voltage-dependent L-type calcium channel subunit beta-2_D60A_mutation Human genes 0.000 description 2
- 238000002835 absorbance Methods 0.000 description 2
- 206010064930 age-related macular degeneration Diseases 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 239000013068 control sample Substances 0.000 description 2
- 230000007123 defense Effects 0.000 description 2
- 230000008021 deposition Effects 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 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 2
- 238000002474 experimental method Methods 0.000 description 2
- 125000000524 functional group Chemical group 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 208000015181 infectious disease Diseases 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 210000003734 kidney Anatomy 0.000 description 2
- 208000002780 macular degeneration Diseases 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 210000000056 organ Anatomy 0.000 description 2
- 230000001717 pathogenic effect Effects 0.000 description 2
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 2
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 2
- 230000003389 potentiating effect Effects 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 230000006641 stabilisation Effects 0.000 description 2
- 238000011105 stabilization Methods 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- WROMPOXWARCANT-UHFFFAOYSA-N tfa trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F.OC(=O)C(F)(F)F WROMPOXWARCANT-UHFFFAOYSA-N 0.000 description 2
- 210000001519 tissue Anatomy 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 1
- UAIUNKRWKOVEES-UHFFFAOYSA-N 3,3',5,5'-tetramethylbenzidine Chemical compound CC1=C(N)C(C)=CC(C=2C=C(C)C(N)=C(C)C=2)=C1 UAIUNKRWKOVEES-UHFFFAOYSA-N 0.000 description 1
- QFVHZQCOUORWEI-UHFFFAOYSA-N 4-[(4-anilino-5-sulfonaphthalen-1-yl)diazenyl]-5-hydroxynaphthalene-2,7-disulfonic acid Chemical compound C=12C(O)=CC(S(O)(=O)=O)=CC2=CC(S(O)(=O)=O)=CC=1N=NC(C1=CC=CC(=C11)S(O)(=O)=O)=CC=C1NC1=CC=CC=C1 QFVHZQCOUORWEI-UHFFFAOYSA-N 0.000 description 1
- 108010089414 Anaphylatoxins Proteins 0.000 description 1
- 108091023037 Aptamer Proteins 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 208000019838 Blood disease Diseases 0.000 description 1
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 108010053085 Complement Factor H Proteins 0.000 description 1
- 229940124073 Complement inhibitor Drugs 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 238000001712 DNA sequencing Methods 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 108010010803 Gelatin Proteins 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
- 239000007995 HEPES buffer Substances 0.000 description 1
- 208000032759 Hemolytic-Uremic Syndrome Diseases 0.000 description 1
- 206010020608 Hypercoagulation Diseases 0.000 description 1
- 108090001090 Lectins Proteins 0.000 description 1
- 102000004856 Lectins Human genes 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 206010057249 Phagocytosis Diseases 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- 108010079723 Shiga Toxin Proteins 0.000 description 1
- 208000037549 Shiga toxin-associated hemolytic uremic syndrome Diseases 0.000 description 1
- 208000021386 Sjogren Syndrome Diseases 0.000 description 1
- 108700005078 Synthetic Genes Proteins 0.000 description 1
- 201000009594 Systemic Scleroderma Diseases 0.000 description 1
- 206010042953 Systemic sclerosis Diseases 0.000 description 1
- 206010046851 Uveitis Diseases 0.000 description 1
- 206010047115 Vasculitis Diseases 0.000 description 1
- 239000008351 acetate buffer Substances 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 230000021917 activation of membrane attack complex Effects 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 230000033289 adaptive immune response Effects 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- VREFGVBLTWBCJP-UHFFFAOYSA-N alprazolam Chemical compound C12=CC(Cl)=CC=C2N2C(C)=NN=C2CN=C1C1=CC=CC=C1 VREFGVBLTWBCJP-UHFFFAOYSA-N 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 239000012491 analyte Substances 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 230000033115 angiogenesis Effects 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 238000005571 anion exchange chromatography Methods 0.000 description 1
- 230000001640 apoptogenic effect Effects 0.000 description 1
- 201000004339 autoimmune neuropathy Diseases 0.000 description 1
- HNYOPLTXPVRDBG-UHFFFAOYSA-N barbituric acid Chemical compound O=C1CC(=O)NC(=O)N1 HNYOPLTXPVRDBG-UHFFFAOYSA-N 0.000 description 1
- OWMVSZAMULFTJU-UHFFFAOYSA-N bis-tris Chemical compound OCCN(CCO)C(CO)(CO)CO OWMVSZAMULFTJU-UHFFFAOYSA-N 0.000 description 1
- 210000001185 bone marrow Anatomy 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 238000011088 calibration curve Methods 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 210000003169 central nervous system Anatomy 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 238000005352 clarification Methods 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 239000004074 complement inhibitor Substances 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 201000001981 dermatomyositis Diseases 0.000 description 1
- 238000010612 desalination reaction Methods 0.000 description 1
- 230000001627 detrimental effect Effects 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- UQLDLKMNUJERMK-UHFFFAOYSA-L di(octadecanoyloxy)lead Chemical compound [Pb+2].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O UQLDLKMNUJERMK-UHFFFAOYSA-L 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 239000012149 elution buffer Substances 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 210000002216 heart Anatomy 0.000 description 1
- 208000018706 hematopoietic system disease Diseases 0.000 description 1
- 208000007475 hemolytic anemia Diseases 0.000 description 1
- 230000002949 hemolytic effect Effects 0.000 description 1
- 238000000589 high-performance liquid chromatography-mass spectrometry Methods 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 1
- 238000000265 homogenisation Methods 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 238000004191 hydrophobic interaction chromatography Methods 0.000 description 1
- 210000002865 immune cell Anatomy 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 230000037451 immune surveillance Effects 0.000 description 1
- 230000002480 immunoprotective effect Effects 0.000 description 1
- 230000004957 immunoregulator effect Effects 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 238000000099 in vitro assay Methods 0.000 description 1
- 210000005007 innate immune system Anatomy 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 1
- 229930027917 kanamycin Natural products 0.000 description 1
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 1
- 229960000318 kanamycin Drugs 0.000 description 1
- 229930182823 kanamycin A Natural products 0.000 description 1
- 239000002523 lectin Substances 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- 238000001823 molecular biology technique Methods 0.000 description 1
- 210000001616 monocyte Anatomy 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 206010028417 myasthenia gravis Diseases 0.000 description 1
- 230000001338 necrotic effect Effects 0.000 description 1
- 108010068617 neonatal Fc receptor Proteins 0.000 description 1
- 210000005036 nerve Anatomy 0.000 description 1
- 208000008795 neuromyelitis optica Diseases 0.000 description 1
- 230000003472 neutralizing effect Effects 0.000 description 1
- 210000000440 neutrophil Anatomy 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 230000014207 opsonization Effects 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 230000007310 pathophysiology Effects 0.000 description 1
- 201000001245 periodontitis Diseases 0.000 description 1
- 230000008782 phagocytosis Effects 0.000 description 1
- 108010025221 plasma protein Z Proteins 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 230000036515 potency Effects 0.000 description 1
- 230000000770 proinflammatory effect Effects 0.000 description 1
- 108020001580 protein domains Proteins 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000013207 serial dilution Methods 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 238000001542 size-exclusion chromatography Methods 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- RGHFKWPGWBFQLN-UHFFFAOYSA-M sodium;5,5-diethylpyrimidin-3-ide-2,4,6-trione Chemical compound [Na+].CCC1(CC)C([O-])=NC(=O)NC1=O RGHFKWPGWBFQLN-UHFFFAOYSA-M 0.000 description 1
- 229940055944 soliris Drugs 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 210000000130 stem cell Anatomy 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 208000011580 syndromic disease Diseases 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 201000005665 thrombophilia Diseases 0.000 description 1
- 230000017423 tissue regeneration Effects 0.000 description 1
- 230000001052 transient effect Effects 0.000 description 1
- 238000002054 transplantation Methods 0.000 description 1
- 230000004614 tumor growth Effects 0.000 description 1
- 230000029663 wound healing Effects 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P13/00—Drugs for disorders of the urinary system
- A61P13/02—Drugs for disorders of the urinary system of urine or of the urinary tract, e.g. urine acidifiers
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P13/00—Drugs for disorders of the urinary system
- A61P13/12—Drugs for disorders of the urinary system of the kidneys
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
-
- 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
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/08—Antiallergic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/315—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Streptococcus (G), e.g. Enterococci
-
- 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
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
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)
- Pharmacology & Pharmacy (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Gastroenterology & Hepatology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Zoology (AREA)
- Immunology (AREA)
- Toxicology (AREA)
- Epidemiology (AREA)
- Urology & Nephrology (AREA)
- Pulmonology (AREA)
- Cardiology (AREA)
- Transplantation (AREA)
- Communicable Diseases (AREA)
- Oncology (AREA)
- Pain & Pain Management (AREA)
- Rheumatology (AREA)
- Ophthalmology & Optometry (AREA)
- Biomedical Technology (AREA)
- Neurology (AREA)
- Neurosurgery (AREA)
- Dermatology (AREA)
- Heart & Thoracic Surgery (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| SE1350986 | 2013-08-28 | ||
| PCT/EP2014/068282 WO2015028558A1 (en) | 2013-08-28 | 2014-08-28 | Stable polypeptides binding to human complement c5 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2842105T3 true ES2842105T3 (es) | 2021-07-12 |
Family
ID=51539238
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES14765883T Active ES2842105T3 (es) | 2013-08-28 | 2014-08-28 | Polipéptidos estables que se unen a C5 de complemento humano |
Country Status (29)
| Country | Link |
|---|---|
| US (1) | US9994626B2 (enExample) |
| EP (2) | EP3811961B1 (enExample) |
| JP (2) | JP6767865B2 (enExample) |
| KR (1) | KR102446636B1 (enExample) |
| CN (1) | CN105658228B (enExample) |
| AU (1) | AU2014314222B2 (enExample) |
| BR (1) | BR112016003142A2 (enExample) |
| CA (1) | CA2926976C (enExample) |
| CY (1) | CY1123732T1 (enExample) |
| DK (1) | DK3038633T3 (enExample) |
| ES (1) | ES2842105T3 (enExample) |
| HR (1) | HRP20210013T1 (enExample) |
| HU (1) | HUE052613T2 (enExample) |
| IL (1) | IL244218A (enExample) |
| LT (1) | LT3038633T (enExample) |
| MX (1) | MX382140B (enExample) |
| MY (1) | MY173804A (enExample) |
| NZ (1) | NZ718153A (enExample) |
| PH (1) | PH12016500371A1 (enExample) |
| PL (1) | PL3038633T3 (enExample) |
| PT (1) | PT3038633T (enExample) |
| RS (1) | RS61347B1 (enExample) |
| RU (2) | RU2733897C2 (enExample) |
| SA (1) | SA516370622B1 (enExample) |
| SG (1) | SG11201602679VA (enExample) |
| SI (1) | SI3038633T1 (enExample) |
| SM (1) | SMT202100006T1 (enExample) |
| UA (1) | UA117933C2 (enExample) |
| WO (1) | WO2015028558A1 (enExample) |
Families Citing this family (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| KR102149028B1 (ko) | 2012-02-20 | 2020-08-27 | 스위디쉬 오르펀 바이오비트럼 에이비 (피유비엘) | 인간 보체 c5에 결합하는 폴리펩티드 |
| HRP20210013T1 (hr) * | 2013-08-28 | 2021-04-02 | Ipc Research, Llc | Stabilni polipeptidi koji se vezuju za ljudski komplement c5 |
| TR201911279T4 (tr) * | 2013-08-28 | 2019-08-21 | Affibody Ab | Mutasyona uğramış bir yapı iskelesine sahip polipeptidlerin bağlanması. |
| UY37651A (es) * | 2017-03-31 | 2018-10-31 | Swedish Orphan Biovitrum Ab Publ | Polipéptido de unión al il-1r-i |
| CN111201246B (zh) | 2017-07-11 | 2023-10-27 | 亚力兄制药公司 | 结合补体成分c5或血清白蛋白的多肽及其融合蛋白 |
| MX2024005285A (es) * | 2021-11-01 | 2024-09-18 | Ipc Res Llc | Administracion de proteinas de union a c5. |
| WO2024227886A1 (en) | 2023-05-02 | 2024-11-07 | Mebrahtu Aman | Bispecific binding molecule |
Family Cites Families (23)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SE509359C2 (sv) | 1989-08-01 | 1999-01-18 | Cemu Bioteknik Ab | Användning av stabiliserade protein- eller peptidkonjugat för framställning av ett läkemedel |
| US6074642A (en) | 1994-05-02 | 2000-06-13 | Alexion Pharmaceuticals, Inc. | Use of antibodies specific to human complement component C5 for the treatment of glomerulonephritis |
| WO2002030985A2 (en) | 2000-10-10 | 2002-04-18 | Tanox, Inc. | Inhibition of complement c5 activation for the treatment and prevention of delayed xenograft or acute vascular rejection |
| AT410798B (de) * | 2001-01-26 | 2003-07-25 | Cistem Biotechnologies Gmbh | Verfahren zur identifizierung, isolierung und herstellung von antigenen gegen ein spezifisches pathogen |
| AU2002331601B2 (en) * | 2001-08-17 | 2006-04-13 | Tanox, Inc. | Complement pathway inhibitors binding to C5 and C5a without preventing the formation of C5b |
| ITMI20021527A1 (it) | 2002-07-11 | 2004-01-12 | Consiglio Nazionale Ricerche | Anticorpi anti componente c5 del complemento e loro uso |
| WO2005023866A2 (en) | 2003-09-10 | 2005-03-17 | Baxter International Inc. | Peptides that inhibit complement activation |
| SE0400274D0 (sv) * | 2004-02-09 | 2004-02-09 | Affibody Ab | New polypeptide |
| GB0518443D0 (en) * | 2005-09-09 | 2005-10-19 | Evolutec Ltd | Method of treating myasthenia gravis |
| AU2007223796B2 (en) * | 2006-03-08 | 2013-01-24 | Astellas Us Llc | Complement binding aptamers and anti-C5 agents useful in the treatment of ocular disorders |
| WO2007106585A1 (en) * | 2006-03-15 | 2007-09-20 | Alexion Pharmaceuticals, Inc. | Treatment of paroxysmal nocturnal hemoglobinuria patients by an inhibitor of complement |
| ES2346178T3 (es) | 2007-07-31 | 2015-11-02 | Affibody Ab | Nuevas composiciones, procedimientos y usos de unión de la albúmina |
| US9187535B2 (en) | 2007-12-19 | 2015-11-17 | Affibody Ab | Polypeptide derived from protein A and able to bind PDGF |
| EP2231860B1 (en) | 2007-12-19 | 2011-10-05 | Affibody AB | Polypeptide derived from protein a and able to bind pdgf |
| EP2072525A1 (en) | 2007-12-21 | 2009-06-24 | Affibody AB | New polypeptides having affinity for HER2 |
| BRPI0916668B1 (pt) | 2008-08-05 | 2021-12-28 | Novartis Ag | Anticorpo monoclonal isolado, composição farmacêutica, ácido nucleico isolado e vetor |
| EP2327725A1 (en) | 2009-11-26 | 2011-06-01 | InflaRx GmbH | Anti-C5a binding moieties with high blocking activity |
| ES2540114T3 (es) * | 2010-07-09 | 2015-07-08 | Affibody Ab | Polipéptidos |
| KR102149028B1 (ko) | 2012-02-20 | 2020-08-27 | 스위디쉬 오르펀 바이오비트럼 에이비 (피유비엘) | 인간 보체 c5에 결합하는 폴리펩티드 |
| JP5980104B2 (ja) | 2012-11-22 | 2016-08-31 | 三菱電機株式会社 | 液晶表示装置の製造方法および液晶表示装置の製造システム |
| US9957330B2 (en) | 2012-12-19 | 2018-05-01 | Affibody Ab | Polypeptides |
| TR201911279T4 (tr) * | 2013-08-28 | 2019-08-21 | Affibody Ab | Mutasyona uğramış bir yapı iskelesine sahip polipeptidlerin bağlanması. |
| HRP20210013T1 (hr) * | 2013-08-28 | 2021-04-02 | Ipc Research, Llc | Stabilni polipeptidi koji se vezuju za ljudski komplement c5 |
-
2014
- 2014-08-28 HR HRP20210013TT patent/HRP20210013T1/hr unknown
- 2014-08-28 SG SG11201602679VA patent/SG11201602679VA/en unknown
- 2014-08-28 ES ES14765883T patent/ES2842105T3/es active Active
- 2014-08-28 UA UAA201603124A patent/UA117933C2/uk unknown
- 2014-08-28 DK DK14765883.5T patent/DK3038633T3/da active
- 2014-08-28 KR KR1020167007498A patent/KR102446636B1/ko active Active
- 2014-08-28 HU HUE14765883A patent/HUE052613T2/hu unknown
- 2014-08-28 US US14/914,290 patent/US9994626B2/en active Active
- 2014-08-28 RS RS20210005A patent/RS61347B1/sr unknown
- 2014-08-28 EP EP20201264.7A patent/EP3811961B1/en active Active
- 2014-08-28 RU RU2016111115A patent/RU2733897C2/ru active
- 2014-08-28 SM SM20210006T patent/SMT202100006T1/it unknown
- 2014-08-28 RU RU2020128977A patent/RU2020128977A/ru unknown
- 2014-08-28 PL PL14765883T patent/PL3038633T3/pl unknown
- 2014-08-28 CN CN201480057470.XA patent/CN105658228B/zh active Active
- 2014-08-28 MY MYPI2016700583A patent/MY173804A/en unknown
- 2014-08-28 JP JP2016537298A patent/JP6767865B2/ja active Active
- 2014-08-28 LT LTEP14765883.5T patent/LT3038633T/lt unknown
- 2014-08-28 EP EP14765883.5A patent/EP3038633B1/en active Active
- 2014-08-28 CA CA2926976A patent/CA2926976C/en active Active
- 2014-08-28 PT PT147658835T patent/PT3038633T/pt unknown
- 2014-08-28 SI SI201431739T patent/SI3038633T1/sl unknown
- 2014-08-28 MX MX2016002397A patent/MX382140B/es unknown
- 2014-08-28 BR BR112016003142A patent/BR112016003142A2/pt not_active Application Discontinuation
- 2014-08-28 NZ NZ718153A patent/NZ718153A/en unknown
- 2014-08-28 WO PCT/EP2014/068282 patent/WO2015028558A1/en not_active Ceased
- 2014-08-28 AU AU2014314222A patent/AU2014314222B2/en active Active
-
2016
- 2016-02-22 IL IL244218A patent/IL244218A/en active IP Right Grant
- 2016-02-24 PH PH12016500371A patent/PH12016500371A1/en unknown
- 2016-02-25 SA SA516370622A patent/SA516370622B1/ar unknown
-
2020
- 2020-07-01 JP JP2020113725A patent/JP2020172505A/ja active Pending
- 2020-12-30 CY CY20201101229T patent/CY1123732T1/el unknown
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| ES2842105T3 (es) | Polipéptidos estables que se unen a C5 de complemento humano | |
| ES2306794T3 (es) | Moleculas de autoensamblaje. | |
| ES2715638T3 (es) | Polipéptidos que se unen al complemento humano C5 | |
| ES2346178T3 (es) | Nuevas composiciones, procedimientos y usos de unión de la albúmina | |
| ES3036522T3 (en) | Single chain variable fragment cd3 binding proteins | |
| ES2676403T3 (es) | Polipéptidos | |
| ES2275348T3 (es) | Polipeptidos del dominio 1 de beta2 gp1 terapeuticos y diagnosticos y metodos para usarlos. | |
| ES2742505T3 (es) | Polipéptidos de unión que tienen un andamio mutado | |
| ES2699753T3 (es) | Mimótopos peptídicos de claudina 18.2 y sus usos | |
| CN117279618A (zh) | 用于靶标分子的选择性耗竭的组合物和方法 | |
| ES2913162T3 (es) | Anticuerpo anti-Myl9 | |
| CN114044823A (zh) | 靶向钙粘蛋白17的纳米抗体及其应用 | |
| HK40050539B (en) | Stable polypeptides binding to human complement c5 | |
| HK40050539A (en) | Stable polypeptides binding to human complement c5 | |
| BR122023020080B1 (pt) | Polipeptídeos e compostos de ligação a c5 do complemento humano | |
| AU2023357539A1 (en) | Ultrastable antibody fragments with a novel disuldide bridge | |
| BR112020018563A2 (pt) | Anticorpos de domínio único que se ligam à neurotoxina do tétano | |
| HK1225656B (en) | Stable polypeptides binding to human complement c5 | |
| CN117007562A (zh) | 一种复合物及其用途 | |
| CA3268444A1 (en) | Ultrastable antibody fragments with a novel disuldide bridge | |
| BR112016003336B1 (pt) | Polipeptídeo; polipeptídeo de fusão; polinucleotídeo; população das variantes de polipeptídeo com base em um scaffold comum; população de polinucleotídeos; combinação de uma população de polipeptídeo; e métodos para selecionar um polipeptídeo desejado tendo uma afinidade com um alvo predeterminado a partir de uma população de polipeptídeos; isolar um polinucleotídeo codificando um polipeptídeo desejado tendo uma afinidade com um alvo predeterminado; identificar um polipeptídeo desejado tendo uma afinidade com um alvo predeterminado; e selecionar e identificar um polipeptídeo desejado tendo uma afinidade com um alvo predeterminado a partir de uma população de polipeptídeos |