JP2012511033A - 多価化合物の可逆阻害用マスキングリガンド - Google Patents
多価化合物の可逆阻害用マスキングリガンド Download PDFInfo
- Publication number
- JP2012511033A JP2012511033A JP2011539791A JP2011539791A JP2012511033A JP 2012511033 A JP2012511033 A JP 2012511033A JP 2011539791 A JP2011539791 A JP 2011539791A JP 2011539791 A JP2011539791 A JP 2011539791A JP 2012511033 A JP2012511033 A JP 2012511033A
- Authority
- JP
- Japan
- Prior art keywords
- antibody
- masking
- epitope
- ligand
- masking ligand
- 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.)
- Pending
Links
- 230000000873 masking effect Effects 0.000 title claims abstract description 101
- 239000003446 ligand Substances 0.000 title claims abstract description 93
- 150000001875 compounds Chemical class 0.000 title description 7
- 230000006965 reversible inhibition Effects 0.000 title 1
- 239000000427 antigen Substances 0.000 claims abstract description 83
- 102000036639 antigens Human genes 0.000 claims abstract description 82
- 108091007433 antigens Proteins 0.000 claims abstract description 82
- 238000000034 method Methods 0.000 claims abstract description 38
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 36
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 31
- 229920001184 polypeptide Polymers 0.000 claims abstract description 29
- 102000035195 Peptidases Human genes 0.000 claims description 33
- 108091005804 Peptidases Proteins 0.000 claims description 33
- 206010028980 Neoplasm Diseases 0.000 claims description 24
- 239000000203 mixture Substances 0.000 claims description 18
- 150000001413 amino acids Chemical class 0.000 claims description 12
- 230000035772 mutation Effects 0.000 claims description 12
- 102000005741 Metalloproteases Human genes 0.000 claims description 7
- 108010006035 Metalloproteases Proteins 0.000 claims description 7
- 239000011159 matrix material Substances 0.000 claims description 6
- 239000003937 drug carrier Substances 0.000 claims description 5
- 102400001368 Epidermal growth factor Human genes 0.000 claims description 3
- 101800003838 Epidermal growth factor Proteins 0.000 claims description 3
- 229940116977 epidermal growth factor Drugs 0.000 claims description 3
- VBEQCZHXXJYVRD-GACYYNSASA-N uroanthelone Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C(C)C)[C@@H](C)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CS)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O)C(C)C)[C@@H](C)CC)C1=CC=C(O)C=C1 VBEQCZHXXJYVRD-GACYYNSASA-N 0.000 claims description 3
- 208000025865 Ulcer Diseases 0.000 claims description 2
- 206010052428 Wound Diseases 0.000 claims description 2
- 208000027418 Wounds and injury Diseases 0.000 claims description 2
- 230000004481 post-translational protein modification Effects 0.000 claims description 2
- 231100000397 ulcer Toxicity 0.000 claims description 2
- 210000001519 tissue Anatomy 0.000 description 40
- 101100536808 Tetrahymena thermophila TGP1 gene Proteins 0.000 description 35
- 102000001301 EGF receptor Human genes 0.000 description 33
- 108060006698 EGF receptor Proteins 0.000 description 33
- 210000004027 cell Anatomy 0.000 description 32
- 229960005395 cetuximab Drugs 0.000 description 32
- 108090000623 proteins and genes Proteins 0.000 description 31
- 102000004169 proteins and genes Human genes 0.000 description 28
- 235000018102 proteins Nutrition 0.000 description 27
- 230000001225 therapeutic effect Effects 0.000 description 26
- 102100030412 Matrix metalloproteinase-9 Human genes 0.000 description 25
- 238000003776 cleavage reaction Methods 0.000 description 18
- 230000007017 scission Effects 0.000 description 18
- 201000011510 cancer Diseases 0.000 description 15
- 101000990902 Homo sapiens Matrix metalloproteinase-9 Proteins 0.000 description 14
- 239000004365 Protease Substances 0.000 description 13
- 201000010099 disease Diseases 0.000 description 13
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 13
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 12
- 229950008001 matuzumab Drugs 0.000 description 12
- 108010015302 Matrix metalloproteinase-9 Proteins 0.000 description 11
- 239000000872 buffer Substances 0.000 description 11
- 230000003993 interaction Effects 0.000 description 11
- 102000004190 Enzymes Human genes 0.000 description 10
- 108090000790 Enzymes Proteins 0.000 description 10
- 229940088598 enzyme Drugs 0.000 description 10
- 230000002797 proteolythic effect Effects 0.000 description 9
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 8
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 7
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical group OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 7
- 241000894007 species Species 0.000 description 7
- 102000002274 Matrix Metalloproteinases Human genes 0.000 description 6
- 108010000684 Matrix Metalloproteinases Proteins 0.000 description 6
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 6
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 6
- 208000015181 infectious disease Diseases 0.000 description 6
- 230000004048 modification Effects 0.000 description 6
- 238000012986 modification Methods 0.000 description 6
- 239000000126 substance Substances 0.000 description 6
- 210000004881 tumor cell Anatomy 0.000 description 6
- 230000002411 adverse Effects 0.000 description 5
- 235000001014 amino acid Nutrition 0.000 description 5
- 239000003795 chemical substances by application Substances 0.000 description 5
- 239000003814 drug Substances 0.000 description 5
- 238000001502 gel electrophoresis Methods 0.000 description 5
- 239000003550 marker Substances 0.000 description 5
- 230000006337 proteolytic cleavage Effects 0.000 description 5
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 5
- 102000005962 receptors Human genes 0.000 description 5
- 108020003175 receptors Proteins 0.000 description 5
- 230000002829 reductive effect Effects 0.000 description 5
- 239000011780 sodium chloride Substances 0.000 description 5
- 241000283707 Capra Species 0.000 description 4
- 238000012413 Fluorescence activated cell sorting analysis Methods 0.000 description 4
- 241000238631 Hexapoda Species 0.000 description 4
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 4
- 238000013459 approach Methods 0.000 description 4
- 239000011324 bead Substances 0.000 description 4
- 238000004113 cell culture Methods 0.000 description 4
- 230000007423 decrease Effects 0.000 description 4
- 238000010586 diagram Methods 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 230000006870 function Effects 0.000 description 4
- 238000004519 manufacturing process Methods 0.000 description 4
- 230000001575 pathological effect Effects 0.000 description 4
- 238000002360 preparation method Methods 0.000 description 4
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 description 4
- 230000004083 survival effect Effects 0.000 description 4
- 238000002560 therapeutic procedure Methods 0.000 description 4
- 206010006187 Breast cancer Diseases 0.000 description 3
- 208000026310 Breast neoplasm Diseases 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 3
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 3
- 206010027476 Metastases Diseases 0.000 description 3
- 241001465754 Metazoa Species 0.000 description 3
- 108010073929 Vascular Endothelial Growth Factor A Proteins 0.000 description 3
- 102000005789 Vascular Endothelial Growth Factors Human genes 0.000 description 3
- 108010019530 Vascular Endothelial Growth Factors Proteins 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 210000004899 c-terminal region Anatomy 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 230000000875 corresponding effect Effects 0.000 description 3
- 238000004132 cross linking Methods 0.000 description 3
- 238000013461 design Methods 0.000 description 3
- 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 3
- 229940079593 drug Drugs 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 239000012634 fragment Substances 0.000 description 3
- 238000003119 immunoblot Methods 0.000 description 3
- 229940127121 immunoconjugate Drugs 0.000 description 3
- 230000005764 inhibitory process Effects 0.000 description 3
- 239000002953 phosphate buffered saline Substances 0.000 description 3
- 210000002307 prostate Anatomy 0.000 description 3
- 230000000717 retained effect Effects 0.000 description 3
- 238000001542 size-exclusion chromatography Methods 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 230000008685 targeting Effects 0.000 description 3
- 230000001988 toxicity Effects 0.000 description 3
- 231100000419 toxicity Toxicity 0.000 description 3
- 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 2
- 108010022366 Carcinoembryonic Antigen Proteins 0.000 description 2
- 102100025475 Carcinoembryonic antigen-related cell adhesion molecule 5 Human genes 0.000 description 2
- 208000001333 Colorectal Neoplasms Diseases 0.000 description 2
- 238000011537 Coomassie blue staining Methods 0.000 description 2
- 230000004544 DNA amplification Effects 0.000 description 2
- 102100041003 Glutamate carboxypeptidase 2 Human genes 0.000 description 2
- 101000892862 Homo sapiens Glutamate carboxypeptidase 2 Proteins 0.000 description 2
- 101001012157 Homo sapiens Receptor tyrosine-protein kinase erbB-2 Proteins 0.000 description 2
- 108090000723 Insulin-Like Growth Factor I Proteins 0.000 description 2
- 241001529936 Murinae Species 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 206010033128 Ovarian cancer Diseases 0.000 description 2
- 206010061535 Ovarian neoplasm Diseases 0.000 description 2
- 102000003992 Peroxidases Human genes 0.000 description 2
- 239000002202 Polyethylene glycol Substances 0.000 description 2
- 108010072866 Prostate-Specific Antigen Proteins 0.000 description 2
- 102100038358 Prostate-specific antigen Human genes 0.000 description 2
- 102100030086 Receptor tyrosine-protein kinase erbB-2 Human genes 0.000 description 2
- 102000013275 Somatomedins Human genes 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 2
- 239000004480 active ingredient Substances 0.000 description 2
- 125000000539 amino acid group Chemical group 0.000 description 2
- 238000010171 animal model Methods 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 238000006664 bond formation reaction Methods 0.000 description 2
- 238000007385 chemical modification Methods 0.000 description 2
- 238000005520 cutting process 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
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 230000009401 metastasis Effects 0.000 description 2
- 239000013642 negative control Substances 0.000 description 2
- 208000002154 non-small cell lung carcinoma Diseases 0.000 description 2
- 208000008443 pancreatic carcinoma Diseases 0.000 description 2
- 108040007629 peroxidase activity proteins Proteins 0.000 description 2
- 230000000144 pharmacologic effect Effects 0.000 description 2
- 229920001223 polyethylene glycol Polymers 0.000 description 2
- 229920002704 polyhistidine Polymers 0.000 description 2
- 238000011533 pre-incubation Methods 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 230000009257 reactivity Effects 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 238000004062 sedimentation Methods 0.000 description 2
- 238000010561 standard procedure Methods 0.000 description 2
- 229940124597 therapeutic agent Drugs 0.000 description 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- 102000003390 tumor necrosis factor Human genes 0.000 description 2
- 241000701447 unidentified baculovirus Species 0.000 description 2
- MZOFCQQQCNRIBI-VMXHOPILSA-N (3s)-4-[[(2s)-1-[[(2s)-1-[[(1s)-1-carboxy-2-hydroxyethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-3-[[2-[[(2s)-2,6-diaminohexanoyl]amino]acetyl]amino]-4-oxobutanoic acid Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](N)CCCCN MZOFCQQQCNRIBI-VMXHOPILSA-N 0.000 description 1
- 125000003088 (fluoren-9-ylmethoxy)carbonyl group Chemical group 0.000 description 1
- RTQWWZBSTRGEAV-PKHIMPSTSA-N 2-[[(2s)-2-[bis(carboxymethyl)amino]-3-[4-(methylcarbamoylamino)phenyl]propyl]-[2-[bis(carboxymethyl)amino]propyl]amino]acetic acid Chemical compound CNC(=O)NC1=CC=C(C[C@@H](CN(CC(C)N(CC(O)=O)CC(O)=O)CC(O)=O)N(CC(O)=O)CC(O)=O)C=C1 RTQWWZBSTRGEAV-PKHIMPSTSA-N 0.000 description 1
- MJZJYWCQPMNPRM-UHFFFAOYSA-N 6,6-dimethyl-1-[3-(2,4,5-trichlorophenoxy)propoxy]-1,6-dihydro-1,3,5-triazine-2,4-diamine Chemical compound CC1(C)N=C(N)N=C(N)N1OCCCOC1=CC(Cl)=C(Cl)C=C1Cl MJZJYWCQPMNPRM-UHFFFAOYSA-N 0.000 description 1
- 102100026802 72 kDa type IV collagenase Human genes 0.000 description 1
- 101710151806 72 kDa type IV collagenase Proteins 0.000 description 1
- 102000030431 Asparaginyl endopeptidase Human genes 0.000 description 1
- 102100022005 B-lymphocyte antigen CD20 Human genes 0.000 description 1
- 206010005003 Bladder cancer Diseases 0.000 description 1
- 108010075254 C-Peptide Proteins 0.000 description 1
- 201000009030 Carcinoma Diseases 0.000 description 1
- 102000000844 Cell Surface Receptors Human genes 0.000 description 1
- 108010001857 Cell Surface Receptors Proteins 0.000 description 1
- 206010009944 Colon cancer Diseases 0.000 description 1
- 230000006820 DNA synthesis Effects 0.000 description 1
- ZNZYKNKBJPZETN-WELNAUFTSA-N Dialdehyde 11678 Chemical group N1C2=CC=CC=C2C2=C1[C@H](C[C@H](/C(=C/O)C(=O)OC)[C@@H](C=C)C=O)NCC2 ZNZYKNKBJPZETN-WELNAUFTSA-N 0.000 description 1
- 101800001224 Disintegrin Proteins 0.000 description 1
- 102000009109 Fc receptors Human genes 0.000 description 1
- 108010087819 Fc receptors Proteins 0.000 description 1
- 208000032612 Glial tumor Diseases 0.000 description 1
- 206010018338 Glioma Diseases 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101000897405 Homo sapiens B-lymphocyte antigen CD20 Proteins 0.000 description 1
- 101001034652 Homo sapiens Insulin-like growth factor 1 receptor Proteins 0.000 description 1
- 101001046683 Homo sapiens Integrin alpha-L Proteins 0.000 description 1
- 101001057504 Homo sapiens Interferon-stimulated gene 20 kDa protein Proteins 0.000 description 1
- 101001055144 Homo sapiens Interleukin-2 receptor subunit alpha Proteins 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 206010061218 Inflammation Diseases 0.000 description 1
- 102100022339 Integrin alpha-L Human genes 0.000 description 1
- 102100027268 Interferon-stimulated gene 20 kDa protein Human genes 0.000 description 1
- PEEHTFAAVSWFBL-UHFFFAOYSA-N Maleimide Chemical compound O=C1NC(=O)C=C1 PEEHTFAAVSWFBL-UHFFFAOYSA-N 0.000 description 1
- 102000000380 Matrix Metalloproteinase 1 Human genes 0.000 description 1
- 108010016113 Matrix Metalloproteinase 1 Proteins 0.000 description 1
- 241000579835 Merops Species 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- QPCDCPDFJACHGM-UHFFFAOYSA-N N,N-bis{2-[bis(carboxymethyl)amino]ethyl}glycine Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(=O)O)CCN(CC(O)=O)CC(O)=O QPCDCPDFJACHGM-UHFFFAOYSA-N 0.000 description 1
- 206010061309 Neoplasm progression Diseases 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 206010061902 Pancreatic neoplasm Diseases 0.000 description 1
- 102000001938 Plasminogen Activators Human genes 0.000 description 1
- 108010001014 Plasminogen Activators Proteins 0.000 description 1
- 206010060862 Prostate cancer Diseases 0.000 description 1
- 208000000236 Prostatic Neoplasms Diseases 0.000 description 1
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 description 1
- 241000700159 Rattus Species 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 102000012479 Serine Proteases Human genes 0.000 description 1
- 108010022999 Serine Proteases Proteins 0.000 description 1
- 241000256251 Spodoptera frugiperda Species 0.000 description 1
- 208000000102 Squamous Cell Carcinoma of Head and Neck Diseases 0.000 description 1
- 241000906446 Theraps Species 0.000 description 1
- 208000007097 Urinary Bladder Neoplasms Diseases 0.000 description 1
- 108091008605 VEGF receptors Proteins 0.000 description 1
- 102100033177 Vascular endothelial growth factor receptor 2 Human genes 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- XYVNHPYNSPGYLI-UUOKFMHZSA-N [(2r,3s,4r,5r)-5-(2-amino-6-oxo-3h-purin-9-yl)-4-hydroxy-2-(phosphonooxymethyl)oxolan-3-yl] dihydrogen phosphate Chemical compound C1=2NC(N)=NC(=O)C=2N=CN1[C@@H]1O[C@H](COP(O)(O)=O)[C@@H](OP(O)(O)=O)[C@H]1O XYVNHPYNSPGYLI-UUOKFMHZSA-N 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 230000010933 acylation Effects 0.000 description 1
- 238000005917 acylation reaction Methods 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 150000001299 aldehydes Chemical class 0.000 description 1
- 229960000548 alemtuzumab Drugs 0.000 description 1
- 125000005262 alkoxyamine group Chemical group 0.000 description 1
- 230000029936 alkylation Effects 0.000 description 1
- 238000005804 alkylation reaction Methods 0.000 description 1
- 230000009435 amidation Effects 0.000 description 1
- 238000007112 amidation reaction Methods 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 238000013103 analytical ultracentrifugation Methods 0.000 description 1
- 108010055066 asparaginylendopeptidase Proteins 0.000 description 1
- 230000001363 autoimmune Effects 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 229960004669 basiliximab Drugs 0.000 description 1
- 229960000397 bevacizumab Drugs 0.000 description 1
- 230000001588 bifunctional effect Effects 0.000 description 1
- 239000000090 biomarker Substances 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 230000006287 biotinylation Effects 0.000 description 1
- 238000007413 biotinylation Methods 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 230000005907 cancer growth Effects 0.000 description 1
- 230000009400 cancer invasion Effects 0.000 description 1
- 229940034605 capromab pendetide Drugs 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 230000004663 cell proliferation Effects 0.000 description 1
- 230000005754 cellular signaling Effects 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 238000010668 complexation reaction Methods 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 230000002596 correlated effect Effects 0.000 description 1
- 150000001944 cysteine derivatives Chemical class 0.000 description 1
- 229960002806 daclizumab Drugs 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 238000009792 diffusion process Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 239000002552 dosage form Substances 0.000 description 1
- 229960002224 eculizumab Drugs 0.000 description 1
- 229960000284 efalizumab Drugs 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 230000009881 electrostatic interaction Effects 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 108010087914 epidermal growth factor receptor VIII Proteins 0.000 description 1
- 208000021045 exocrine pancreatic carcinoma Diseases 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 210000005095 gastrointestinal system Anatomy 0.000 description 1
- 229960003297 gemtuzumab ozogamicin Drugs 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 230000036252 glycation Effects 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 201000010536 head and neck cancer Diseases 0.000 description 1
- 201000003911 head and neck carcinoma Diseases 0.000 description 1
- 208000014829 head and neck neoplasm Diseases 0.000 description 1
- 201000000459 head and neck squamous cell carcinoma Diseases 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 102000045648 human IGF1R Human genes 0.000 description 1
- 210000004408 hybridoma Anatomy 0.000 description 1
- 229960001001 ibritumomab tiuxetan Drugs 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 238000003364 immunohistochemistry Methods 0.000 description 1
- 230000007233 immunological mechanism Effects 0.000 description 1
- 238000007901 in situ hybridization Methods 0.000 description 1
- 238000000099 in vitro assay Methods 0.000 description 1
- 230000002458 infectious effect Effects 0.000 description 1
- 230000004968 inflammatory condition Effects 0.000 description 1
- 230000004054 inflammatory process Effects 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 150000002576 ketones Chemical class 0.000 description 1
- 231100000636 lethal dose Toxicity 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 230000003211 malignant effect Effects 0.000 description 1
- 208000015486 malignant pancreatic neoplasm Diseases 0.000 description 1
- 238000007726 management method Methods 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 238000002493 microarray Methods 0.000 description 1
- 238000000386 microscopy Methods 0.000 description 1
- 230000000394 mitotic effect Effects 0.000 description 1
- 238000003032 molecular docking Methods 0.000 description 1
- 230000004001 molecular interaction Effects 0.000 description 1
- 230000009456 molecular mechanism Effects 0.000 description 1
- 229960005027 natalizumab Drugs 0.000 description 1
- 230000009826 neoplastic cell growth Effects 0.000 description 1
- 230000003472 neutralizing effect Effects 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 231100000956 nontoxicity Toxicity 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 229960000470 omalizumab Drugs 0.000 description 1
- 238000011275 oncology therapy Methods 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 230000004768 organ dysfunction Effects 0.000 description 1
- 150000002923 oximes Chemical class 0.000 description 1
- 229960000402 palivizumab Drugs 0.000 description 1
- 201000002528 pancreatic cancer Diseases 0.000 description 1
- 201000008129 pancreatic ductal adenocarcinoma Diseases 0.000 description 1
- 229960001972 panitumumab Drugs 0.000 description 1
- 230000008506 pathogenesis Effects 0.000 description 1
- 230000006320 pegylation Effects 0.000 description 1
- 229940067082 pentetate Drugs 0.000 description 1
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 1
- 239000000816 peptidomimetic Substances 0.000 description 1
- 239000012466 permeate Substances 0.000 description 1
- 229960002087 pertuzumab Drugs 0.000 description 1
- 238000002823 phage display Methods 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 230000035479 physiological effects, processes and functions Effects 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 230000036470 plasma concentration Effects 0.000 description 1
- 229940127126 plasminogen activator Drugs 0.000 description 1
- 230000013823 prenylation Effects 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 229940002612 prodrug Drugs 0.000 description 1
- 239000000651 prodrug Substances 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- NGVDGCNFYWLIFO-UHFFFAOYSA-N pyridoxal 5'-phosphate Chemical compound CC1=NC=C(COP(O)(O)=O)C(C=O)=C1O NGVDGCNFYWLIFO-UHFFFAOYSA-N 0.000 description 1
- 235000007682 pyridoxal 5'-phosphate Nutrition 0.000 description 1
- 239000011589 pyridoxal 5'-phosphate Substances 0.000 description 1
- 229960003876 ranibizumab Drugs 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 229960004641 rituximab Drugs 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 238000005563 spheronization Methods 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 125000004354 sulfur functional group Chemical group 0.000 description 1
- 238000001356 surgical procedure Methods 0.000 description 1
- 208000011580 syndromic disease Diseases 0.000 description 1
- 230000002195 synergetic effect Effects 0.000 description 1
- 238000007910 systemic administration Methods 0.000 description 1
- 238000011191 terminal modification Methods 0.000 description 1
- 125000005931 tert-butyloxycarbonyl group Chemical group [H]C([H])([H])C(OC(*)=O)(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 231100001274 therapeutic index Toxicity 0.000 description 1
- 125000003396 thiol group Chemical group [H]S* 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 238000005891 transamination reaction Methods 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 229960000575 trastuzumab Drugs 0.000 description 1
- 230000005740 tumor formation Effects 0.000 description 1
- 230000005751 tumor progression Effects 0.000 description 1
- 208000029729 tumor suppressor gene on chromosome 11 Diseases 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 201000005112 urinary bladder cancer Diseases 0.000 description 1
- 229960003824 ustekinumab Drugs 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Images
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
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/71—Receptors; Cell surface antigens; Cell surface determinants for growth factors; for growth regulators
-
- 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
- A61P17/02—Drugs for dermatological disorders for treating wounds, ulcers, burns, scars, keloids, or the like
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2863—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against receptors for growth factors, growth regulators
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Immunology (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Pharmacology & Pharmacy (AREA)
- Cell Biology (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Toxicology (AREA)
- Veterinary Medicine (AREA)
- Dermatology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US12065708P | 2008-12-08 | 2008-12-08 | |
| US61/120,657 | 2008-12-08 | ||
| US14761109P | 2009-01-27 | 2009-01-27 | |
| US61/147,611 | 2009-01-27 | ||
| PCT/US2009/067119 WO2010077643A1 (en) | 2008-12-08 | 2009-12-08 | Masking ligands for reversible inhibition of multivalent compounds |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2012511033A true JP2012511033A (ja) | 2012-05-17 |
| JP2012511033A5 JP2012511033A5 (enExample) | 2013-02-14 |
Family
ID=42310107
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2011539791A Pending JP2012511033A (ja) | 2008-12-08 | 2009-12-08 | 多価化合物の可逆阻害用マスキングリガンド |
Country Status (4)
| Country | Link |
|---|---|
| US (1) | US20100189727A1 (enExample) |
| EP (1) | EP2356131A4 (enExample) |
| JP (1) | JP2012511033A (enExample) |
| WO (1) | WO2010077643A1 (enExample) |
Cited By (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2016520614A (ja) * | 2013-05-28 | 2016-07-14 | ディーシービー−ユーエスエー エルエルシーDcb−Usa Llc | タンパク質薬物の不活性化のための抗体ロッカー |
| JP2016538240A (ja) * | 2013-09-25 | 2016-12-08 | シトムクス セラピューティクス,インコーポレイティド | マトリックスメタロプロテイナーゼ基質及び他の切断可能部分並びにそれらの使用方法 |
| JP2018509182A (ja) * | 2015-03-13 | 2018-04-05 | サイトメックス セラピューティクス インコーポレイテッド | 抗pdl1抗体、活性化可能抗pdl1抗体、およびその使用方法 |
| JP2018520642A (ja) * | 2015-05-01 | 2018-08-02 | ジェネンテック, インコーポレイテッド | マスク抗cd3抗体及びその使用方法 |
| JP2020098195A (ja) * | 2013-01-04 | 2020-06-25 | シトムクス セラピューティクス,インコーポレイティド | 生体系におけるプロテアーゼ活性を検出するための組成物及び方法 |
| US11168144B2 (en) | 2017-06-01 | 2021-11-09 | Cytomx Therapeutics, Inc. | Activatable anti-PDL1 antibodies, and methods of use thereof |
| JP2022065174A (ja) * | 2013-07-25 | 2022-04-26 | シトムクス セラピューティクス,インコーポレイティド | 多重特異性抗体、多重特異性活性化可能抗体、及びそれらの使用方法 |
Families Citing this family (63)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20090304719A1 (en) | 2007-08-22 | 2009-12-10 | Patrick Daugherty | Activatable binding polypeptides and methods of identification and use thereof |
| US8895702B2 (en) | 2008-12-08 | 2014-11-25 | City Of Hope | Development of masked therapeutic antibodies to limit off-target effects; application to anti-EGFR antibodies |
| US20110178279A1 (en) * | 2009-08-03 | 2011-07-21 | Williams John C | Development of masked therapeutic antibodies to limit off-target effects: application to anti-egfr antibodies |
| CA2749339A1 (en) | 2009-01-12 | 2010-07-15 | Cytomx Therapeutics, Llc | Modified antibody compositions, methods of making and using thereof |
| RU2011138951A (ru) | 2009-02-23 | 2013-03-27 | Сайтомкс Терапьютикс, Инк. | Пропротеины и способы их применения |
| AU2012228100B2 (en) * | 2011-03-17 | 2016-09-08 | The University Of Birmingham | Re-directed immunotherapy |
| KR101963230B1 (ko) * | 2011-12-26 | 2019-03-29 | 삼성전자주식회사 | 복수개의 단일 항체를 포함하는 단백질 복합체 |
| GB201203442D0 (en) | 2012-02-28 | 2012-04-11 | Univ Birmingham | Immunotherapeutic molecules and uses |
| IN2014MN02164A (enExample) * | 2012-04-27 | 2015-08-28 | Cytomx Therapeutics Inc | |
| KR101911438B1 (ko) | 2012-10-31 | 2018-10-24 | 삼성전자주식회사 | 이중 특이 항원 결합 단백질 복합체 및 이중 특이 항체의 제조 방법 |
| JP6133431B2 (ja) | 2012-11-24 | 2017-05-24 | ハンジョウ ディーエーシー バイオテック シーオー.,エルティディ.Hangzhou Dac Biotech Co.,Ltd. | 親水性連結体及び薬物分子と細胞結合分子との共役反応における親水性連結体の使用 |
| KR20160018579A (ko) | 2013-06-04 | 2016-02-17 | 싸이톰스 테라퓨틱스, 인크. | 활성화가능 항체를 접합하기 위한 조성물 및 방법 |
| US9540440B2 (en) | 2013-10-30 | 2017-01-10 | Cytomx Therapeutics, Inc. | Activatable antibodies that bind epidermal growth factor receptor and methods of use thereof |
| US9737623B2 (en) | 2013-12-11 | 2017-08-22 | Cytomx Therapeutics, Inc. | Antibodies that bind activatable antibodies and methods of use thereof |
| EP3736292B1 (en) | 2013-12-17 | 2024-05-08 | Genentech, Inc. | Anti-cd3 antibodies and methods of use |
| PT3122757T (pt) | 2014-02-28 | 2023-11-03 | Hangzhou Dac Biotech Co Ltd | Ligantes carregados e as suas utilizações em conjugação |
| BR112017001579A2 (pt) | 2014-07-25 | 2017-11-21 | Cytomx Therapeutics Inc | anticorpos anti-cd3, anticorpos anti-cd3 ativáveis, anticorpos anti-cd3 multiespecíficos, anticorpos anti-cd3 ativáveis multiespecíficos e métodos de uso dos mesmos |
| EA201790569A1 (ru) | 2014-09-12 | 2017-08-31 | Дженентек, Инк. | Антитела и иммуноконъюгаты против cll-1 |
| LT3221363T (lt) | 2014-11-21 | 2020-08-10 | Bristol-Myers Squibb Company | Antikūnai prieš cd73 ir jų panaudojimas |
| SG10202006538TA (en) | 2014-12-23 | 2020-08-28 | Bristol Myers Squibb Co | Antibodies to tigit |
| EP3932428A1 (en) | 2015-05-21 | 2022-01-05 | Harpoon Therapeutics, Inc. | Trispecific binding proteins and methods of use |
| JP6797137B2 (ja) | 2015-05-29 | 2020-12-09 | ブリストル−マイヤーズ スクイブ カンパニーBristol−Myers Squibb Company | Ox40に対する抗体およびその使用 |
| CN107847568B (zh) | 2015-06-16 | 2022-12-20 | 豪夫迈·罗氏有限公司 | 抗cll-1抗体和使用方法 |
| EP3313886A1 (en) | 2015-06-29 | 2018-05-02 | The Rockefeller University | Antibodies to cd40 with enhanced agonist activity |
| US11938193B2 (en) | 2016-01-08 | 2024-03-26 | Washington University | Compositions comprising chemerin and methods of use thereof |
| KR20230038311A (ko) | 2016-03-04 | 2023-03-17 | 브리스톨-마이어스 스큅 컴퍼니 | 항-cd73 항체와의 조합 요법 |
| IL263102B2 (en) | 2016-05-20 | 2023-11-01 | Harpoon Therapeutics Inc | A serum albumin-binding protein with a single site |
| US11623958B2 (en) | 2016-05-20 | 2023-04-11 | Harpoon Therapeutics, Inc. | Single chain variable fragment CD3 binding proteins |
| LT3461261T (lt) | 2016-05-20 | 2025-08-25 | Harpoon Therapeutics, Inc. | Vienos grandinės kintamo fragmento cd3 surišantys baltymai |
| WO2018093821A1 (en) | 2016-11-15 | 2018-05-24 | Genentech, Inc. | Dosing for treatment with anti-cd20/anti-cd3 bispecific antibodies |
| US10849973B2 (en) | 2016-11-23 | 2020-12-01 | Harpoon Therapeutics, Inc. | Prostate specific membrane antigen binding protein |
| KR20190087539A (ko) | 2016-11-23 | 2019-07-24 | 하푼 테라퓨틱스, 인크. | Psma 표적화 삼중특이성 단백질 및 사용 방법 |
| CN110036034A (zh) | 2016-12-09 | 2019-07-19 | 西雅图遗传学公司 | 卷曲螺旋掩蔽的二价抗体 |
| WO2018160754A2 (en) * | 2017-02-28 | 2018-09-07 | Harpoon Therapeutics, Inc. | Inducible monovalent antigen binding protein |
| TWI788340B (zh) | 2017-04-07 | 2023-01-01 | 美商必治妥美雅史谷比公司 | 抗icos促效劑抗體及其用途 |
| KR102376863B1 (ko) | 2017-05-12 | 2022-03-21 | 하푼 테라퓨틱스, 인크. | 메소텔린 결합 단백질 |
| US10730954B2 (en) | 2017-05-12 | 2020-08-04 | Harpoon Therapeutics, Inc. | MSLN targeting trispecific proteins and methods of use |
| EP3625253A4 (en) * | 2017-05-16 | 2021-03-24 | Scalmibio, Inc. | ACTIVABLE ANTIBODIES AND THEIR METHODS OF USE |
| KR20200015742A (ko) * | 2017-06-20 | 2020-02-12 | 더 보드 오브 리젠츠 오브 더 유니버시티 오브 텍사스 시스템 | 암 치료를 위한 인터페론 전구약물 |
| WO2019036433A2 (en) | 2017-08-16 | 2019-02-21 | Bristol-Myers Squibb Company | ANTIBODIES IN THE FORM OF PRODRUGS, PRODRUGS BASED THEREON, THEIR METHODS OF USE AND PREPARATION |
| IL315737A (en) | 2017-10-13 | 2024-11-01 | Harpoon Therapeutics Inc | B-cell maturation antigen-binding proteins |
| CN111630070B (zh) | 2017-10-13 | 2024-07-30 | 哈普恩治疗公司 | 三特异性蛋白质及使用方法 |
| BR112020007309A2 (pt) | 2017-10-14 | 2020-09-29 | Cytomx Therapeutics, Inc. | anticorpos, anticorpos ativáveis, anticorpos biespecíficos e anticorpos ativáveis biespecíficos e métodos de uso dos mesmos |
| KR102813744B1 (ko) | 2017-12-27 | 2025-05-28 | 브리스톨-마이어스 스큅 컴퍼니 | 항-cd40 항체 및 그의 용도 |
| WO2019136405A1 (en) * | 2018-01-05 | 2019-07-11 | City Of Hope | Multi-specific ligand binders |
| AR115360A1 (es) | 2018-02-08 | 2021-01-13 | Genentech Inc | Moléculas de unión al antígeno y métodos de uso |
| PE20210290A1 (es) | 2018-03-21 | 2021-02-11 | Five Prime Therapeutics Inc | ANTICUERPOS DE UNION A VISTA A pH ACIDO |
| AU2019271138A1 (en) | 2018-05-14 | 2021-01-07 | Harpoon Therapeutics, Inc. | Binding moiety for conditional activation of immunoglobulin molecules |
| BR112021000303A2 (pt) | 2018-07-11 | 2021-04-13 | Five Prime Therapeutics, Inc. | Anticorpos que se ligam a vista em ph ácido |
| WO2020061482A1 (en) | 2018-09-21 | 2020-03-26 | Harpoon Therapeutics, Inc. | Egfr binding proteins and methods of use |
| US10815311B2 (en) | 2018-09-25 | 2020-10-27 | Harpoon Therapeutics, Inc. | DLL3 binding proteins and methods of use |
| MY205758A (en) | 2018-11-16 | 2024-11-12 | Bristol Myers Squibb Co | Anti-nkg2a antibodies and uses thereof |
| US12478674B2 (en) | 2019-04-18 | 2025-11-25 | Bristol-Myers Squibb Company | Ipilimumab variants with enhanced specificity for binding at low pH |
| US20220251206A1 (en) | 2019-06-11 | 2022-08-11 | Bristol-Myers Squibb Company | Anti-ctla4 antibody prodruggable (probody) at a cdr position |
| AU2020350689A1 (en) | 2019-09-19 | 2022-03-31 | Bristol-Myers Squibb Company | Antibodies binding to VISTA at acidic pH |
| WO2021168303A1 (en) | 2020-02-21 | 2021-08-26 | Harpoon Therapeutics, Inc. | Flt3 binding proteins and methods of use |
| US20230140384A1 (en) | 2020-03-09 | 2023-05-04 | Bristol-Myers Squibb Company | Antibodies to cd40 with enhanced agonist activity |
| WO2021231732A1 (en) | 2020-05-15 | 2021-11-18 | Bristol-Myers Squibb Company | Antibodies to garp |
| JP7788447B2 (ja) | 2020-08-13 | 2025-12-18 | ブリストル-マイヤーズ スクイブ カンパニー | 目的の細胞を標的とするためのil-2の向け直し方法 |
| EP4240766A2 (en) | 2020-11-04 | 2023-09-13 | Genentech, Inc. | Subcutaneous dosing of anti-cd20/anti-cd3 bispecific antibodies |
| JP7402381B2 (ja) | 2020-11-04 | 2023-12-20 | ジェネンテック, インコーポレイテッド | 抗cd20/抗cd3二重特異性抗体による処置のための投与 |
| JP2023546368A (ja) | 2021-05-14 | 2023-11-02 | ジェネンテック, インコーポレイテッド | モスネツズマブおよびポラツズマブベドチンを用いたcd20陽性増殖性障害の処置のための方法 |
| EP4626919A1 (en) * | 2022-11-28 | 2025-10-08 | Zhejiang Shimai Pharmaceutical Co., Ltd. | Protease cleavable recombinant bispecific antibodies and compositions and uses thereof |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2005185281A (ja) * | 2003-12-04 | 2005-07-14 | Mbl Venture Capital Co Ltd | 細胞表面抗原に対する抗体取得とその抗原同定 |
| JP2005536987A (ja) * | 2002-04-01 | 2005-12-08 | ユーロ−セルティーク エス.エイ. | 抗原提示細胞標的化機構を含むエピトープ構築物 |
| JP2007524105A (ja) * | 2004-02-25 | 2007-08-23 | バイオエンハンスメンツ リミテッド | 結合物質 |
| JP2007527225A (ja) * | 2003-07-30 | 2007-09-27 | ユニバーシティ オブ ピッツバーグ オブ ザ コモンウェルス システム オブ ハイヤー エデュケイション | Epha2t−細胞エピトープアゴニストおよびその使用 |
Family Cites Families (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5306731A (en) * | 1985-06-14 | 1994-04-26 | Massachusetts Eye And Ear Infirmary | Method and products for treating the eye |
| US5585250A (en) * | 1993-08-20 | 1996-12-17 | The United States Of America As Represented By The Department Of Health & Human Services | Dampening of an immunodominant epitope of an antigen for use in plant, animal and human compositions and immunotherapies |
| US5861160A (en) * | 1995-06-07 | 1999-01-19 | Ambico, Inc. | Isospora suis sporozoite antigen |
| GB9622500D0 (en) * | 1996-10-29 | 1997-01-08 | Oxford Biomedica Ltd | Therapeutic gene |
| US7141392B2 (en) * | 2001-01-09 | 2006-11-28 | Queen Mary And Westfield College | Latent fusion protein |
| US20030134824A1 (en) * | 2001-11-12 | 2003-07-17 | Ronald Breslow | Beta-cyclodextrin dimers and phthalocyanines and uses thereof |
| US6680236B2 (en) * | 2002-01-11 | 2004-01-20 | Raytheon Company | Ion-implantation and shallow etching to produce effective edge termination in high-voltage heterojunction bipolar transistors |
| EP2316922B1 (en) * | 2002-05-24 | 2013-05-22 | Merck Sharp & Dohme Corp. | Neutralizing human anti-IGFR antibody |
| JP4351430B2 (ja) * | 2002-10-04 | 2009-10-28 | 財団法人癌研究会 | ナノ黒鉛構造体に結合能を有するペプチド |
| CN1548537B (zh) * | 2002-12-27 | 2010-05-05 | 深圳市源兴生物医药科技有限公司 | 疫苗制备方法和抗肿瘤疫苗 |
| US7338432B2 (en) * | 2003-11-17 | 2008-03-04 | Konstantin Valtchev | Urethral sling introducer and method of use |
| US7767792B2 (en) * | 2004-02-20 | 2010-08-03 | Ludwig Institute For Cancer Research Ltd. | Antibodies to EGF receptor epitope peptides |
| WO2006090813A1 (ja) * | 2005-02-25 | 2006-08-31 | National University Corporation Hokkaido University | 腫瘍組織で選択的に分解性を示す血中滞留性素子 |
-
2009
- 2009-12-08 WO PCT/US2009/067119 patent/WO2010077643A1/en not_active Ceased
- 2009-12-08 JP JP2011539791A patent/JP2012511033A/ja active Pending
- 2009-12-08 US US12/633,102 patent/US20100189727A1/en not_active Abandoned
- 2009-12-08 EP EP09836702A patent/EP2356131A4/en not_active Withdrawn
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2005536987A (ja) * | 2002-04-01 | 2005-12-08 | ユーロ−セルティーク エス.エイ. | 抗原提示細胞標的化機構を含むエピトープ構築物 |
| JP2007527225A (ja) * | 2003-07-30 | 2007-09-27 | ユニバーシティ オブ ピッツバーグ オブ ザ コモンウェルス システム オブ ハイヤー エデュケイション | Epha2t−細胞エピトープアゴニストおよびその使用 |
| JP2005185281A (ja) * | 2003-12-04 | 2005-07-14 | Mbl Venture Capital Co Ltd | 細胞表面抗原に対する抗体取得とその抗原同定 |
| JP2007524105A (ja) * | 2004-02-25 | 2007-08-23 | バイオエンハンスメンツ リミテッド | 結合物質 |
Cited By (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2020098195A (ja) * | 2013-01-04 | 2020-06-25 | シトムクス セラピューティクス,インコーポレイティド | 生体系におけるプロテアーゼ活性を検出するための組成物及び方法 |
| JP7001652B2 (ja) | 2013-01-04 | 2022-02-21 | シトムクス セラピューティクス,インコーポレイティド | 生体系におけるプロテアーゼ活性を検出するための組成物及び方法 |
| JP2016520614A (ja) * | 2013-05-28 | 2016-07-14 | ディーシービー−ユーエスエー エルエルシーDcb−Usa Llc | タンパク質薬物の不活性化のための抗体ロッカー |
| JP2022065174A (ja) * | 2013-07-25 | 2022-04-26 | シトムクス セラピューティクス,インコーポレイティド | 多重特異性抗体、多重特異性活性化可能抗体、及びそれらの使用方法 |
| JP2016538240A (ja) * | 2013-09-25 | 2016-12-08 | シトムクス セラピューティクス,インコーポレイティド | マトリックスメタロプロテイナーゼ基質及び他の切断可能部分並びにそれらの使用方法 |
| JP2018509182A (ja) * | 2015-03-13 | 2018-04-05 | サイトメックス セラピューティクス インコーポレイテッド | 抗pdl1抗体、活性化可能抗pdl1抗体、およびその使用方法 |
| JP2021072807A (ja) * | 2015-03-13 | 2021-05-13 | サイトメックス セラピューティクス インコーポレイテッド | 抗pdl1抗体、活性化可能抗pdl1抗体、およびその使用方法 |
| US11174316B2 (en) | 2015-03-13 | 2021-11-16 | Cytomx Therapeutics, Inc. | Anti-PDL1 antibodies, activatable anti-PDL1 antibodies, and methods of use thereof |
| JP7165217B2 (ja) | 2015-03-13 | 2022-11-02 | サイトメックス セラピューティクス インコーポレイテッド | 抗pdl1抗体、活性化可能抗pdl1抗体、およびその使用方法 |
| JP2018520642A (ja) * | 2015-05-01 | 2018-08-02 | ジェネンテック, インコーポレイテッド | マスク抗cd3抗体及びその使用方法 |
| US11168144B2 (en) | 2017-06-01 | 2021-11-09 | Cytomx Therapeutics, Inc. | Activatable anti-PDL1 antibodies, and methods of use thereof |
Also Published As
| Publication number | Publication date |
|---|---|
| EP2356131A4 (en) | 2012-09-12 |
| EP2356131A1 (en) | 2011-08-17 |
| WO2010077643A1 (en) | 2010-07-08 |
| US20100189727A1 (en) | 2010-07-29 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP2012511033A (ja) | 多価化合物の可逆阻害用マスキングリガンド | |
| JP7337864B2 (ja) | マトリプターゼ及びu‐プラスミノーゲン活性化因子の基質及び他の切断可能部分、並びにその使用方法 | |
| JP7412521B2 (ja) | Cd47に対するヒト化及びキメラモノクローナル抗体 | |
| JP7076152B2 (ja) | IgG結合ペプチドによる抗体の特異的修飾 | |
| JP6571730B2 (ja) | 改変した抗体組成物、それを作製および使用する方法 | |
| CN106163556B (zh) | 基质金属蛋白酶底物和其它可切割部分及其使用方法 | |
| BR112021010433A2 (pt) | Substratos cliváveis de metaloprotease de matriz e de serina ou cisteína protease e métodos de uso destes | |
| US10519247B2 (en) | Targeting HER2 and HER3 with bispecific antibodies in cancerous cells | |
| CN107531758A (zh) | 基质金属蛋白酶可切割且丝氨酸蛋白酶可切割底物及其使用方法 | |
| KR20200031113A (ko) | 활성화 가능한 항체의 특성을 정성적 및/또는 정량적으로 분석하는 방법 및 이의 용도 | |
| BR112020004543A2 (pt) | proteínas de ligação ativadas condicionalmente restritas | |
| KR20110100260A (ko) | Sparc 결합 scfvs | |
| US20180271997A1 (en) | Methods and Reagents to Treat Tumor and Cancer | |
| WO2018231661A1 (en) | Methods and reagents to treat tumor and cancer | |
| US20250188172A1 (en) | Compositions targeting epidermal growth factor receptor and methods for making and using the same | |
| EP4240407A1 (en) | Antigen binding domain with reduced clipping rate | |
| WO2023143547A1 (zh) | 抗cd28抗体及其应用 | |
| US20240360195A1 (en) | Novel fab dimers | |
| TW202540163A (zh) | 利用環境應答性胜肽的蛋白質之製造方法 | |
| HK40083794A (en) | Platform for constructing multispecific antibody | |
| HK40023271A (en) | Matriptase and u-plasminogen activator substrates and other cleavable moieties and methods of use thereof | |
| NZ755670A (en) | Multispecific antibodies, multispecific activatable antibodies and methods of using the same |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| RD01 | Notification of change of attorney |
Free format text: JAPANESE INTERMEDIATE CODE: A7426 Effective date: 20120727 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A821 Effective date: 20120727 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20121206 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20121217 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20140513 |
|
| A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20141021 |