JP2010511397A - 血清タンパク質と結合可能なペプチド - Google Patents
血清タンパク質と結合可能なペプチド Download PDFInfo
- Publication number
- JP2010511397A JP2010511397A JP2009539745A JP2009539745A JP2010511397A JP 2010511397 A JP2010511397 A JP 2010511397A JP 2009539745 A JP2009539745 A JP 2009539745A JP 2009539745 A JP2009539745 A JP 2009539745A JP 2010511397 A JP2010511397 A JP 2010511397A
- Authority
- JP
- Japan
- Prior art keywords
- amino acid
- sequence
- acid sequence
- sequences
- immunoglobulin
- 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.)
- Withdrawn
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 210
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 155
- 102000004506 Blood Proteins Human genes 0.000 title claims abstract description 131
- 108010017384 Blood Proteins Proteins 0.000 title claims abstract description 131
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract description 645
- 150000001875 compounds Chemical class 0.000 claims abstract description 191
- 230000027455 binding Effects 0.000 claims abstract description 171
- 229920001184 polypeptide Polymers 0.000 claims abstract description 135
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 111
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 106
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 73
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 42
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 42
- 230000004927 fusion Effects 0.000 claims abstract description 25
- 239000008194 pharmaceutical composition Substances 0.000 claims abstract description 15
- 108060003951 Immunoglobulin Proteins 0.000 claims description 263
- 102000018358 immunoglobulin Human genes 0.000 claims description 263
- 238000000034 method Methods 0.000 claims description 255
- 239000012634 fragment Substances 0.000 claims description 163
- 125000000539 amino acid group Chemical group 0.000 claims description 128
- 235000001014 amino acid Nutrition 0.000 claims description 114
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 107
- 108091006905 Human Serum Albumin Proteins 0.000 claims description 104
- 102000008100 Human Serum Albumin Human genes 0.000 claims description 104
- 230000001225 therapeutic effect Effects 0.000 claims description 103
- 102000007562 Serum Albumin Human genes 0.000 claims description 102
- 108010071390 Serum Albumin Proteins 0.000 claims description 102
- 235000018102 proteins Nutrition 0.000 claims description 100
- 239000002773 nucleotide Substances 0.000 claims description 96
- 125000003729 nucleotide group Chemical group 0.000 claims description 96
- 150000001413 amino acids Chemical class 0.000 claims description 85
- 108091007433 antigens Proteins 0.000 claims description 58
- 102000036639 antigens Human genes 0.000 claims description 58
- 239000000427 antigen Substances 0.000 claims description 57
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 claims description 51
- 210000004027 cell Anatomy 0.000 claims description 48
- 238000012216 screening Methods 0.000 claims description 42
- 210000002966 serum Anatomy 0.000 claims description 37
- 108010003723 Single-Domain Antibodies Proteins 0.000 claims description 34
- 102100026120 IgG receptor FcRn large subunit p51 Human genes 0.000 claims description 27
- 102100035361 Cerebellar degeneration-related protein 2 Human genes 0.000 claims description 26
- 101000737796 Homo sapiens Cerebellar degeneration-related protein 2 Proteins 0.000 claims description 26
- 101710177940 IgG receptor FcRn large subunit p51 Proteins 0.000 claims description 26
- 230000028993 immune response Effects 0.000 claims description 24
- 125000006850 spacer group Chemical group 0.000 claims description 21
- 241000124008 Mammalia Species 0.000 claims description 19
- 230000003321 amplification Effects 0.000 claims description 18
- 238000003199 nucleic acid amplification method Methods 0.000 claims description 18
- 102000008946 Fibrinogen Human genes 0.000 claims description 17
- 108010049003 Fibrinogen Proteins 0.000 claims description 17
- 102000009488 Thyroxine-Binding Proteins Human genes 0.000 claims description 17
- 108010048889 Thyroxine-Binding Proteins Proteins 0.000 claims description 17
- 102000004338 Transferrin Human genes 0.000 claims description 17
- 108090000901 Transferrin Proteins 0.000 claims description 17
- 230000009824 affinity maturation Effects 0.000 claims description 17
- 229940012952 fibrinogen Drugs 0.000 claims description 17
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims description 17
- 239000012581 transferrin Substances 0.000 claims description 17
- 238000004519 manufacturing process Methods 0.000 claims description 16
- 238000006467 substitution reaction Methods 0.000 claims description 16
- 229940072221 immunoglobulins Drugs 0.000 claims description 15
- 241001465754 Metazoa Species 0.000 claims description 13
- 238000011282 treatment Methods 0.000 claims description 12
- GOJUJUVQIVIZAV-UHFFFAOYSA-N 2-amino-4,6-dichloropyrimidine-5-carbaldehyde Chemical group NC1=NC(Cl)=C(C=O)C(Cl)=N1 GOJUJUVQIVIZAV-UHFFFAOYSA-N 0.000 claims description 11
- 108010021625 Immunoglobulin Fragments Proteins 0.000 claims description 10
- 102000008394 Immunoglobulin Fragments Human genes 0.000 claims description 10
- 244000005700 microbiome Species 0.000 claims description 10
- 230000002829 reductive effect Effects 0.000 claims description 10
- 238000007792 addition Methods 0.000 claims description 8
- 239000003085 diluting agent Substances 0.000 claims description 8
- 239000000546 pharmaceutical excipient Substances 0.000 claims description 8
- 239000003937 drug carrier Substances 0.000 claims description 7
- 230000036039 immunity Effects 0.000 claims description 7
- 238000003780 insertion Methods 0.000 claims description 7
- 230000037431 insertion Effects 0.000 claims description 7
- 238000001943 fluorescence-activated cell sorting Methods 0.000 claims description 5
- 210000003719 b-lymphocyte Anatomy 0.000 claims description 4
- 230000015572 biosynthetic process Effects 0.000 claims description 4
- 238000012258 culturing Methods 0.000 claims description 4
- 230000008569 process Effects 0.000 claims description 4
- 238000000684 flow cytometry Methods 0.000 claims description 3
- 102100024952 Protein CBFA2T1 Human genes 0.000 claims 63
- 101100112922 Candida albicans CDR3 gene Proteins 0.000 claims 12
- 230000001900 immune effect Effects 0.000 claims 3
- 241000282832 Camelidae Species 0.000 claims 2
- 108020004705 Codon Proteins 0.000 claims 1
- 102000006395 Globulins Human genes 0.000 claims 1
- 108010044091 Globulins Proteins 0.000 claims 1
- 102000037865 fusion proteins Human genes 0.000 abstract description 76
- 108020001507 fusion proteins Proteins 0.000 abstract description 76
- 239000000203 mixture Substances 0.000 abstract description 11
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 59
- 239000013615 primer Substances 0.000 description 42
- 239000003814 drug Substances 0.000 description 39
- 230000000670 limiting effect Effects 0.000 description 34
- 229940124597 therapeutic agent Drugs 0.000 description 33
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 27
- 238000010494 dissociation reaction Methods 0.000 description 25
- 230000005593 dissociations Effects 0.000 description 25
- 102000009027 Albumins Human genes 0.000 description 20
- 108010088751 Albumins Proteins 0.000 description 20
- 201000010099 disease Diseases 0.000 description 20
- 108010058846 Ovalbumin Proteins 0.000 description 14
- 235000002198 Annona diversifolia Nutrition 0.000 description 13
- 229940092253 ovalbumin Drugs 0.000 description 13
- 241000282842 Lama glama Species 0.000 description 12
- 230000003993 interaction Effects 0.000 description 12
- 238000012552 review Methods 0.000 description 12
- 238000004458 analytical method Methods 0.000 description 10
- 230000000890 antigenic effect Effects 0.000 description 10
- 241001524679 Escherichia virus M13 Species 0.000 description 9
- 230000037396 body weight Effects 0.000 description 9
- 241000282567 Macaca fascicularis Species 0.000 description 8
- 238000005259 measurement Methods 0.000 description 8
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 description 8
- 241001504519 Papio ursinus Species 0.000 description 7
- 102000025171 antigen binding proteins Human genes 0.000 description 7
- 108091000831 antigen binding proteins Proteins 0.000 description 7
- 208000035475 disorder Diseases 0.000 description 7
- 230000009871 nonspecific binding Effects 0.000 description 7
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 6
- 238000002965 ELISA Methods 0.000 description 6
- 241000282553 Macaca Species 0.000 description 6
- 241000699666 Mus <mouse, genus> Species 0.000 description 6
- 241000288906 Primates Species 0.000 description 6
- 230000000903 blocking effect Effects 0.000 description 6
- 231100000673 dose–response relationship Toxicity 0.000 description 6
- 238000010647 peptide synthesis reaction Methods 0.000 description 6
- 210000003705 ribosome Anatomy 0.000 description 6
- 238000011269 treatment regimen Methods 0.000 description 6
- 241000282412 Homo Species 0.000 description 5
- 241000282838 Lama Species 0.000 description 5
- 238000013459 approach Methods 0.000 description 5
- 229960002685 biotin Drugs 0.000 description 5
- 239000011616 biotin Substances 0.000 description 5
- 239000000872 buffer Substances 0.000 description 5
- 239000011248 coating agent Substances 0.000 description 5
- 238000000576 coating method Methods 0.000 description 5
- 230000008878 coupling Effects 0.000 description 5
- 238000010168 coupling process Methods 0.000 description 5
- 238000005859 coupling reaction Methods 0.000 description 5
- 238000010790 dilution Methods 0.000 description 5
- 239000012895 dilution Substances 0.000 description 5
- 208000037765 diseases and disorders Diseases 0.000 description 5
- 230000002068 genetic effect Effects 0.000 description 5
- 230000002427 irreversible effect Effects 0.000 description 5
- 230000004001 molecular interaction Effects 0.000 description 5
- 239000013642 negative control Substances 0.000 description 5
- 241000894007 species Species 0.000 description 5
- 208000024891 symptom Diseases 0.000 description 5
- 235000017274 Diospyros sandwicensis Nutrition 0.000 description 4
- 101001012157 Homo sapiens Receptor tyrosine-protein kinase erbB-2 Proteins 0.000 description 4
- 206010028980 Neoplasm Diseases 0.000 description 4
- 102100030086 Receptor tyrosine-protein kinase erbB-2 Human genes 0.000 description 4
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 4
- 230000004087 circulation Effects 0.000 description 4
- 230000001419 dependent effect Effects 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 230000006870 function Effects 0.000 description 4
- 238000002649 immunization Methods 0.000 description 4
- 238000002347 injection Methods 0.000 description 4
- 239000007924 injection Substances 0.000 description 4
- 238000001668 nucleic acid synthesis Methods 0.000 description 4
- 230000002441 reversible effect Effects 0.000 description 4
- 238000002741 site-directed mutagenesis Methods 0.000 description 4
- 230000009870 specific binding Effects 0.000 description 4
- 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 description 3
- MGGVALXERJRIRO-UHFFFAOYSA-N 4-[2-(2,3-dihydro-1H-inden-2-ylamino)pyrimidin-5-yl]-2-[2-oxo-2-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)ethyl]-1H-pyrazol-5-one Chemical compound C1C(CC2=CC=CC=C12)NC1=NC=C(C=N1)C=1C(=NN(C=1)CC(=O)N1CC2=C(CC1)NN=N2)O MGGVALXERJRIRO-UHFFFAOYSA-N 0.000 description 3
- 241000282693 Cercopithecidae Species 0.000 description 3
- 101000920778 Homo sapiens DNA excision repair protein ERCC-8 Proteins 0.000 description 3
- 102000006496 Immunoglobulin Heavy Chains Human genes 0.000 description 3
- 108010019476 Immunoglobulin Heavy Chains Proteins 0.000 description 3
- 241000282560 Macaca mulatta Species 0.000 description 3
- 206010070834 Sensitisation Diseases 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- ZMANZCXQSJIPKH-UHFFFAOYSA-N Triethylamine Chemical compound CCN(CC)CC ZMANZCXQSJIPKH-UHFFFAOYSA-N 0.000 description 3
- -1 amino acid sequence compound Chemical class 0.000 description 3
- 238000003556 assay Methods 0.000 description 3
- 235000020958 biotin Nutrition 0.000 description 3
- 210000004369 blood Anatomy 0.000 description 3
- 239000008280 blood Substances 0.000 description 3
- 230000015556 catabolic process Effects 0.000 description 3
- 239000003795 chemical substances by application Substances 0.000 description 3
- 238000003776 cleavage reaction Methods 0.000 description 3
- 238000006731 degradation reaction Methods 0.000 description 3
- 238000012217 deletion Methods 0.000 description 3
- 230000037430 deletion Effects 0.000 description 3
- 238000001514 detection method Methods 0.000 description 3
- 229940079593 drug Drugs 0.000 description 3
- 230000003053 immunization Effects 0.000 description 3
- 239000004615 ingredient Substances 0.000 description 3
- 238000002955 isolation Methods 0.000 description 3
- 210000001165 lymph node Anatomy 0.000 description 3
- 238000007857 nested PCR Methods 0.000 description 3
- 210000005105 peripheral blood lymphocyte Anatomy 0.000 description 3
- 230000002265 prevention Effects 0.000 description 3
- 238000000159 protein binding assay Methods 0.000 description 3
- 230000009467 reduction Effects 0.000 description 3
- 230000004044 response Effects 0.000 description 3
- 230000007017 scission Effects 0.000 description 3
- 230000008313 sensitization Effects 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- HZAXFHJVJLSVMW-UHFFFAOYSA-N 2-Aminoethan-1-ol Chemical compound NCCO HZAXFHJVJLSVMW-UHFFFAOYSA-N 0.000 description 2
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 2
- 241000283707 Capra Species 0.000 description 2
- 102000001187 Collagen Type III Human genes 0.000 description 2
- 108010069502 Collagen Type III Proteins 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 241000282520 Papio Species 0.000 description 2
- 229920001213 Polysorbate 20 Polymers 0.000 description 2
- 241000700159 Rattus Species 0.000 description 2
- 101001117144 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) [Pyruvate dehydrogenase (acetyl-transferring)] kinase 1, mitochondrial Proteins 0.000 description 2
- 108010090804 Streptavidin Proteins 0.000 description 2
- 150000001412 amines Chemical class 0.000 description 2
- 238000000137 annealing Methods 0.000 description 2
- 230000008827 biological function Effects 0.000 description 2
- 238000004364 calculation method Methods 0.000 description 2
- 238000010367 cloning Methods 0.000 description 2
- 238000010276 construction Methods 0.000 description 2
- 210000005220 cytoplasmic tail Anatomy 0.000 description 2
- 238000002330 electrospray ionisation mass spectrometry Methods 0.000 description 2
- 238000011156 evaluation Methods 0.000 description 2
- 102000048696 human ERCC8 Human genes 0.000 description 2
- 230000002209 hydrophobic effect Effects 0.000 description 2
- 230000005847 immunogenicity Effects 0.000 description 2
- 238000009169 immunotherapy Methods 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 238000001802 infusion Methods 0.000 description 2
- 230000007246 mechanism Effects 0.000 description 2
- 230000001404 mediated effect Effects 0.000 description 2
- 230000035772 mutation Effects 0.000 description 2
- 108010068617 neonatal Fc receptor Proteins 0.000 description 2
- 230000000144 pharmacologic effect Effects 0.000 description 2
- 239000012071 phase Substances 0.000 description 2
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 2
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 2
- 230000000069 prophylactic effect Effects 0.000 description 2
- 238000003127 radioimmunoassay Methods 0.000 description 2
- 108020003175 receptors Proteins 0.000 description 2
- 102000005962 receptors Human genes 0.000 description 2
- 239000011347 resin Substances 0.000 description 2
- 229920005989 resin Polymers 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 150000003384 small molecules Chemical class 0.000 description 2
- 230000002195 synergetic effect Effects 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 125000003088 (fluoren-9-ylmethoxy)carbonyl group Chemical group 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 102100021935 C-C motif chemokine 26 Human genes 0.000 description 1
- 101100314454 Caenorhabditis elegans tra-1 gene Proteins 0.000 description 1
- 241000282472 Canis lupus familiaris Species 0.000 description 1
- 241000251730 Chondrichthyes Species 0.000 description 1
- 239000003155 DNA primer Substances 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 101000897493 Homo sapiens C-C motif chemokine 26 Proteins 0.000 description 1
- 101000737793 Homo sapiens Cerebellar degeneration-related antigen 1 Proteins 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 102100037850 Interferon gamma Human genes 0.000 description 1
- 101000928455 Macaca fascicularis Albumin Proteins 0.000 description 1
- 108010090054 Membrane Glycoproteins Proteins 0.000 description 1
- 102000012750 Membrane Glycoproteins Human genes 0.000 description 1
- 101001044384 Mus musculus Interferon gamma Proteins 0.000 description 1
- 101100046526 Mus musculus Tnf gene Proteins 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 101710135898 Myc proto-oncogene protein Proteins 0.000 description 1
- 102100038895 Myc proto-oncogene protein Human genes 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 241000283984 Rodentia Species 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 101710150448 Transcriptional regulator Myc Proteins 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 125000001931 aliphatic group Chemical group 0.000 description 1
- 208000033571 alveolar capillary dysplasia with misalignment of pulmonary veins Diseases 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 238000000540 analysis of variance Methods 0.000 description 1
- 239000012491 analyte Substances 0.000 description 1
- 230000030741 antigen processing and presentation Effects 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 238000005452 bending Methods 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 102000015736 beta 2-Microglobulin Human genes 0.000 description 1
- 108010081355 beta 2-Microglobulin Proteins 0.000 description 1
- 239000011230 binding agent Substances 0.000 description 1
- 239000012148 binding buffer Substances 0.000 description 1
- 230000009141 biological interaction Effects 0.000 description 1
- 230000017531 blood circulation Effects 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 238000012875 competitive assay Methods 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 230000009260 cross reactivity Effects 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- 230000002354 daily effect Effects 0.000 description 1
- 230000009849 deactivation Effects 0.000 description 1
- 230000001934 delay Effects 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 230000037213 diet Effects 0.000 description 1
- 235000005911 diet Nutrition 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 239000002552 dosage form Substances 0.000 description 1
- 230000001159 endocytotic effect Effects 0.000 description 1
- 210000002472 endoplasmic reticulum Anatomy 0.000 description 1
- 210000001163 endosome Anatomy 0.000 description 1
- 210000002889 endothelial cell Anatomy 0.000 description 1
- 210000002919 epithelial cell Anatomy 0.000 description 1
- 230000003203 everyday effect Effects 0.000 description 1
- 230000029142 excretion Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000001917 fluorescence detection Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 108010033706 glycylserine Proteins 0.000 description 1
- 244000144993 groups of animals Species 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 210000003494 hepatocyte Anatomy 0.000 description 1
- 230000013632 homeostatic process Effects 0.000 description 1
- 229940042743 immune sera Drugs 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 239000007927 intramuscular injection Substances 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 230000031700 light absorption Effects 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 230000008774 maternal effect Effects 0.000 description 1
- 239000002609 medium Substances 0.000 description 1
- 230000003278 mimic effect Effects 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 230000017074 necrotic cell death Effects 0.000 description 1
- 208000004594 persistent fetal circulation syndrome Diseases 0.000 description 1
- 239000008177 pharmaceutical agent Substances 0.000 description 1
- 210000002826 placenta Anatomy 0.000 description 1
- 230000003169 placental effect Effects 0.000 description 1
- 230000036470 plasma concentration Effects 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 102000040430 polynucleotide Human genes 0.000 description 1
- 108091033319 polynucleotide Proteins 0.000 description 1
- 239000002157 polynucleotide Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 238000011809 primate model Methods 0.000 description 1
- 230000012743 protein tagging Effects 0.000 description 1
- 239000012429 reaction media Substances 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 230000008707 rearrangement Effects 0.000 description 1
- 230000033300 receptor internalization Effects 0.000 description 1
- 230000008929 regeneration Effects 0.000 description 1
- 238000011069 regeneration method Methods 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 238000013391 scatchard analysis Methods 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000002864 sequence alignment Methods 0.000 description 1
- 230000009919 sequestration Effects 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 238000011285 therapeutic regimen Methods 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 230000031998 transcytosis Effects 0.000 description 1
- 230000009261 transgenic effect Effects 0.000 description 1
- 230000005945 translocation Effects 0.000 description 1
- 230000032258 transport Effects 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 210000002993 trophoblast Anatomy 0.000 description 1
- 238000004704 ultra performance liquid chromatography Methods 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 210000003462 vein Anatomy 0.000 description 1
- 230000003442 weekly effect Effects 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
-
- 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
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/32—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against translation products of oncogenes
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/5005—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells
- G01N33/5008—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics
- G01N33/5044—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics involving specific cell types
- G01N33/5047—Cells of the immune system
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6854—Immunoglobulins
- G01N33/6857—Antibody fragments
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/22—Immunoglobulins specific features characterized by taxonomic origin from camelids, e.g. camel, llama or dromedary
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/31—Immunoglobulins specific features characterized by aspects of specificity or valency multispecific
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/565—Complementarity determining region [CDR]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/569—Single domain, e.g. dAb, sdAb, VHH, VNAR or nanobody®
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/31—Fusion polypeptide fusions, other than Fc, for prolonged plasma life, e.g. albumin
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Immunology (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Biomedical Technology (AREA)
- Medicinal Chemistry (AREA)
- Hematology (AREA)
- Biochemistry (AREA)
- Urology & Nephrology (AREA)
- Cell Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Physics & Mathematics (AREA)
- Biophysics (AREA)
- Microbiology (AREA)
- Analytical Chemistry (AREA)
- Food Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Genetics & Genomics (AREA)
- Biotechnology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Tropical Medicine & Parasitology (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Oncology (AREA)
- Toxicology (AREA)
- General Chemical & Material Sciences (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US87292306P | 2006-12-05 | 2006-12-05 | |
| PCT/EP2007/063348 WO2008068280A1 (en) | 2006-12-05 | 2007-12-05 | Peptides capable of binding to serum proteins |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2010511397A true JP2010511397A (ja) | 2010-04-15 |
| JP2010511397A5 JP2010511397A5 (enExample) | 2010-12-16 |
Family
ID=39272498
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2009539745A Withdrawn JP2010511397A (ja) | 2006-12-05 | 2007-12-05 | 血清タンパク質と結合可能なペプチド |
Country Status (7)
| Country | Link |
|---|---|
| US (1) | US20080267949A1 (enExample) |
| EP (1) | EP2097449A1 (enExample) |
| JP (1) | JP2010511397A (enExample) |
| CN (1) | CN101611056A (enExample) |
| AU (1) | AU2007328900A1 (enExample) |
| CA (1) | CA2671581A1 (enExample) |
| WO (1) | WO2008068280A1 (enExample) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| KR101551306B1 (ko) | 2015-03-23 | 2015-09-09 | 아주대학교산학협력단 | 뉴로필린1 특이적 결합 펩타이드 및 이 펩타이드가 융합된 융합 단백질, 및 이의 용도 |
Families Citing this family (85)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US9453251B2 (en) | 2002-10-08 | 2016-09-27 | Pfenex Inc. | Expression of mammalian proteins in Pseudomonas fluorescens |
| JP2008507294A (ja) | 2004-07-26 | 2008-03-13 | ダウ グローバル テクノロジーズ インコーポレイティド | 菌株遺伝子操作による改善されたタンパク質発現のための方法 |
| US9512236B2 (en) | 2006-12-19 | 2016-12-06 | Ablynx N.V. | Amino acid sequences directed against GPCRS and polypeptides comprising the same for the treatment of GPCR-related diseases and disorders |
| US9580719B2 (en) | 2007-04-27 | 2017-02-28 | Pfenex, Inc. | Method for rapidly screening microbial hosts to identify certain strains with improved yield and/or quality in the expression of heterologous proteins |
| EP2615172A1 (en) | 2007-04-27 | 2013-07-17 | Pfenex Inc. | Method for rapidly screening microbial hosts to identify certain strains with improved yield and/or quality in the expression of heterologous proteins |
| CN101970490A (zh) | 2007-11-27 | 2011-02-09 | 埃博灵克斯股份有限公司 | 针对异二聚体细胞因子和/或其受体的氨基酸序列以及包括所述氨基酸序列的多肽 |
| WO2009127691A1 (en) * | 2008-04-17 | 2009-10-22 | Ablynx N.V. | Peptides capable of binding to serum proteins and compounds, constructs and polypeptides comprising the same |
| US9212226B2 (en) | 2008-05-16 | 2015-12-15 | Ablynx N.V. | Amino acid sequences directed against CXCR4 and other GPCRs and compounds comprising the same |
| DK2285408T3 (en) | 2008-06-05 | 2019-02-04 | Ablynx Nv | AMINO ACID SEQUENCES AGAINST COATING PROTEINS IN A VIRUS AND POLYPEPTIDES INCLUDING THESE FOR TREATMENT OF VIRUSAL DISEASES |
| US8444976B2 (en) | 2008-07-02 | 2013-05-21 | Argen-X B.V. | Antigen binding polypeptides |
| EP2417163B1 (en) | 2009-04-10 | 2019-02-27 | Ablynx N.V. | Improved amino acid sequences directed against il-6r and polypeptides comprising the same for the treatment of il-6r related diseases and disorders |
| US20120134984A1 (en) * | 2009-06-01 | 2012-05-31 | Olga Lubman | Molecules with extended half-lives and uses thereof |
| MX340541B (es) | 2009-06-05 | 2016-07-13 | Alblynx Nv | Secuencias de aminoacidos mejoradas dirigidas contra virus sincitial respiratorio humano y polipeptidos que comprenden las mismas para la prevencion y/o tratamiento de infecciones del tracto respiratorio. |
| US9644022B2 (en) | 2009-11-30 | 2017-05-09 | Ablynx N.V. | Amino acid sequences directed against human respiratory syncytial virus (HRSV) and polypeptides comprising the same for the prevention and/or treatment of respiratory tract infections |
| WO2011083140A1 (en) | 2010-01-08 | 2011-07-14 | Ablynx Nv | Immunoglobulin single variable domain directed against human cxcr4 |
| WO2011095545A1 (en) | 2010-02-05 | 2011-08-11 | Ablynx Nv | Peptides capable of binding to serum albumin and compounds, constructs and polypeptides comprising the same |
| US9120855B2 (en) | 2010-02-10 | 2015-09-01 | Novartis Ag | Biologic compounds directed against death receptor 5 |
| EP2536754A1 (en) | 2010-02-16 | 2012-12-26 | Novo Nordisk A/S | Factor viii fusion protein |
| WO2011107507A1 (en) | 2010-03-03 | 2011-09-09 | Boehringer Ingelheim International Gmbh | Biparatopic abeta binding polypeptides |
| WO2011117423A1 (en) | 2010-03-26 | 2011-09-29 | Ablynx N.V. | Immunoglobulin single variable domains directed against cxcr7 |
| JP2013525408A (ja) | 2010-04-30 | 2013-06-20 | アブリンクス エン．ヴェー． | ヘテロ二量体サイトカインｉｌ−２３のｐ１９サブユニットに指向性を有するナノボディのアミノ酸配列 |
| SG185354A1 (en) | 2010-05-20 | 2012-12-28 | Ablynx Nv | Biological materials related to her3 |
| WO2012042026A1 (en) | 2010-09-30 | 2012-04-05 | Ablynx Nv | Biological materials related to c-met |
| US11644471B2 (en) | 2010-09-30 | 2023-05-09 | Ablynx N.V. | Techniques for predicting, detecting and reducing aspecific protein interference in assays involving immunoglobulin single variable domains |
| US20150158948A9 (en) | 2011-03-28 | 2015-06-11 | Francis Descamps | Bispecific anti-cxcr7 immunoglobulin single variable domains |
| UA117218C2 (uk) | 2011-05-05 | 2018-07-10 | Мерк Патент Гмбх | Поліпептид, спрямований проти il-17a, il-17f та/або il17-a/f |
| RU2661677C2 (ru) | 2011-05-27 | 2018-07-18 | Аблинкс Нв | Ингибирование резорбции кости с помощью связывающих rank-l пептидов |
| JP2014525736A (ja) | 2011-06-23 | 2014-10-02 | アブリンクス エン．ヴェー． | ＩｇＥに対する免疫グロブリン単一可変ドメイン |
| EP3363813A1 (en) | 2011-06-23 | 2018-08-22 | Ablynx NV | Techniques for predicting, detecting and reducing aspecific protein interference in assays involving immunoglobin single variable domains |
| EP4350345A3 (en) | 2011-06-23 | 2024-07-24 | Ablynx N.V. | Techniques for predicting, detecting and reducing aspecific protein interference in assays involving immunoglobin single variable domains |
| NZ780183A (en) | 2011-06-23 | 2024-12-20 | Ablynx Nv | Techniques for predicting, detecting and reducing aspecific protein interference in assays involving immunoglobulin single variable domains |
| WO2013041722A1 (en) | 2011-09-23 | 2013-03-28 | Ablynx Nv | Prolonged inhibition of interleukin-6 mediated signaling |
| EP2747783B1 (en) | 2011-09-30 | 2017-06-14 | Ablynx N.V. | Biological materials related to c-met |
| UA115781C2 (uk) | 2012-02-27 | 2017-12-26 | Бьорінгер Інгельхайм Інтернаціональ Гмбх | Cx3cr1-зв'язуючий поліпептид |
| NL1040254C2 (en) | 2013-05-17 | 2014-11-24 | Ablynx Nv | Stable formulations of immunoglobulin single variable domains and uses thereof. |
| US9409139B2 (en) | 2013-08-05 | 2016-08-09 | Twist Bioscience Corporation | De novo synthesized gene libraries |
| PT3248986T (pt) | 2014-05-16 | 2022-04-05 | Ablynx Nv | Domínios variáveis de imunoglobulina |
| NL2013661B1 (en) | 2014-10-21 | 2016-10-05 | Ablynx Nv | KV1.3 Binding immunoglobulins. |
| DE102014217793A1 (de) * | 2014-09-05 | 2016-03-10 | Jörg Labahn | Fusionsprotein und Aufreinigungsverfahren |
| CA2975852A1 (en) | 2015-02-04 | 2016-08-11 | Twist Bioscience Corporation | Methods and devices for de novo oligonucleic acid assembly |
| ES3029413T3 (en) | 2015-04-02 | 2025-06-24 | Ablynx Nv | Bispecific cxcr4-cd-4 polypeptides with potent anti-hiv activity |
| WO2016172377A1 (en) | 2015-04-21 | 2016-10-27 | Twist Bioscience Corporation | Devices and methods for oligonucleic acid library synthesis |
| EP3611192B1 (en) | 2015-05-13 | 2025-03-05 | Ablynx N.V. | T cell recruiting polypeptides based on tcr alpha/beta reactivity |
| SI3294319T1 (sl) | 2015-05-13 | 2024-09-30 | Ablynx Nv | Polipeptidi, ki rekrutirajo celice T na osnovi reaktivnosti CD3 |
| AU2016324296A1 (en) | 2015-09-18 | 2018-04-12 | Twist Bioscience Corporation | Oligonucleic acid variant libraries and synthesis thereof |
| CN108698012A (zh) | 2015-09-22 | 2018-10-23 | 特韦斯特生物科学公司 | 用于核酸合成的柔性基底 |
| NO2768984T3 (enExample) | 2015-11-12 | 2018-06-09 | ||
| HK1254952A1 (zh) | 2015-11-18 | 2019-08-02 | Merck Sharp & Dohme Llc | Ctla4结合剂 |
| SG10201911035QA (en) | 2015-11-18 | 2020-01-30 | Merck Sharp & Dohme | Pd1 and/or lag3 binders |
| CA3006398A1 (en) | 2015-11-27 | 2017-06-01 | Ablynx Nv | Polypeptides inhibiting cd40l |
| MA54648A (fr) | 2015-12-04 | 2021-11-10 | Boehringer Ingelheim Int | Polypeptides biparatopiques antagonistes de la signalisation wnt dans des cellules tumorales |
| WO2017202776A1 (en) | 2016-05-23 | 2017-11-30 | Luxembourg Institute Of Health (Lih) | Multifunctional heteromultimeric constructs. |
| WO2018007442A1 (en) | 2016-07-06 | 2018-01-11 | Ablynx N.V. | Treatment of il-6r related diseases |
| CN106282214A (zh) * | 2016-08-03 | 2017-01-04 | 康众（北京）生物科技有限公司 | 一种快速获得纳米抗体的方法及其应用 |
| WO2018029182A1 (en) | 2016-08-08 | 2018-02-15 | Ablynx N.V. | Il-6r single variable domain antibodies for treatment of il-6r related diseases |
| EP3512880A1 (en) | 2016-09-15 | 2019-07-24 | Ablynx NV | Immunoglobulin single variable domains directed against macrophage migration inhibitory factor |
| CN110248724B (zh) | 2016-09-21 | 2022-11-18 | 特韦斯特生物科学公司 | 基于核酸的数据存储 |
| AU2017361846B2 (en) | 2016-11-16 | 2024-08-22 | Ablynx Nv | T cell recruiting polypeptides capable of binding CD123 and TCR alpha/beta |
| WO2018156792A1 (en) | 2017-02-22 | 2018-08-30 | Twist Bioscience Corporation | Nucleic acid based data storage |
| US11033636B2 (en) | 2017-05-31 | 2021-06-15 | Boehringer Ingelheim International Gmbh | Polypeptides antagonizing Wnt signaling in tumor cells |
| KR102778120B1 (ko) | 2017-06-02 | 2025-03-06 | 메르크 파텐트 게엠베하 | Mmp13 결합성 면역글로불린 |
| LT3630847T (lt) | 2017-06-02 | 2024-12-10 | Merck Patent Gmbh | Adamts surišantys imunoglobulinai |
| IL270951B2 (en) | 2017-06-02 | 2025-05-01 | Merck Patent Gmbh | ADAMTS5, MMP13 and aggrecan-binding polypeptides |
| CN110997716B (zh) | 2017-06-02 | 2024-03-15 | 埃博灵克斯股份有限公司 | 结合聚集蛋白聚糖的免疫球蛋白 |
| WO2018231864A1 (en) | 2017-06-12 | 2018-12-20 | Twist Bioscience Corporation | Methods for seamless nucleic acid assembly |
| IL271205B2 (en) | 2017-06-12 | 2025-02-01 | Twist Bioscience Corp | Methods for assembling continuous nucleic acids |
| US11407837B2 (en) | 2017-09-11 | 2022-08-09 | Twist Bioscience Corporation | GPCR binding proteins and synthesis thereof |
| KR102637566B1 (ko) | 2017-10-20 | 2024-02-16 | 트위스트 바이오사이언스 코포레이션 | 폴리뉴클레오타이드 합성을 위한 가열된 나노웰 |
| CN112041438B (zh) | 2018-01-04 | 2025-05-23 | 特韦斯特生物科学公司 | 基于dna的数字信息存储 |
| CA3100739A1 (en) | 2018-05-18 | 2019-11-21 | Twist Bioscience Corporation | Polynucleotides, reagents, and methods for nucleic acid hybridization |
| GB201818460D0 (en) * | 2018-11-13 | 2018-12-26 | Crescendo Biologics Ltd | Single domain antibodies that bind human serum albumin |
| CA3124980A1 (en) | 2018-12-26 | 2020-07-02 | Twist Bioscience Corporation | Highly accurate de novo polynucleotide synthesis |
| KR20210143766A (ko) | 2019-02-26 | 2021-11-29 | 트위스트 바이오사이언스 코포레이션 | Glp1 수용체에 대한 변이체 핵산 라이브러리 |
| CN113785057A (zh) | 2019-02-26 | 2021-12-10 | 特韦斯特生物科学公司 | 用于抗体优化的变异核酸文库 |
| CN109942704B (zh) * | 2019-04-12 | 2023-01-20 | 深圳普瑞金生物药业股份有限公司 | Hsa单域抗体、核酸及试剂盒 |
| US20220227850A1 (en) * | 2019-05-15 | 2022-07-21 | Crescendo Biologics Limited | Binding molecules |
| JP2022550497A (ja) | 2019-06-21 | 2022-12-02 | ツイスト バイオサイエンス コーポレーション | バーコードに基づいた核酸配列アセンブリ |
| AU2020355027A1 (en) | 2019-09-23 | 2022-04-21 | Twist Bioscience Corporation | Antibodies that bind CD3 Epsilon |
| CA3155629A1 (en) | 2019-09-23 | 2021-04-01 | Twist Bioscience Corporation | Variant nucleic acid libraries for crth2 |
| CA3209052A1 (en) | 2021-02-19 | 2022-08-25 | Rafael Cristian CASELLAS | Single domain antibodies that neutralize sars-cov-2 |
| US12258406B2 (en) | 2021-03-24 | 2025-03-25 | Twist Bioscience Corporation | Antibodies that bind CD3 Epsilon |
| TW202440614A (zh) | 2022-12-23 | 2024-10-16 | 比利時商艾伯霖克斯公司 | 基於蛋白質的接合載體 |
| WO2024261235A1 (en) | 2023-06-22 | 2024-12-26 | Ablynx Nv | Chimeric proteins for modulating cytokine receptor activity |
| US20250236673A1 (en) | 2023-12-22 | 2025-07-24 | Ablynx N.V. | Protein-based carriers for site-specific amine conjugation |
| WO2025133253A2 (en) | 2023-12-22 | 2025-06-26 | Ablynx Nv | Protein-based conjugation carriers for intranuclear delivery |
Family Cites Families (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0656946B2 (en) * | 1992-08-21 | 2010-03-31 | Vrije Universiteit Brussel | Immunoglobulins devoid of light chains |
| EP0888381A4 (en) * | 1995-12-21 | 2001-10-17 | Scripps Research Inst | TARGETED THERAPEUTIC AND DIAGNOSTIC AGENTS, METHODS FOR THEIR PRODUCTION AND USE |
| AU2002351896A1 (en) * | 2001-12-11 | 2003-06-23 | Ablynx N.V. | Method for displaying loops from immunoglobulin domains in different contexts |
| JP2005517674A (ja) * | 2002-01-03 | 2005-06-16 | フラームス・インテルウニフェルシタイル・インステイチュート・フォール・ビオテヒノロヒー・ヴェーゼットウェー | 腫瘍の処置に有用な新規免疫コンジュゲート |
| WO2005044858A1 (en) * | 2003-11-07 | 2005-05-19 | Ablynx N.V. | Camelidae single domain antibodies vhh directed against epidermal growth factor receptor and uses therefor |
| EP3299393A1 (en) * | 2002-11-08 | 2018-03-28 | Ablynx N.V. | Single domain antibodies directed against tumour necrosis factor-alpha and uses therefor |
| CA2595682A1 (en) * | 2005-01-31 | 2006-08-03 | Ablynx N.V. | Method for generating variable domain sequences of heavy chain antibodies |
| US20070269422A1 (en) * | 2006-05-17 | 2007-11-22 | Ablynx N.V. | Serum albumin binding proteins with long half-lives |
| WO2009127691A1 (en) * | 2008-04-17 | 2009-10-22 | Ablynx N.V. | Peptides capable of binding to serum proteins and compounds, constructs and polypeptides comprising the same |
| US20110243954A1 (en) * | 2008-04-17 | 2011-10-06 | Ablynx N.V. | Peptides capable of binding to serum proteins and compounds, constructs and polypeptides comprising the same |
-
2007
- 2007-12-05 JP JP2009539745A patent/JP2010511397A/ja not_active Withdrawn
- 2007-12-05 AU AU2007328900A patent/AU2007328900A1/en not_active Abandoned
- 2007-12-05 EP EP07847841A patent/EP2097449A1/en not_active Withdrawn
- 2007-12-05 US US11/999,497 patent/US20080267949A1/en not_active Abandoned
- 2007-12-05 CA CA002671581A patent/CA2671581A1/en not_active Abandoned
- 2007-12-05 CN CNA2007800509560A patent/CN101611056A/zh active Pending
- 2007-12-05 WO PCT/EP2007/063348 patent/WO2008068280A1/en not_active Ceased
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| KR101551306B1 (ko) | 2015-03-23 | 2015-09-09 | 아주대학교산학협력단 | 뉴로필린1 특이적 결합 펩타이드 및 이 펩타이드가 융합된 융합 단백질, 및 이의 용도 |
| WO2016153276A1 (ko) * | 2015-03-23 | 2016-09-29 | 아주대학교산학협력단 | 뉴로필린1 특이적 결합 펩타이드 및 이 펩타이드가 융합된 융합 단백질, 및 이의 용도 |
| US10400022B2 (en) | 2015-03-23 | 2019-09-03 | Ajou University Industry-Academic Cooperation Foundation | Neuropilin-1 specific binding peptide, fusion protein fused with same, and use thereof |
Also Published As
| Publication number | Publication date |
|---|---|
| AU2007328900A1 (en) | 2008-06-12 |
| EP2097449A1 (en) | 2009-09-09 |
| CN101611056A (zh) | 2009-12-23 |
| CA2671581A1 (en) | 2008-06-12 |
| WO2008068280A1 (en) | 2008-06-12 |
| US20080267949A1 (en) | 2008-10-30 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP2010511397A (ja) | 血清タンパク質と結合可能なペプチド | |
| JP7093380B2 (ja) | Ｉｌ－１７ａ、ｉｌ－１７ｆおよび／またはｉｌ１７－ａ／ｆに対するアミノ酸配列および前記アミノ酸配列を含むポリペプチド | |
| JP5240870B2 (ja) | 改善した免疫グロブリン配列を提供する方法 | |
| CN105061593B (zh) | 改良的抗血清清蛋白结合变体 | |
| AU2011254559B2 (en) | Improved anti-serum albumin binding variants | |
| US10618964B2 (en) | Nanobody against IL-6R | |
| JP2013518853A (ja) | 血清アルブミンと結合することが可能なペプチド並びにこれを含む化合物、構築物及びポリペプチド | |
| JP2011516603A (ja) | 血清タンパク質と結合することが可能なペプチド、並びにこれを含む化合物、構築物及びポリペプチド | |
| CA2705890A1 (en) | Amino acid sequences directed against heterodimeric cytokines and/or their receptors and polypeptides comprising the same | |
| CN101589057A (zh) | 以条件性方式结合于需要的分子的氨基酸序列 | |
| KR20230053002A (ko) | 개선된 면역글로불린 가변 도메인 | |
| AU2024221136A1 (en) | Polypeptides binding to the neonatal fc receptor | |
| EP4665755A1 (en) | Polypeptides binding to the neonatal fc receptor |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20101022 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20101022 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20111012 |
|
| A761 | Written withdrawal of application |
Free format text: JAPANESE INTERMEDIATE CODE: A761 Effective date: 20120912 |