DK2603528T3 - FAB-glycosylated ANTIBODIES - Google Patents
FAB-glycosylated ANTIBODIES Download PDFInfo
- Publication number
- DK2603528T3 DK2603528T3 DK11760415.7T DK11760415T DK2603528T3 DK 2603528 T3 DK2603528 T3 DK 2603528T3 DK 11760415 T DK11760415 T DK 11760415T DK 2603528 T3 DK2603528 T3 DK 2603528T3
- Authority
- DK
- Denmark
- Prior art keywords
- antibody
- amino acid
- fragments
- composition
- derivative
- Prior art date
Links
- 238000006206 glycosylation reaction Methods 0.000 claims description 372
- 230000013595 glycosylation Effects 0.000 claims description 371
- 239000012634 fragment Substances 0.000 claims description 361
- 210000004027 cell Anatomy 0.000 claims description 272
- 239000000203 mixture Substances 0.000 claims description 243
- 150000001720 carbohydrates Chemical class 0.000 claims description 224
- 235000014633 carbohydrates Nutrition 0.000 claims description 223
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 194
- 125000005629 sialic acid group Chemical group 0.000 claims description 117
- 241000282414 Homo sapiens Species 0.000 claims description 99
- 230000001965 increasing effect Effects 0.000 claims description 94
- 230000009450 sialylation Effects 0.000 claims description 79
- 230000000694 effects Effects 0.000 claims description 69
- 206010028980 Neoplasm Diseases 0.000 claims description 67
- SHZGCJCMOBCMKK-DHVFOXMCSA-N L-fucopyranose Chemical group C[C@@H]1OC(O)[C@@H](O)[C@H](O)[C@@H]1O SHZGCJCMOBCMKK-DHVFOXMCSA-N 0.000 claims description 66
- 238000000034 method Methods 0.000 claims description 54
- YOHYSYJDKVYCJI-UHFFFAOYSA-N n-[3-[[6-[3-(trifluoromethyl)anilino]pyrimidin-4-yl]amino]phenyl]cyclopropanecarboxamide Chemical group FC(F)(F)C1=CC=CC(NC=2N=CN=C(NC=3C=C(NC(=O)C4CC4)C=CC=3)C=2)=C1 YOHYSYJDKVYCJI-UHFFFAOYSA-N 0.000 claims description 50
- 150000001413 amino acids Chemical class 0.000 claims description 47
- 102000052116 epidermal growth factor receptor activity proteins Human genes 0.000 claims description 44
- 108700015053 epidermal growth factor receptor activity proteins Proteins 0.000 claims description 44
- SQVRNKJHWKZAKO-UHFFFAOYSA-N beta-N-Acetyl-D-neuraminic acid Natural products CC(=O)NC1C(O)CC(O)(C(O)=O)OC1C(O)C(O)CO SQVRNKJHWKZAKO-UHFFFAOYSA-N 0.000 claims description 37
- 201000011510 cancer Diseases 0.000 claims description 35
- SQVRNKJHWKZAKO-OQPLDHBCSA-N sialic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)OC1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-OQPLDHBCSA-N 0.000 claims description 34
- 210000004881 tumor cell Anatomy 0.000 claims description 31
- 241000699666 Mus <mouse, genus> Species 0.000 claims description 30
- 101710113436 GTPase KRas Proteins 0.000 claims description 28
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 claims description 27
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 claims description 27
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 claims description 23
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 claims description 23
- 230000014509 gene expression Effects 0.000 claims description 23
- 230000035772 mutation Effects 0.000 claims description 23
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 20
- NFGXHKASABOEEW-UHFFFAOYSA-N 1-methylethyl 11-methoxy-3,7,11-trimethyl-2,4-dodecadienoate Chemical compound COC(C)(C)CCCC(C)CC=CC(C)=CC(=O)OC(C)C NFGXHKASABOEEW-UHFFFAOYSA-N 0.000 claims description 19
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 18
- 125000002842 L-seryl group Chemical group O=C([*])[C@](N([H])[H])([H])C([H])([H])O[H] 0.000 claims description 17
- 238000011282 treatment Methods 0.000 claims description 17
- FDJKUWYYUZCUJX-KVNVFURPSA-N N-glycolylneuraminic acid Chemical group OC[C@H](O)[C@H](O)[C@@H]1O[C@](O)(C(O)=O)C[C@H](O)[C@H]1NC(=O)CO FDJKUWYYUZCUJX-KVNVFURPSA-N 0.000 claims description 16
- 229920001184 polypeptide Polymers 0.000 claims description 16
- OVRNDRQMDRJTHS-FMDGEEDCSA-N N-acetyl-beta-D-glucosamine Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O OVRNDRQMDRJTHS-FMDGEEDCSA-N 0.000 claims description 12
- 241000288906 Primates Species 0.000 claims description 12
- 229940082789 erbitux Drugs 0.000 claims description 11
- 230000019491 signal transduction Effects 0.000 claims description 11
- OVRNDRQMDRJTHS-UHFFFAOYSA-N N-acelyl-D-glucosamine Natural products CC(=O)NC1C(O)OC(CO)C(O)C1O OVRNDRQMDRJTHS-UHFFFAOYSA-N 0.000 claims description 9
- MBLBDJOUHNCFQT-LXGUWJNJSA-N N-acetylglucosamine Natural products CC(=O)N[C@@H](C=O)[C@@H](O)[C@H](O)[C@H](O)CO MBLBDJOUHNCFQT-LXGUWJNJSA-N 0.000 claims description 9
- 108010008177 Fd immunoglobulins Proteins 0.000 claims description 8
- 241000700159 Rattus Species 0.000 claims description 8
- 230000004913 activation Effects 0.000 claims description 8
- OVRNDRQMDRJTHS-RTRLPJTCSA-N N-acetyl-D-glucosamine Chemical compound CC(=O)N[C@H]1C(O)O[C@H](CO)[C@@H](O)[C@@H]1O OVRNDRQMDRJTHS-RTRLPJTCSA-N 0.000 claims description 6
- 101100194625 Rattus norvegicus Rgs19 gene Proteins 0.000 claims description 6
- 239000003814 drug Substances 0.000 claims description 6
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 5
- 108090000430 Phosphatidylinositol 3-kinases Proteins 0.000 claims description 5
- 102000003993 Phosphatidylinositol 3-kinases Human genes 0.000 claims description 5
- 239000002253 acid Substances 0.000 claims description 5
- 241000283707 Capra Species 0.000 claims description 4
- 238000002560 therapeutic procedure Methods 0.000 claims description 4
- 229950006780 n-acetylglucosamine Drugs 0.000 claims description 3
- 230000002018 overexpression Effects 0.000 claims description 3
- 241000282836 Camelus dromedarius Species 0.000 claims description 2
- 230000008569 process Effects 0.000 claims description 2
- 102000009929 raf Kinases Human genes 0.000 claims description 2
- 108010077182 raf Kinases Proteins 0.000 claims description 2
- MSWZFWKMSRAUBD-IVMDWMLBSA-N glucosamine group Chemical group OC1[C@H](N)[C@@H](O)[C@H](O)[C@H](O1)CO MSWZFWKMSRAUBD-IVMDWMLBSA-N 0.000 claims 2
- 229960005395 cetuximab Drugs 0.000 description 146
- 230000027455 binding Effects 0.000 description 101
- 235000001014 amino acid Nutrition 0.000 description 66
- 125000000837 carbohydrate group Chemical group 0.000 description 64
- 239000000427 antigen Substances 0.000 description 62
- 108091007433 antigens Proteins 0.000 description 61
- 102000036639 antigens Human genes 0.000 description 61
- 229940126618 pankomab Drugs 0.000 description 59
- 230000010056 antibody-dependent cellular cytotoxicity Effects 0.000 description 57
- SHZGCJCMOBCMKK-UHFFFAOYSA-N D-mannomethylose Natural products CC1OC(O)C(O)C(O)C1O SHZGCJCMOBCMKK-UHFFFAOYSA-N 0.000 description 53
- 230000003247 decreasing effect Effects 0.000 description 49
- 229940024606 amino acid Drugs 0.000 description 42
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 28
- 150000007523 nucleic acids Chemical class 0.000 description 26
- PNNNRSAQSRJVSB-SLPGGIOYSA-N Fucose Natural products C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)C=O PNNNRSAQSRJVSB-SLPGGIOYSA-N 0.000 description 25
- 230000033581 fucosylation Effects 0.000 description 23
- 108020004707 nucleic acids Proteins 0.000 description 23
- 102000039446 nucleic acids Human genes 0.000 description 23
- 108090000623 proteins and genes Proteins 0.000 description 22
- 230000001976 improved effect Effects 0.000 description 21
- 241001465754 Metazoa Species 0.000 description 19
- 239000003795 chemical substances by application Substances 0.000 description 19
- 230000001225 therapeutic effect Effects 0.000 description 19
- 230000009089 cytolysis Effects 0.000 description 18
- 235000018102 proteins Nutrition 0.000 description 17
- 102000004169 proteins and genes Human genes 0.000 description 17
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 16
- 238000004519 manufacturing process Methods 0.000 description 16
- 102000004190 Enzymes Human genes 0.000 description 15
- 108090000790 Enzymes Proteins 0.000 description 15
- 238000003556 assay Methods 0.000 description 15
- 229940088598 enzyme Drugs 0.000 description 15
- 230000004988 N-glycosylation Effects 0.000 description 14
- 230000004071 biological effect Effects 0.000 description 13
- 230000005764 inhibitory process Effects 0.000 description 13
- 102000003952 Caspase 3 Human genes 0.000 description 12
- 108090000397 Caspase 3 Proteins 0.000 description 12
- 125000000539 amino acid group Chemical group 0.000 description 12
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 12
- 108091035707 Consensus sequence Proteins 0.000 description 11
- 241000699670 Mus sp. Species 0.000 description 11
- 229960000548 alemtuzumab Drugs 0.000 description 11
- 238000002474 experimental method Methods 0.000 description 11
- 239000003446 ligand Substances 0.000 description 11
- 230000035755 proliferation Effects 0.000 description 11
- 229950007874 solanezumab Drugs 0.000 description 11
- 239000000126 substance Substances 0.000 description 11
- 206010009944 Colon cancer Diseases 0.000 description 10
- 238000002360 preparation method Methods 0.000 description 10
- 208000001333 Colorectal Neoplasms Diseases 0.000 description 9
- 241000699660 Mus musculus Species 0.000 description 9
- SQVRNKJHWKZAKO-PFQGKNLYSA-N N-acetyl-beta-neuraminic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)O[C@H]1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-PFQGKNLYSA-N 0.000 description 9
- 238000011534 incubation Methods 0.000 description 9
- 238000011580 nude mouse model Methods 0.000 description 9
- 239000008194 pharmaceutical composition Substances 0.000 description 9
- 102000009109 Fc receptors Human genes 0.000 description 8
- 108010087819 Fc receptors Proteins 0.000 description 8
- 230000006907 apoptotic process Effects 0.000 description 8
- 210000005260 human cell Anatomy 0.000 description 8
- 238000001727 in vivo Methods 0.000 description 8
- 241000894007 species Species 0.000 description 8
- 210000001519 tissue Anatomy 0.000 description 8
- 230000004614 tumor growth Effects 0.000 description 8
- 102000003886 Glycoproteins Human genes 0.000 description 7
- 108090000288 Glycoproteins Proteins 0.000 description 7
- 230000037396 body weight Effects 0.000 description 7
- 230000006870 function Effects 0.000 description 7
- 230000026731 phosphorylation Effects 0.000 description 7
- 238000006366 phosphorylation reaction Methods 0.000 description 7
- 210000002966 serum Anatomy 0.000 description 7
- 238000006467 substitution reaction Methods 0.000 description 7
- 241000282567 Macaca fascicularis Species 0.000 description 6
- 206010027476 Metastases Diseases 0.000 description 6
- 230000008901 benefit Effects 0.000 description 6
- 230000000903 blocking effect Effects 0.000 description 6
- 238000003745 diagnosis Methods 0.000 description 6
- 238000010494 dissociation reaction Methods 0.000 description 6
- 230000005593 dissociations Effects 0.000 description 6
- 239000012636 effector Substances 0.000 description 6
- 230000006882 induction of apoptosis Effects 0.000 description 6
- 210000000066 myeloid cell Anatomy 0.000 description 6
- 208000002154 non-small cell lung carcinoma Diseases 0.000 description 6
- 230000002265 prevention Effects 0.000 description 6
- 102000005962 receptors Human genes 0.000 description 6
- 108020003175 receptors Proteins 0.000 description 6
- 230000002829 reductive effect Effects 0.000 description 6
- 230000001988 toxicity Effects 0.000 description 6
- 231100000419 toxicity Toxicity 0.000 description 6
- 208000029729 tumor suppressor gene on chromosome 11 Diseases 0.000 description 6
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 5
- 101100454807 Caenorhabditis elegans lgg-1 gene Proteins 0.000 description 5
- 108020004705 Codon Proteins 0.000 description 5
- 238000002965 ELISA Methods 0.000 description 5
- OVRNDRQMDRJTHS-CBQIKETKSA-N N-Acetyl-D-Galactosamine Chemical group CC(=O)N[C@H]1[C@@H](O)O[C@H](CO)[C@H](O)[C@@H]1O OVRNDRQMDRJTHS-CBQIKETKSA-N 0.000 description 5
- 108091000080 Phosphotransferase Proteins 0.000 description 5
- 239000004365 Protease Substances 0.000 description 5
- 102000003838 Sialyltransferases Human genes 0.000 description 5
- 108090000141 Sialyltransferases Proteins 0.000 description 5
- 101710120037 Toxin CcdB Proteins 0.000 description 5
- 230000002411 adverse Effects 0.000 description 5
- 238000004458 analytical method Methods 0.000 description 5
- 230000000259 anti-tumor effect Effects 0.000 description 5
- 230000015572 biosynthetic process Effects 0.000 description 5
- 210000000601 blood cell Anatomy 0.000 description 5
- 230000004540 complement-dependent cytotoxicity Effects 0.000 description 5
- 229940127089 cytotoxic agent Drugs 0.000 description 5
- 230000001419 dependent effect Effects 0.000 description 5
- 201000010099 disease Diseases 0.000 description 5
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 5
- 210000000987 immune system Anatomy 0.000 description 5
- 102000020233 phosphotransferase Human genes 0.000 description 5
- 238000004393 prognosis Methods 0.000 description 5
- 238000012360 testing method Methods 0.000 description 5
- 231100000041 toxicology testing Toxicity 0.000 description 5
- 101100454808 Caenorhabditis elegans lgg-2 gene Proteins 0.000 description 4
- 108010078791 Carrier Proteins Proteins 0.000 description 4
- 102100035360 Cerebellar degeneration-related antigen 1 Human genes 0.000 description 4
- 102000001301 EGF receptor Human genes 0.000 description 4
- 108060006698 EGF receptor Proteins 0.000 description 4
- 206010058467 Lung neoplasm malignant Diseases 0.000 description 4
- MBLBDJOUHNCFQT-UHFFFAOYSA-N N-acetyl-D-galactosamine Natural products CC(=O)NC(C=O)C(O)C(O)C(O)CO MBLBDJOUHNCFQT-UHFFFAOYSA-N 0.000 description 4
- SUHQNCLNRUAGOO-UHFFFAOYSA-N N-glycoloyl-neuraminic acid Natural products OCC(O)C(O)C(O)C(NC(=O)CO)C(O)CC(=O)C(O)=O SUHQNCLNRUAGOO-UHFFFAOYSA-N 0.000 description 4
- FDJKUWYYUZCUJX-UHFFFAOYSA-N N-glycolyl-beta-neuraminic acid Natural products OCC(O)C(O)C1OC(O)(C(O)=O)CC(O)C1NC(=O)CO FDJKUWYYUZCUJX-UHFFFAOYSA-N 0.000 description 4
- 238000007792 addition Methods 0.000 description 4
- 239000002246 antineoplastic agent Substances 0.000 description 4
- 239000000872 buffer Substances 0.000 description 4
- 230000004663 cell proliferation Effects 0.000 description 4
- 238000007385 chemical modification Methods 0.000 description 4
- 150000001875 compounds Chemical class 0.000 description 4
- 238000004132 cross linking Methods 0.000 description 4
- 238000012217 deletion Methods 0.000 description 4
- 230000037430 deletion Effects 0.000 description 4
- 238000001514 detection method Methods 0.000 description 4
- 239000003085 diluting agent Substances 0.000 description 4
- 238000000684 flow cytometry Methods 0.000 description 4
- 238000009472 formulation Methods 0.000 description 4
- 239000001963 growth medium Substances 0.000 description 4
- 208000014829 head and neck neoplasm Diseases 0.000 description 4
- 239000003550 marker Substances 0.000 description 4
- 239000002609 medium Substances 0.000 description 4
- 230000004048 modification Effects 0.000 description 4
- 238000012986 modification Methods 0.000 description 4
- 238000012544 monitoring process Methods 0.000 description 4
- 150000002772 monosaccharides Chemical group 0.000 description 4
- 208000025113 myeloid leukemia Diseases 0.000 description 4
- 238000002732 pharmacokinetic assay Methods 0.000 description 4
- 238000011321 prophylaxis Methods 0.000 description 4
- 238000001959 radiotherapy Methods 0.000 description 4
- 230000009467 reduction Effects 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- 125000000341 threoninyl group Chemical group [H]OC([H])(C([H])([H])[H])C([H])(N([H])[H])C(*)=O 0.000 description 4
- 230000003442 weekly effect Effects 0.000 description 4
- 206010006187 Breast cancer Diseases 0.000 description 3
- 208000026310 Breast neoplasm Diseases 0.000 description 3
- 101100217502 Caenorhabditis elegans lgg-3 gene Proteins 0.000 description 3
- 201000009030 Carcinoma Diseases 0.000 description 3
- 229910052693 Europium Inorganic materials 0.000 description 3
- 241000282412 Homo Species 0.000 description 3
- 101001133056 Homo sapiens Mucin-1 Proteins 0.000 description 3
- KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 3
- 102100034256 Mucin-1 Human genes 0.000 description 3
- 101100346932 Mus musculus Muc1 gene Proteins 0.000 description 3
- 108091028043 Nucleic acid sequence Proteins 0.000 description 3
- 230000004989 O-glycosylation Effects 0.000 description 3
- 229930012538 Paclitaxel Natural products 0.000 description 3
- 108090000526 Papain Proteins 0.000 description 3
- 230000009471 action Effects 0.000 description 3
- 230000003213 activating effect Effects 0.000 description 3
- 239000013543 active substance Substances 0.000 description 3
- 230000001640 apoptogenic effect Effects 0.000 description 3
- 125000000613 asparagine group Chemical group N[C@@H](CC(N)=O)C(=O)* 0.000 description 3
- 210000000481 breast Anatomy 0.000 description 3
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 3
- 238000012258 culturing Methods 0.000 description 3
- 231100000599 cytotoxic agent Toxicity 0.000 description 3
- 230000002950 deficient Effects 0.000 description 3
- 238000010790 dilution Methods 0.000 description 3
- 239000012895 dilution Substances 0.000 description 3
- 230000002255 enzymatic effect Effects 0.000 description 3
- OGPBJKLSAFTDLK-UHFFFAOYSA-N europium atom Chemical compound [Eu] OGPBJKLSAFTDLK-UHFFFAOYSA-N 0.000 description 3
- 229930182830 galactose Natural products 0.000 description 3
- 238000010353 genetic engineering Methods 0.000 description 3
- 201000010536 head and neck cancer Diseases 0.000 description 3
- 238000000338 in vitro Methods 0.000 description 3
- 230000005917 in vivo anti-tumor Effects 0.000 description 3
- 230000001939 inductive effect Effects 0.000 description 3
- 238000002347 injection Methods 0.000 description 3
- 239000007924 injection Substances 0.000 description 3
- 230000003834 intracellular effect Effects 0.000 description 3
- 238000001990 intravenous administration Methods 0.000 description 3
- 229960004768 irinotecan Drugs 0.000 description 3
- UWKQSNNFCGGAFS-XIFFEERXSA-N irinotecan Chemical compound C1=C2C(CC)=C3CN(C(C4=C([C@@](C(=O)OC4)(O)CC)C=4)=O)C=4C3=NC2=CC=C1OC(=O)N(CC1)CCC1N1CCCCC1 UWKQSNNFCGGAFS-XIFFEERXSA-N 0.000 description 3
- 238000002372 labelling Methods 0.000 description 3
- 201000005202 lung cancer Diseases 0.000 description 3
- 208000020816 lung neoplasm Diseases 0.000 description 3
- 125000000311 mannosyl group Chemical group C1([C@@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 3
- 238000005259 measurement Methods 0.000 description 3
- 230000010534 mechanism of action Effects 0.000 description 3
- 230000001404 mediated effect Effects 0.000 description 3
- 230000009401 metastasis Effects 0.000 description 3
- 239000013642 negative control Substances 0.000 description 3
- 229960001592 paclitaxel Drugs 0.000 description 3
- 229940055729 papain Drugs 0.000 description 3
- 235000019834 papain Nutrition 0.000 description 3
- 238000004007 reversed phase HPLC Methods 0.000 description 3
- 238000013391 scatchard analysis Methods 0.000 description 3
- 125000001424 substituent group Chemical group 0.000 description 3
- RCINICONZNJXQF-MZXODVADSA-N taxol Chemical compound O([C@@H]1[C@@]2(C[C@@H](C(C)=C(C2(C)C)[C@H](C([C@]2(C)[C@@H](O)C[C@H]3OC[C@]3([C@H]21)OC(C)=O)=O)OC(=O)C)OC(=O)[C@H](O)[C@@H](NC(=O)C=1C=CC=CC=1)C=1C=CC=CC=1)O)C(=O)C1=CC=CC=C1 RCINICONZNJXQF-MZXODVADSA-N 0.000 description 3
- 238000012546 transfer Methods 0.000 description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- AZKSAVLVSZKNRD-UHFFFAOYSA-M 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide Chemical compound [Br-].S1C(C)=C(C)N=C1[N+]1=NC(C=2C=CC=CC=2)=NN1C1=CC=CC=C1 AZKSAVLVSZKNRD-UHFFFAOYSA-M 0.000 description 2
- 108700028369 Alleles Proteins 0.000 description 2
- FRBAHXABMQXSJQ-FXQIFTODSA-N Arg-Ser-Ser Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(O)=O FRBAHXABMQXSJQ-FXQIFTODSA-N 0.000 description 2
- 102100033787 CMP-sialic acid transporter Human genes 0.000 description 2
- 101710150575 CMP-sialic acid transporter Proteins 0.000 description 2
- 102000011727 Caspases Human genes 0.000 description 2
- 108010076667 Caspases Proteins 0.000 description 2
- 206010052358 Colorectal cancer metastatic Diseases 0.000 description 2
- 108010089072 Dolichyl-diphosphooligosaccharide-protein glycotransferase Proteins 0.000 description 2
- AOJJSUZBOXZQNB-TZSSRYMLSA-N Doxorubicin Chemical compound O([C@H]1C[C@@](O)(CC=2C(O)=C3C(=O)C=4C=CC=C(C=4C(=O)C3=C(O)C=21)OC)C(=O)CO)[C@H]1C[C@H](N)[C@H](O)[C@H](C)O1 AOJJSUZBOXZQNB-TZSSRYMLSA-N 0.000 description 2
- 206010014733 Endometrial cancer Diseases 0.000 description 2
- 206010014759 Endometrial neoplasm Diseases 0.000 description 2
- 102000010911 Enzyme Precursors Human genes 0.000 description 2
- 108010062466 Enzyme Precursors Proteins 0.000 description 2
- 206010017993 Gastrointestinal neoplasms Diseases 0.000 description 2
- 108060003951 Immunoglobulin Proteins 0.000 description 2
- 108010091135 Immunoglobulin Fc Fragments Proteins 0.000 description 2
- 102000018071 Immunoglobulin Fc Fragments Human genes 0.000 description 2
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 2
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 2
- 208000008839 Kidney Neoplasms Diseases 0.000 description 2
- 231100000002 MTT assay Toxicity 0.000 description 2
- 238000000134 MTT assay Methods 0.000 description 2
- 102100035286 N-acetyl-D-glucosamine kinase Human genes 0.000 description 2
- 108010032040 N-acetylglucosamine kinase Proteins 0.000 description 2
- 102100033341 N-acetylmannosamine kinase Human genes 0.000 description 2
- 108010029147 N-acylmannosamine kinase Proteins 0.000 description 2
- 108010081778 N-acylneuraminate cytidylyltransferase Proteins 0.000 description 2
- FDJKUWYYUZCUJX-PGIATKPXSA-N N-glycoloylneuraminic acid Chemical compound OC[C@@H](O)[C@@H](O)[C@@H]1OC(O)(C(O)=O)C[C@H](O)[C@H]1NC(=O)CO FDJKUWYYUZCUJX-PGIATKPXSA-N 0.000 description 2
- 206010033128 Ovarian cancer Diseases 0.000 description 2
- 206010061535 Ovarian neoplasm Diseases 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- SFECXGVELZFBFJ-VEVYYDQMSA-N Pro-Asp-Thr Chemical compound [H]N1CCC[C@H]1C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O SFECXGVELZFBFJ-VEVYYDQMSA-N 0.000 description 2
- 206010060862 Prostate cancer Diseases 0.000 description 2
- 238000012228 RNA interference-mediated gene silencing Methods 0.000 description 2
- 102000004879 Racemases and epimerases Human genes 0.000 description 2
- 108090001066 Racemases and epimerases Proteins 0.000 description 2
- 206010038389 Renal cancer Diseases 0.000 description 2
- 241000283984 Rodentia Species 0.000 description 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 2
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 2
- 101710091363 UDP-N-acetylglucosamine 2-epimerase Proteins 0.000 description 2
- 208000006105 Uterine Cervical Neoplasms Diseases 0.000 description 2
- DIOSYUIWOQCXNR-ONGXEEELSA-N Val-Lys-Gly Chemical compound CC(C)[C@H](N)C(=O)N[C@@H](CCCCN)C(=O)NCC(O)=O DIOSYUIWOQCXNR-ONGXEEELSA-N 0.000 description 2
- 230000002159 abnormal effect Effects 0.000 description 2
- 238000010521 absorption reaction Methods 0.000 description 2
- 238000011319 anticancer therapy Methods 0.000 description 2
- 238000003782 apoptosis assay Methods 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 108010060035 arginylproline Proteins 0.000 description 2
- 108010068265 aspartyltyrosine Proteins 0.000 description 2
- 229960000074 biopharmaceutical Drugs 0.000 description 2
- 239000000969 carrier Substances 0.000 description 2
- 230000006037 cell lysis Effects 0.000 description 2
- 201000010881 cervical cancer Diseases 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 208000029742 colonic neoplasm Diseases 0.000 description 2
- 231100000433 cytotoxic Toxicity 0.000 description 2
- 239000002254 cytotoxic agent Substances 0.000 description 2
- 230000001472 cytotoxic effect Effects 0.000 description 2
- 230000007547 defect Effects 0.000 description 2
- 230000007783 downstream signaling Effects 0.000 description 2
- 239000012530 fluid Substances 0.000 description 2
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 2
- 239000012537 formulation buffer Substances 0.000 description 2
- 108020001507 fusion proteins Proteins 0.000 description 2
- 102000037865 fusion proteins Human genes 0.000 description 2
- 230000009368 gene silencing by RNA Effects 0.000 description 2
- 150000004676 glycans Chemical class 0.000 description 2
- 229910052739 hydrogen Inorganic materials 0.000 description 2
- 239000001257 hydrogen Substances 0.000 description 2
- 238000003384 imaging method Methods 0.000 description 2
- 230000001900 immune effect Effects 0.000 description 2
- 102000018358 immunoglobulin Human genes 0.000 description 2
- 230000006698 induction Effects 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 201000002313 intestinal cancer Diseases 0.000 description 2
- 201000010982 kidney cancer Diseases 0.000 description 2
- 230000002147 killing effect Effects 0.000 description 2
- 208000032839 leukemia Diseases 0.000 description 2
- 210000004072 lung Anatomy 0.000 description 2
- 239000006166 lysate Substances 0.000 description 2
- 210000002540 macrophage Anatomy 0.000 description 2
- 230000003211 malignant effect Effects 0.000 description 2
- 210000004962 mammalian cell Anatomy 0.000 description 2
- 238000002703 mutagenesis Methods 0.000 description 2
- 231100000350 mutagenesis Toxicity 0.000 description 2
- 230000000869 mutational effect Effects 0.000 description 2
- 231100000252 nontoxic Toxicity 0.000 description 2
- 230000003000 nontoxic effect Effects 0.000 description 2
- 239000002773 nucleotide Substances 0.000 description 2
- 125000003729 nucleotide group Chemical group 0.000 description 2
- 238000011275 oncology therapy Methods 0.000 description 2
- 210000003463 organelle Anatomy 0.000 description 2
- 230000036961 partial effect Effects 0.000 description 2
- 230000037361 pathway Effects 0.000 description 2
- 239000000546 pharmaceutical excipient Substances 0.000 description 2
- BASFCYQUMIYNBI-UHFFFAOYSA-N platinum Chemical compound [Pt] BASFCYQUMIYNBI-UHFFFAOYSA-N 0.000 description 2
- 239000013641 positive control Substances 0.000 description 2
- 239000002243 precursor Substances 0.000 description 2
- 235000019419 proteases Nutrition 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 239000000376 reactant Substances 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 102200006539 rs121913529 Human genes 0.000 description 2
- 208000011581 secondary neoplasm Diseases 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 125000005630 sialyl group Chemical group 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 206010041823 squamous cell carcinoma Diseases 0.000 description 2
- 239000003381 stabilizer Substances 0.000 description 2
- 230000000638 stimulation Effects 0.000 description 2
- 238000007920 subcutaneous administration Methods 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 239000003981 vehicle Substances 0.000 description 2
- 210000003905 vulva Anatomy 0.000 description 2
- 201000004916 vulva carcinoma Diseases 0.000 description 2
- 208000013013 vulvar carcinoma Diseases 0.000 description 2
- VAOYPHGXHKUTHC-UHFFFAOYSA-N 2-[2-[bis(carboxymethyl)amino]ethyl-[2-[bis(carboxymethyl)amino]-3-(4-isothiocyanatophenyl)propyl]amino]acetic acid Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(=O)O)CC(N(CC(O)=O)CC(O)=O)CC1=CC=C(N=C=S)C=C1 VAOYPHGXHKUTHC-UHFFFAOYSA-N 0.000 description 1
- 208000010507 Adenocarcinoma of Lung Diseases 0.000 description 1
- MEFILNJXAVSUTO-JXUBOQSCSA-N Ala-Leu-Thr Chemical compound C[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)O)C(O)=O MEFILNJXAVSUTO-JXUBOQSCSA-N 0.000 description 1
- 108010032595 Antibody Binding Sites Proteins 0.000 description 1
- 101100227726 Arabidopsis thaliana FRL3 gene Proteins 0.000 description 1
- GIVATXIGCXFQQA-FXQIFTODSA-N Arg-Ala-Ser Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](C)NC(=O)[C@@H](N)CCCN=C(N)N GIVATXIGCXFQQA-FXQIFTODSA-N 0.000 description 1
- LQJAALCCPOTJGB-YUMQZZPRSA-N Arg-Pro Chemical compound NC(N)=NCCC[C@H](N)C(=O)N1CCC[C@H]1C(O)=O LQJAALCCPOTJGB-YUMQZZPRSA-N 0.000 description 1
- QHUOOCKNNURZSL-IHRRRGAJSA-N Arg-Tyr-Ser Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CO)C(O)=O QHUOOCKNNURZSL-IHRRRGAJSA-N 0.000 description 1
- HUZGPXBILPMCHM-IHRRRGAJSA-N Asn-Arg-Phe Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC1=CC=CC=C1)C(O)=O HUZGPXBILPMCHM-IHRRRGAJSA-N 0.000 description 1
- RJUHZPRQRQLCFL-IMJSIDKUSA-N Asn-Asn Chemical compound NC(=O)C[C@H](N)C(=O)N[C@@H](CC(N)=O)C(O)=O RJUHZPRQRQLCFL-IMJSIDKUSA-N 0.000 description 1
- ACRYGQFHAQHDSF-ZLUOBGJFSA-N Asn-Asn-Asn Chemical compound NC(=O)C[C@H](N)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O ACRYGQFHAQHDSF-ZLUOBGJFSA-N 0.000 description 1
- BVLIJXXSXBUGEC-SRVKXCTJSA-N Asn-Asn-Tyr Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O BVLIJXXSXBUGEC-SRVKXCTJSA-N 0.000 description 1
- PBSQFBAJKPLRJY-BYULHYEWSA-N Asn-Gly-Ile Chemical compound CC[C@H](C)[C@@H](C(=O)O)NC(=O)CNC(=O)[C@H](CC(=O)N)N PBSQFBAJKPLRJY-BYULHYEWSA-N 0.000 description 1
- ANPFQTJEPONRPL-UGYAYLCHSA-N Asn-Ile-Asp Chemical compound NC(=O)C[C@H](N)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(O)=O)C(O)=O ANPFQTJEPONRPL-UGYAYLCHSA-N 0.000 description 1
- HDHZCEDPLTVHFZ-GUBZILKMSA-N Asn-Leu-Glu Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(O)=O HDHZCEDPLTVHFZ-GUBZILKMSA-N 0.000 description 1
- HPASIOLTWSNMFB-OLHMAJIHSA-N Asn-Thr-Asp Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(O)=O)C(O)=O HPASIOLTWSNMFB-OLHMAJIHSA-N 0.000 description 1
- YSYTWUMRHSFODC-QWRGUYRKSA-N Asn-Tyr-Gly Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)NCC(O)=O YSYTWUMRHSFODC-QWRGUYRKSA-N 0.000 description 1
- CGYKCTPUGXFPMG-IHPCNDPISA-N Asn-Tyr-Trp Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC1=CNC2=C1C=CC=C2)C(O)=O CGYKCTPUGXFPMG-IHPCNDPISA-N 0.000 description 1
- LIVXPXUVXFRWNY-CIUDSAMLSA-N Asp-Lys-Ala Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(O)=O LIVXPXUVXFRWNY-CIUDSAMLSA-N 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 208000003174 Brain Neoplasms Diseases 0.000 description 1
- 206010055113 Breast cancer metastatic Diseases 0.000 description 1
- 101100120609 Caenorhabditis elegans frh-1 gene Proteins 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 208000024172 Cardiovascular disease Diseases 0.000 description 1
- 206010008342 Cervix carcinoma Diseases 0.000 description 1
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
- 241000699800 Cricetinae Species 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 101710112752 Cytotoxin Proteins 0.000 description 1
- RGHNJXZEOKUKBD-SQOUGZDYSA-M D-gluconate Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C([O-])=O RGHNJXZEOKUKBD-SQOUGZDYSA-M 0.000 description 1
- 108020004414 DNA Proteins 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 108020005199 Dehydrogenases Proteins 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 241000283073 Equus caballus Species 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 208000000461 Esophageal Neoplasms Diseases 0.000 description 1
- 101150023991 FMNL1 gene Proteins 0.000 description 1
- 101150005226 FRL1 gene Proteins 0.000 description 1
- 101150065691 FRL2 gene Proteins 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- 102100028930 Formin-like protein 1 Human genes 0.000 description 1
- 102100032789 Formin-like protein 3 Human genes 0.000 description 1
- 108010045674 Fucose-1-phosphate guanylyltransferase Proteins 0.000 description 1
- 108010062427 GDP-mannose 4,6-dehydratase Proteins 0.000 description 1
- 102000002312 GDPmannose 4,6-dehydratase Human genes 0.000 description 1
- 206010018338 Glioma Diseases 0.000 description 1
- CAVMESABQIKFKT-IUCAKERBSA-N Glu-Gly-His Chemical compound C1=C(NC=N1)C[C@@H](C(=O)O)NC(=O)CNC(=O)[C@H](CCC(=O)O)N CAVMESABQIKFKT-IUCAKERBSA-N 0.000 description 1
- QIQABBIDHGQXGA-ZPFDUUQYSA-N Glu-Ile-Arg Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCCN=C(N)N)C(O)=O QIQABBIDHGQXGA-ZPFDUUQYSA-N 0.000 description 1
- SYAYROHMAIHWFB-KBIXCLLPSA-N Glu-Ser-Ile Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)CC)C(O)=O SYAYROHMAIHWFB-KBIXCLLPSA-N 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Chemical compound OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- UXJHNZODTMHWRD-WHFBIAKZSA-N Gly-Asn-Ala Chemical compound [H]NCC(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(O)=O UXJHNZODTMHWRD-WHFBIAKZSA-N 0.000 description 1
- QGZSAHIZRQHCEQ-QWRGUYRKSA-N Gly-Asp-Tyr Chemical compound NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@H](C(O)=O)CC1=CC=C(O)C=C1 QGZSAHIZRQHCEQ-QWRGUYRKSA-N 0.000 description 1
- WNZOCXUOGVYYBJ-CDMKHQONSA-N Gly-Phe-Thr Chemical compound C[C@H]([C@@H](C(=O)O)NC(=O)[C@H](CC1=CC=CC=C1)NC(=O)CN)O WNZOCXUOGVYYBJ-CDMKHQONSA-N 0.000 description 1
- 239000012981 Hank's balanced salt solution Substances 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- IDXZDKMBEXLFMB-HGNGGELXSA-N His-Ile Chemical compound CC[C@H](C)[C@@H](C(O)=O)NC(=O)[C@@H](N)CC1=CNC=N1 IDXZDKMBEXLFMB-HGNGGELXSA-N 0.000 description 1
- HIJIJPFILYPTFR-ACRUOGEOSA-N His-Tyr-Tyr Chemical compound [H]N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O HIJIJPFILYPTFR-ACRUOGEOSA-N 0.000 description 1
- UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 description 1
- 206010020751 Hypersensitivity Diseases 0.000 description 1
- HDODQNPMSHDXJT-GHCJXIJMSA-N Ile-Asn-Ser Chemical compound CC[C@H](C)[C@H](N)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(O)=O HDODQNPMSHDXJT-GHCJXIJMSA-N 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 208000005016 Intestinal Neoplasms Diseases 0.000 description 1
- 241000880493 Leptailurus serval Species 0.000 description 1
- BQSLGJHIAGOZCD-CIUDSAMLSA-N Leu-Ala-Ser Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(O)=O BQSLGJHIAGOZCD-CIUDSAMLSA-N 0.000 description 1
- OYQUOLRTJHWVSQ-SRVKXCTJSA-N Leu-His-Ser Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CO)C(O)=O OYQUOLRTJHWVSQ-SRVKXCTJSA-N 0.000 description 1
- VCHVSKNMTXWIIP-SRVKXCTJSA-N Leu-Lys-Ser Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CO)C(O)=O VCHVSKNMTXWIIP-SRVKXCTJSA-N 0.000 description 1
- DPURXCQCHSQPAN-AVGNSLFASA-N Leu-Pro-Pro Chemical compound CC(C)C[C@H](N)C(=O)N1CCC[C@H]1C(=O)N1[C@H](C(O)=O)CCC1 DPURXCQCHSQPAN-AVGNSLFASA-N 0.000 description 1
- 206010025323 Lymphomas Diseases 0.000 description 1
- UWKNTTJNVSYXPC-CIUDSAMLSA-N Lys-Ala-Ser Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](C)NC(=O)[C@@H](N)CCCCN UWKNTTJNVSYXPC-CIUDSAMLSA-N 0.000 description 1
- NNKLKUUGESXCBS-KBPBESRZSA-N Lys-Gly-Tyr Chemical compound [H]N[C@@H](CCCCN)C(=O)NCC(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O NNKLKUUGESXCBS-KBPBESRZSA-N 0.000 description 1
- IOQWIOPSKJOEKI-SRVKXCTJSA-N Lys-Ser-Leu Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(O)=O IOQWIOPSKJOEKI-SRVKXCTJSA-N 0.000 description 1
- MIMXMVDLMDMOJD-BZSNNMDCSA-N Lys-Tyr-Leu Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC(C)C)C(O)=O MIMXMVDLMDMOJD-BZSNNMDCSA-N 0.000 description 1
- GILLQRYAWOMHED-DCAQKATOSA-N Lys-Val-Ser Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](N)CCCCN GILLQRYAWOMHED-DCAQKATOSA-N 0.000 description 1
- FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- PWHULOQIROXLJO-UHFFFAOYSA-N Manganese Chemical compound [Mn] PWHULOQIROXLJO-UHFFFAOYSA-N 0.000 description 1
- PCTFVQATEGYHJU-FXQIFTODSA-N Met-Ser-Asn Chemical compound [H]N[C@@H](CCSC)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(O)=O PCTFVQATEGYHJU-FXQIFTODSA-N 0.000 description 1
- 108010063954 Mucins Proteins 0.000 description 1
- 102000015728 Mucins Human genes 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 235000009421 Myristica fragrans Nutrition 0.000 description 1
- YBAFDPFAUTYYRW-UHFFFAOYSA-N N-L-alpha-glutamyl-L-leucine Natural products CC(C)CC(C(O)=O)NC(=O)C(N)CCC(O)=O YBAFDPFAUTYYRW-UHFFFAOYSA-N 0.000 description 1
- 206010029260 Neuroblastoma Diseases 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 206010061902 Pancreatic neoplasm Diseases 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 241000009328 Perro Species 0.000 description 1
- CUMXHKAOHNWRFQ-BZSNNMDCSA-N Phe-Asp-Tyr Chemical compound C([C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)C1=CC=CC=C1 CUMXHKAOHNWRFQ-BZSNNMDCSA-N 0.000 description 1
- FXPZZKBHNOMLGA-HJWJTTGWSA-N Phe-Ile-Arg Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CCCN=C(N)N)C(=O)O)NC(=O)[C@H](CC1=CC=CC=C1)N FXPZZKBHNOMLGA-HJWJTTGWSA-N 0.000 description 1
- RAGOJJCBGXARPO-XVSYOHENSA-N Phe-Thr-Asp Chemical compound OC(=O)C[C@@H](C(O)=O)NC(=O)[C@H]([C@H](O)C)NC(=O)[C@@H](N)CC1=CC=CC=C1 RAGOJJCBGXARPO-XVSYOHENSA-N 0.000 description 1
- ZTVSVSFBHUVYIN-UFYCRDLUSA-N Phe-Tyr-Met Chemical compound C([C@@H](C(=O)N[C@@H](CCSC)C(O)=O)NC(=O)[C@@H](N)CC=1C=CC=CC=1)C1=CC=C(O)C=C1 ZTVSVSFBHUVYIN-UFYCRDLUSA-N 0.000 description 1
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
- AWQGDZBKQTYNMN-IHRRRGAJSA-N Pro-Phe-Asp Chemical compound C1C[C@H](NC1)C(=O)N[C@@H](CC2=CC=CC=C2)C(=O)N[C@@H](CC(=O)O)C(=O)O AWQGDZBKQTYNMN-IHRRRGAJSA-N 0.000 description 1
- SPLBRAKYXGOFSO-UNQGMJICSA-N Pro-Phe-Thr Chemical compound C[C@H]([C@@H](C(=O)O)NC(=O)[C@H](CC1=CC=CC=C1)NC(=O)[C@@H]2CCCN2)O SPLBRAKYXGOFSO-UNQGMJICSA-N 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 208000000236 Prostatic Neoplasms Diseases 0.000 description 1
- 241000700157 Rattus norvegicus Species 0.000 description 1
- 208000015634 Rectal Neoplasms Diseases 0.000 description 1
- 208000006265 Renal cell carcinoma Diseases 0.000 description 1
- 201000010208 Seminoma Diseases 0.000 description 1
- YMTLKLXDFCSCNX-BYPYZUCNSA-N Ser-Gly-Gly Chemical compound OC[C@H](N)C(=O)NCC(=O)NCC(O)=O YMTLKLXDFCSCNX-BYPYZUCNSA-N 0.000 description 1
- IFPBAGJBHSNYPR-ZKWXMUAHSA-N Ser-Ile-Gly Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(O)=O IFPBAGJBHSNYPR-ZKWXMUAHSA-N 0.000 description 1
- HEUVHBXOVZONPU-BJDJZHNGSA-N Ser-Leu-Ile Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)CC)C(O)=O HEUVHBXOVZONPU-BJDJZHNGSA-N 0.000 description 1
- QNBVFKZSSRYNFX-CUJWVEQBSA-N Ser-Thr-His Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CC1=CN=CN1)C(=O)O)NC(=O)[C@H](CO)N)O QNBVFKZSSRYNFX-CUJWVEQBSA-N 0.000 description 1
- ZKOKTQPHFMRSJP-YJRXYDGGSA-N Ser-Thr-Tyr Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O ZKOKTQPHFMRSJP-YJRXYDGGSA-N 0.000 description 1
- 108010003723 Single-Domain Antibodies Proteins 0.000 description 1
- 208000000453 Skin Neoplasms Diseases 0.000 description 1
- 208000000102 Squamous Cell Carcinoma of Head and Neck Diseases 0.000 description 1
- 208000005718 Stomach Neoplasms Diseases 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- 241000282898 Sus scrofa Species 0.000 description 1
- 229940123237 Taxane Drugs 0.000 description 1
- 206010043276 Teratoma Diseases 0.000 description 1
- IGROJMCBGRFRGI-YTLHQDLWSA-N Thr-Ala-Ala Chemical compound C[C@@H](O)[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(O)=O IGROJMCBGRFRGI-YTLHQDLWSA-N 0.000 description 1
- CTONFVDJYCAMQM-IUKAMOBKSA-N Thr-Asn-Ile Chemical compound CC[C@H](C)[C@@H](C(=O)O)NC(=O)[C@H](CC(=O)N)NC(=O)[C@H]([C@@H](C)O)N CTONFVDJYCAMQM-IUKAMOBKSA-N 0.000 description 1
- VBMOVTMNHWPZJR-SUSMZKCASA-N Thr-Thr-Glu Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCC(O)=O)C(O)=O VBMOVTMNHWPZJR-SUSMZKCASA-N 0.000 description 1
- VGNLMPBYWWNQFS-ZEILLAHLSA-N Thr-Thr-His Chemical compound C[C@H]([C@@H](C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC1=CN=CN1)C(=O)O)N)O VGNLMPBYWWNQFS-ZEILLAHLSA-N 0.000 description 1
- XVHAUVJXBFGUPC-RPTUDFQQSA-N Thr-Tyr-Phe Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC1=CC=CC=C1)C(O)=O XVHAUVJXBFGUPC-RPTUDFQQSA-N 0.000 description 1
- PWONLXBUSVIZPH-RHYQMDGZSA-N Thr-Val-Lys Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)O)N)O PWONLXBUSVIZPH-RHYQMDGZSA-N 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 208000024770 Thyroid neoplasm Diseases 0.000 description 1
- 206010052779 Transplant rejections Diseases 0.000 description 1
- IKUMWSDCGQVGHC-UMPQAUOISA-N Trp-Pro-Thr Chemical compound C[C@H]([C@@H](C(=O)O)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CC2=CNC3=CC=CC=C32)N)O IKUMWSDCGQVGHC-UMPQAUOISA-N 0.000 description 1
- IELISNUVHBKYBX-XDTLVQLUSA-N Tyr-Ala-Glu Chemical compound OC(=O)CC[C@@H](C(O)=O)NC(=O)[C@H](C)NC(=O)[C@@H](N)CC1=CC=C(O)C=C1 IELISNUVHBKYBX-XDTLVQLUSA-N 0.000 description 1
- LGEYOIQBBIPHQN-UWJYBYFXSA-N Tyr-Ala-Ser Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](C)NC(=O)[C@@H](N)CC1=CC=C(O)C=C1 LGEYOIQBBIPHQN-UWJYBYFXSA-N 0.000 description 1
- VTFWAGGJDRSQFG-MELADBBJSA-N Tyr-Asn-Pro Chemical compound C1C[C@@H](N(C1)C(=O)[C@H](CC(=O)N)NC(=O)[C@H](CC2=CC=C(C=C2)O)N)C(=O)O VTFWAGGJDRSQFG-MELADBBJSA-N 0.000 description 1
- ZNFPUOSTMUMUDR-JRQIVUDYSA-N Tyr-Asn-Thr Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O ZNFPUOSTMUMUDR-JRQIVUDYSA-N 0.000 description 1
- HDSKHCBAVVWPCQ-FHWLQOOXSA-N Tyr-Glu-Phe Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC1=CC=CC=C1)C(O)=O HDSKHCBAVVWPCQ-FHWLQOOXSA-N 0.000 description 1
- YKCXQOBTISTQJD-BZSNNMDCSA-N Tyr-Leu-His Chemical compound CC(C)C[C@@H](C(=O)N[C@@H](CC1=CN=CN1)C(=O)O)NC(=O)[C@H](CC2=CC=C(C=C2)O)N YKCXQOBTISTQJD-BZSNNMDCSA-N 0.000 description 1
- XJPXTYLVMUZGNW-IHRRRGAJSA-N Tyr-Pro-Asp Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CC(O)=O)C(O)=O XJPXTYLVMUZGNW-IHRRRGAJSA-N 0.000 description 1
- GQVZBMROTPEPIF-SRVKXCTJSA-N Tyr-Ser-Asp Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(O)=O)C(O)=O GQVZBMROTPEPIF-SRVKXCTJSA-N 0.000 description 1
- OJCISMMNNUNNJA-BZSNNMDCSA-N Tyr-Tyr-Asp Chemical compound C([C@H](N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CC(O)=O)C(O)=O)C1=CC=C(O)C=C1 OJCISMMNNUNNJA-BZSNNMDCSA-N 0.000 description 1
- 208000002495 Uterine Neoplasms Diseases 0.000 description 1
- NXRAUQGGHPCJIB-RCOVLWMOSA-N Val-Gly-Asn Chemical compound CC(C)[C@H](N)C(=O)NCC(=O)N[C@@H](CC(N)=O)C(O)=O NXRAUQGGHPCJIB-RCOVLWMOSA-N 0.000 description 1
- MYLNLEIZWHVENT-VKOGCVSHSA-N Val-Ile-Trp Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CC1=CNC2=CC=CC=C21)C(=O)O)NC(=O)[C@H](C(C)C)N MYLNLEIZWHVENT-VKOGCVSHSA-N 0.000 description 1
- NSUUANXHLKKHQB-BZSNNMDCSA-N Val-Pro-Trp Chemical compound CC(C)[C@H](N)C(=O)N1CCC[C@H]1C(=O)N[C@H](C(O)=O)CC1=CNC2=CC=CC=C12 NSUUANXHLKKHQB-BZSNNMDCSA-N 0.000 description 1
- 238000005411 Van der Waals force Methods 0.000 description 1
- 229940122803 Vinca alkaloid Drugs 0.000 description 1
- 208000036142 Viral infection Diseases 0.000 description 1
- 108010081404 acein-2 Proteins 0.000 description 1
- 125000002777 acetyl group Chemical group [H]C([H])([H])C(*)=O 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 201000005188 adrenal gland cancer Diseases 0.000 description 1
- 208000024447 adrenal gland neoplasm Diseases 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 108010087924 alanylproline Proteins 0.000 description 1
- 108010070783 alanyltyrosine Proteins 0.000 description 1
- 229930013930 alkaloid Natural products 0.000 description 1
- 229940100198 alkylating agent Drugs 0.000 description 1
- 239000002168 alkylating agent Substances 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 125000000129 anionic group Chemical group 0.000 description 1
- 230000000340 anti-metabolite Effects 0.000 description 1
- 230000000118 anti-neoplastic effect Effects 0.000 description 1
- 230000009830 antibody antigen interaction Effects 0.000 description 1
- 238000009175 antibody therapy Methods 0.000 description 1
- 229940100197 antimetabolite Drugs 0.000 description 1
- 239000002256 antimetabolite Substances 0.000 description 1
- 229940034982 antineoplastic agent Drugs 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 230000003078 antioxidant effect Effects 0.000 description 1
- 108010069205 aspartyl-phenylalanine Proteins 0.000 description 1
- 108010047857 aspartylglycine Proteins 0.000 description 1
- 108010092854 aspartyllysine Proteins 0.000 description 1
- 238000011717 athymic nude mouse Methods 0.000 description 1
- 238000010170 biological method Methods 0.000 description 1
- 230000006696 biosynthetic metabolic pathway Effects 0.000 description 1
- 239000006172 buffering agent Substances 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 238000004364 calculation method Methods 0.000 description 1
- 238000011088 calibration curve Methods 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 239000006143 cell culture medium Substances 0.000 description 1
- 230000022534 cell killing Effects 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000002512 chemotherapy Methods 0.000 description 1
- DQLATGHUWYMOKM-UHFFFAOYSA-L cisplatin Chemical compound N[Pt](N)(Cl)Cl DQLATGHUWYMOKM-UHFFFAOYSA-L 0.000 description 1
- 229960004316 cisplatin Drugs 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000013377 clone selection method Methods 0.000 description 1
- 201000010897 colon adenocarcinoma Diseases 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 230000004154 complement system Effects 0.000 description 1
- 239000008139 complexing agent Substances 0.000 description 1
- 230000001268 conjugating effect Effects 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 210000000805 cytoplasm Anatomy 0.000 description 1
- 230000003013 cytotoxicity Effects 0.000 description 1
- 231100000135 cytotoxicity Toxicity 0.000 description 1
- 238000002784 cytotoxicity assay Methods 0.000 description 1
- 231100000263 cytotoxicity test Toxicity 0.000 description 1
- 239000002619 cytotoxin Substances 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 230000003831 deregulation Effects 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 230000001627 detrimental effect Effects 0.000 description 1
- 238000006471 dimerization reaction Methods 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 239000003534 dna topoisomerase inhibitor Substances 0.000 description 1
- 229960004679 doxorubicin Drugs 0.000 description 1
- 239000003937 drug carrier Substances 0.000 description 1
- 238000012377 drug delivery Methods 0.000 description 1
- 230000009881 electrostatic interaction Effects 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- YJGVMLPVUAXIQN-UHFFFAOYSA-N epipodophyllotoxin Natural products COC1=C(OC)C(OC)=CC(C2C3=CC=4OCOC=4C=C3C(O)C3C2C(OC3)=O)=C1 YJGVMLPVUAXIQN-UHFFFAOYSA-N 0.000 description 1
- 210000002919 epithelial cell Anatomy 0.000 description 1
- 201000004101 esophageal cancer Diseases 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 238000013210 evaluation model Methods 0.000 description 1
- 101150029401 fmnl3 gene Proteins 0.000 description 1
- 101150023212 fut8 gene Proteins 0.000 description 1
- 206010017758 gastric cancer Diseases 0.000 description 1
- 238000003197 gene knockdown Methods 0.000 description 1
- 238000003209 gene knockout Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 229940050410 gluconate Drugs 0.000 description 1
- 108010089804 glycyl-threonine Proteins 0.000 description 1
- 108010037850 glycylvaline Proteins 0.000 description 1
- 239000008187 granular material Substances 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 201000003911 head and neck carcinoma Diseases 0.000 description 1
- 201000000459 head and neck squamous cell carcinoma Diseases 0.000 description 1
- 201000005787 hematologic cancer Diseases 0.000 description 1
- 208000024200 hematopoietic and lymphoid system neoplasm Diseases 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 230000008105 immune reaction Effects 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 208000027866 inflammatory disease Diseases 0.000 description 1
- 230000004068 intracellular signaling Effects 0.000 description 1
- 238000007917 intracranial administration Methods 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 238000007913 intrathecal administration Methods 0.000 description 1
- 230000009545 invasion Effects 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- BQINXKOTJQCISL-GRCPKETISA-N keto-neuraminic acid Chemical class OC(=O)C(=O)C[C@H](O)[C@@H](N)[C@@H](O)[C@H](O)[C@H](O)CO BQINXKOTJQCISL-GRCPKETISA-N 0.000 description 1
- 230000002045 lasting effect Effects 0.000 description 1
- 108010073472 leucyl-prolyl-proline Proteins 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 201000007270 liver cancer Diseases 0.000 description 1
- 208000014018 liver neoplasm Diseases 0.000 description 1
- 201000005249 lung adenocarcinoma Diseases 0.000 description 1
- 201000005296 lung carcinoma Diseases 0.000 description 1
- 210000005265 lung cell Anatomy 0.000 description 1
- 201000010453 lymph node cancer Diseases 0.000 description 1
- 239000012139 lysis buffer Substances 0.000 description 1
- 239000001115 mace Substances 0.000 description 1
- 208000002780 macular degeneration Diseases 0.000 description 1
- 239000011777 magnesium Substances 0.000 description 1
- 229910052749 magnesium Inorganic materials 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 208000015486 malignant pancreatic neoplasm Diseases 0.000 description 1
- 208000026037 malignant tumor of neck Diseases 0.000 description 1
- 229910052748 manganese Inorganic materials 0.000 description 1
- 239000011572 manganese Substances 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 238000000691 measurement method Methods 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 201000001441 melanoma Diseases 0.000 description 1
- 206010061289 metastatic neoplasm Diseases 0.000 description 1
- 230000011987 methylation Effects 0.000 description 1
- 238000007069 methylation reaction Methods 0.000 description 1
- 230000002438 mitochondrial effect Effects 0.000 description 1
- 229940125645 monoclonal antibody drug Drugs 0.000 description 1
- 201000006417 multiple sclerosis Diseases 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- VMGAPWLDMVPYIA-HIDZBRGKSA-N n'-amino-n-iminomethanimidamide Chemical compound N\N=C\N=N VMGAPWLDMVPYIA-HIDZBRGKSA-N 0.000 description 1
- 210000000822 natural killer cell Anatomy 0.000 description 1
- 231100000956 nontoxicity Toxicity 0.000 description 1
- 231100000590 oncogenic Toxicity 0.000 description 1
- 230000002246 oncogenic effect Effects 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 230000008520 organization Effects 0.000 description 1
- 239000003002 pH adjusting agent Substances 0.000 description 1
- 230000020477 pH reduction Effects 0.000 description 1
- 208000008443 pancreatic carcinoma Diseases 0.000 description 1
- 229940124531 pharmaceutical excipient Drugs 0.000 description 1
- 230000000144 pharmacologic effect Effects 0.000 description 1
- 108010024607 phenylalanylalanine Proteins 0.000 description 1
- 108010073025 phenylalanylphenylalanine Proteins 0.000 description 1
- 108010051242 phenylalanylserine Proteins 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 239000002953 phosphate buffered saline Substances 0.000 description 1
- 238000003566 phosphorylation assay Methods 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 229910052697 platinum Inorganic materials 0.000 description 1
- 229960001237 podophyllotoxin Drugs 0.000 description 1
- YJGVMLPVUAXIQN-XVVDYKMHSA-N podophyllotoxin Chemical compound COC1=C(OC)C(OC)=CC([C@@H]2C3=CC=4OCOC=4C=C3[C@H](O)[C@@H]3[C@@H]2C(OC3)=O)=C1 YJGVMLPVUAXIQN-XVVDYKMHSA-N 0.000 description 1
- YVCVYCSAAZQOJI-UHFFFAOYSA-N podophyllotoxin Natural products COC1=C(O)C(OC)=CC(C2C3=CC=4OCOC=4C=C3C(O)C3C2C(OC3)=O)=C1 YVCVYCSAAZQOJI-UHFFFAOYSA-N 0.000 description 1
- 229920000768 polyamine Polymers 0.000 description 1
- 239000011591 potassium Substances 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000002335 preservative effect Effects 0.000 description 1
- 229940002612 prodrug Drugs 0.000 description 1
- 239000000651 prodrug Substances 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 239000012521 purified sample Substances 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 238000007420 radioactive assay Methods 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 206010038038 rectal cancer Diseases 0.000 description 1
- 201000001275 rectum cancer Diseases 0.000 description 1
- BOLDJAUMGUJJKM-LSDHHAIUSA-N renifolin D Natural products CC(=C)[C@@H]1Cc2c(O)c(O)ccc2[C@H]1CC(=O)c3ccc(O)cc3O BOLDJAUMGUJJKM-LSDHHAIUSA-N 0.000 description 1
- 231100000191 repeated dose toxicity Toxicity 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 238000004366 reverse phase liquid chromatography Methods 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 229960004641 rituximab Drugs 0.000 description 1
- 229920002477 rna polymer Polymers 0.000 description 1
- 102200006532 rs112445441 Human genes 0.000 description 1
- 102220053950 rs121913238 Human genes 0.000 description 1
- 102200006520 rs121913240 Human genes 0.000 description 1
- 102200006531 rs121913529 Human genes 0.000 description 1
- 102200006538 rs121913530 Human genes 0.000 description 1
- 102200006540 rs121913530 Human genes 0.000 description 1
- 102200006541 rs121913530 Human genes 0.000 description 1
- 102200006533 rs121913535 Human genes 0.000 description 1
- 102200007373 rs17851045 Human genes 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 239000000523 sample Substances 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 108010071207 serylmethionine Proteins 0.000 description 1
- 230000011664 signaling Effects 0.000 description 1
- 201000000849 skin cancer Diseases 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000008247 solid mixture Substances 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 201000011549 stomach cancer Diseases 0.000 description 1
- 150000003467 sulfuric acid derivatives Chemical class 0.000 description 1
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 150000003505 terpenes Chemical class 0.000 description 1
- 125000003831 tetrazolyl group Chemical group 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 108010033670 threonyl-aspartyl-tyrosine Proteins 0.000 description 1
- 201000002510 thyroid cancer Diseases 0.000 description 1
- 239000008181 tonicity modifier Substances 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 229940044693 topoisomerase inhibitor Drugs 0.000 description 1
- 229960000303 topotecan Drugs 0.000 description 1
- UCFGDBYHRUNTLO-QHCPKHFHSA-N topotecan Chemical compound C1=C(O)C(CN(C)C)=C2C=C(CN3C4=CC5=C(C3=O)COC(=O)[C@]5(O)CC)C4=NC2=C1 UCFGDBYHRUNTLO-QHCPKHFHSA-N 0.000 description 1
- 231100000583 toxicological profile Toxicity 0.000 description 1
- 231100000027 toxicology Toxicity 0.000 description 1
- 206010044412 transitional cell carcinoma Diseases 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- 229960000575 trastuzumab Drugs 0.000 description 1
- 238000007492 two-way ANOVA Methods 0.000 description 1
- 108010077037 tyrosyl-tyrosyl-phenylalanine Proteins 0.000 description 1
- 108010003137 tyrosyltyrosine Proteins 0.000 description 1
- 206010046766 uterine cancer Diseases 0.000 description 1
- -1 vinca alkaloids Natural products 0.000 description 1
- 230000009385 viral infection Effects 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 239000000080 wetting agent Substances 0.000 description 1
- 238000012447 xenograft mouse model Methods 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
Classifications
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
-
- 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
-
- 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
- C07K16/30—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants from tumour cells
- C07K16/3076—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants from tumour cells against structure-related tumour-associated moieties
- C07K16/3092—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants from tumour cells against structure-related tumour-associated moieties against tumour-associated mucins
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/40—Immunoglobulins specific features characterized by post-translational modification
- C07K2317/41—Glycosylation, sialylation, or fucosylation
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/55—Fab or Fab'
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
- C07K2317/732—Antibody-dependent cellular cytotoxicity [ADCC]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/92—Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/94—Stability, e.g. half-life, pH, temperature or enzyme-resistance
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Immunology (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Cell Biology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- General Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP2010004878 | 2010-08-10 | ||
| PCT/EP2011/063791 WO2012020065A1 (en) | 2010-08-10 | 2011-08-10 | Fab-glycosylated antibodies |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| DK2603528T3 true DK2603528T3 (en) | 2016-11-28 |
Family
ID=44674756
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DK11760415.7T DK2603528T3 (en) | 2010-08-10 | 2011-08-10 | FAB-glycosylated ANTIBODIES |
Country Status (12)
| Country | Link |
|---|---|
| US (1) | US9359439B2 (enExample) |
| EP (1) | EP2603528B1 (enExample) |
| JP (2) | JP6334166B2 (enExample) |
| CN (1) | CN103119064B (enExample) |
| AU (1) | AU2011288464B2 (enExample) |
| BR (1) | BR112013003095B1 (enExample) |
| CA (1) | CA2805984C (enExample) |
| DK (1) | DK2603528T3 (enExample) |
| ES (1) | ES2605304T3 (enExample) |
| PL (1) | PL2603528T3 (enExample) |
| PT (1) | PT2603528T (enExample) |
| WO (1) | WO2012020065A1 (enExample) |
Families Citing this family (18)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US9051370B2 (en) | 2010-08-10 | 2015-06-09 | Glycotope Gmbh | Humanized EGFR antibodies |
| UY34317A (es) | 2011-09-12 | 2013-02-28 | Genzyme Corp | Anticuerpo antireceptor de célula T (alfa)/ß |
| US9790268B2 (en) | 2012-09-12 | 2017-10-17 | Genzyme Corporation | Fc containing polypeptides with altered glycosylation and reduced effector function |
| KR102420934B1 (ko) | 2013-03-11 | 2022-07-15 | 젠자임 코포레이션 | 과글리코실화된 결합 폴리펩티드 |
| US9217168B2 (en) | 2013-03-14 | 2015-12-22 | Momenta Pharmaceuticals, Inc. | Methods of cell culture |
| CN105229030A (zh) * | 2013-04-22 | 2016-01-06 | 葛莱高托普有限公司 | 用具有低岩藻糖基化的抗-egfr抗体的抗-癌治疗 |
| EP4640239A2 (en) | 2014-03-19 | 2025-10-29 | Genzyme Corporation | Site-specific glycoengineering of targeting moieties |
| CN114181312A (zh) * | 2014-09-10 | 2022-03-15 | 豪夫迈·罗氏有限公司 | 半乳糖改造的免疫球蛋白1抗体 |
| CA2944085C (en) * | 2014-09-16 | 2018-04-10 | Ease Charm Limited | Anti-egfr antibody and uses of same |
| PL3204425T3 (pl) | 2014-10-09 | 2021-03-08 | Genzyme Corporation | Glikomodyfikowane koniugaty przeciwciał z lekami |
| EP3271391A1 (en) * | 2015-03-20 | 2018-01-24 | Ablynx N.V. | Glycosylated immunoglobulin single variable domains |
| WO2017162733A1 (en) * | 2016-03-22 | 2017-09-28 | Glycotope Gmbh | Iga antibodies with enhanced stability |
| CA3050039A1 (en) * | 2017-01-27 | 2018-08-02 | Glycotope Gmbh | Anti-cancer treatments with an anti-muc1 antibody and an erbb inhibitor |
| CN110352074B (zh) | 2017-02-28 | 2024-07-16 | 思进股份有限公司 | 用于偶联的半胱氨酸突变抗体 |
| EP3707167A4 (en) * | 2017-11-09 | 2021-08-04 | National Research Council of Canada | ANTIBODY GLYCOCONJUGATES, PRODUCTION AND USE PROCESSES |
| BR112020023373A2 (pt) | 2018-05-18 | 2021-02-09 | Daiichi Sankyo Company, Limited | conjugado, composição, e, uso de um conjugado ou de uma composição |
| EP3947458A1 (en) | 2019-04-03 | 2022-02-09 | Genzyme Corporation | Anti-alpha beta tcr binding polypeptides with reduced fragmentation |
| CA3196014A1 (en) * | 2020-09-21 | 2022-03-24 | Systimmune, Inc. | Specificity enchanced bispecific antibody (seba) |
Family Cites Families (22)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4943533A (en) | 1984-03-01 | 1990-07-24 | The Regents Of The University Of California | Hybrid cell lines that produce monoclonal antibodies to epidermal growth factor receptor |
| GB9200415D0 (en) | 1992-01-09 | 1992-02-26 | Bagshawe Kenneth D | Inactivation of cytotoxic drugs |
| US5443953A (en) * | 1993-12-08 | 1995-08-22 | Immunomedics, Inc. | Preparation and use of immunoconjugates |
| AU6267896A (en) | 1995-06-07 | 1996-12-30 | Imclone Systems Incorporated | Antibody and antibody fragments for inhibiting the growth oftumors |
| US6172213B1 (en) * | 1997-07-02 | 2001-01-09 | Genentech, Inc. | Anti-IgE antibodies and method of improving polypeptides |
| US20040192898A1 (en) | 2001-08-17 | 2004-09-30 | Jia Audrey Yunhua | Anti-abeta antibodies |
| WO2003074679A2 (en) | 2002-03-01 | 2003-09-12 | Xencor | Antibody optimization |
| DE10303664A1 (de) | 2003-01-23 | 2004-08-12 | Nemod Immuntherapie Ag | Erkennungsmoleküle zur Behandlung und Detektion von Tumoren |
| EP1706079B1 (en) * | 2003-08-14 | 2013-02-20 | ThromboGenics N.V. | Antibodies against factor viii with modified glycosylation in the variable region |
| WO2005017130A2 (en) | 2003-08-18 | 2005-02-24 | Glycotope Gmbh | Tumour cell lines nm-f9 (dsm acc2606) and nm-d4 (dsm acc2605), uses thereof |
| JP4913604B2 (ja) | 2004-02-13 | 2012-04-11 | グリコトープ ゲーエムベーハー | 高活性糖タンパク質−製造条件、及びその効率的製造方法 |
| US20060051353A1 (en) * | 2004-05-14 | 2006-03-09 | Jean-Frederic Colombel | Methods and compositions to evaluate antibody treatment response |
| CA2607663C (en) | 2005-05-19 | 2014-08-12 | Amgen Inc. | Compositions and methods for increasing the stability of antibodies |
| WO2007005786A2 (en) | 2005-06-30 | 2007-01-11 | Centocor, Inc. | Methods and compositions with enhanced therapeutic activity |
| GB0519398D0 (en) * | 2005-09-23 | 2005-11-02 | Antisoma Plc | Biological materials and uses thereof |
| CA2631630A1 (en) * | 2005-11-30 | 2007-06-07 | University Of Southern California | Fc.gamma. polymorphisms for predicting disease and treatment outcome |
| HRP20150307T1 (hr) * | 2006-09-10 | 2015-04-24 | Glycotope Gmbh | Upotreba ljudskih stanica podrijetlom iz ljudske leukemije za eksprimiranje protutijela |
| WO2008101177A2 (en) | 2007-02-16 | 2008-08-21 | University Of Virginia Patent Foundation | Ige antibodies to chimeric or humanized igg therapeutic monoclonal antibodies as a screening test for anaphylaxis |
| CA2720610C (en) * | 2008-04-07 | 2016-08-23 | Bayer Healthcare Llc | Methods of recombinant production of glycoproteins |
| AU2009256246B2 (en) * | 2008-06-03 | 2013-07-18 | Abbvie Inc. | Dual variable domain immunoglobulins and uses thereof |
| EP2281844A1 (en) | 2009-07-31 | 2011-02-09 | Glycotope GmbH | MUC 1 antibodies |
| US9051370B2 (en) * | 2010-08-10 | 2015-06-09 | Glycotope Gmbh | Humanized EGFR antibodies |
-
2011
- 2011-08-10 WO PCT/EP2011/063791 patent/WO2012020065A1/en not_active Ceased
- 2011-08-10 JP JP2013523612A patent/JP6334166B2/ja active Active
- 2011-08-10 PT PT117604157T patent/PT2603528T/pt unknown
- 2011-08-10 AU AU2011288464A patent/AU2011288464B2/en active Active
- 2011-08-10 PL PL11760415T patent/PL2603528T3/pl unknown
- 2011-08-10 CN CN201180039635.7A patent/CN103119064B/zh active Active
- 2011-08-10 US US13/816,390 patent/US9359439B2/en active Active
- 2011-08-10 BR BR112013003095-0A patent/BR112013003095B1/pt active IP Right Grant
- 2011-08-10 ES ES11760415.7T patent/ES2605304T3/es active Active
- 2011-08-10 EP EP11760415.7A patent/EP2603528B1/en active Active
- 2011-08-10 DK DK11760415.7T patent/DK2603528T3/en active
- 2011-08-10 CA CA2805984A patent/CA2805984C/en active Active
-
2016
- 2016-07-29 JP JP2016149616A patent/JP2016185169A/ja not_active Withdrawn
Also Published As
| Publication number | Publication date |
|---|---|
| JP6334166B2 (ja) | 2018-05-30 |
| AU2011288464A1 (en) | 2013-02-14 |
| CN103119064A (zh) | 2013-05-22 |
| BR112013003095A2 (pt) | 2016-07-05 |
| PT2603528T (pt) | 2016-12-01 |
| US20130209458A1 (en) | 2013-08-15 |
| ES2605304T3 (es) | 2017-03-13 |
| WO2012020065A1 (en) | 2012-02-16 |
| JP2016185169A (ja) | 2016-10-27 |
| US9359439B2 (en) | 2016-06-07 |
| AU2011288464B2 (en) | 2015-10-29 |
| EP2603528B1 (en) | 2016-10-12 |
| EP2603528A1 (en) | 2013-06-19 |
| CA2805984A1 (en) | 2012-02-16 |
| BR112013003095B1 (pt) | 2023-03-28 |
| JP2013535970A (ja) | 2013-09-19 |
| CA2805984C (en) | 2021-05-25 |
| CN103119064B (zh) | 2018-09-04 |
| PL2603528T3 (pl) | 2017-07-31 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| DK2603528T3 (en) | FAB-glycosylated ANTIBODIES | |
| JP7502402B2 (ja) | 抗muc1抗体-薬物コンジュゲート | |
| KR102755090B1 (ko) | 과글리코실화된 결합 폴리펩티드 | |
| CN117440973A (zh) | 与ror1结合的抗原结合蛋白 | |
| CN120187759A (zh) | 抗gucy2c抗体及其用途 | |
| RU2804703C2 (ru) | Конъюгат антитело против muc1-лекарственное средство | |
| RU2792347C2 (ru) | Антитело против muc1 | |
| HK40038925B (en) | Anti-muc1- exatecan antibody-drug conjugate | |
| HK40038925A (en) | Anti-muc1- exatecan antibody-drug conjugate | |
| HK40041660A (en) | Anti-muc1 antibody |