CA2700391A1 - Designed armadillo repeat proteins - Google Patents
Designed armadillo repeat proteins Download PDFInfo
- Publication number
- CA2700391A1 CA2700391A1 CA2700391A CA2700391A CA2700391A1 CA 2700391 A1 CA2700391 A1 CA 2700391A1 CA 2700391 A CA2700391 A CA 2700391A CA 2700391 A CA2700391 A CA 2700391A CA 2700391 A1 CA2700391 A1 CA 2700391A1
- Authority
- CA
- Canada
- Prior art keywords
- repeat
- armadillo
- amino acid
- modules
- proteins
- 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.)
- Abandoned
Links
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 347
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 338
- 108010014223 Armadillo Domain Proteins Proteins 0.000 title claims abstract description 237
- 102000016904 Armadillo Domain Proteins Human genes 0.000 title claims abstract description 236
- 241000289632 Dasypodidae Species 0.000 title claims abstract description 222
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 126
- 150000001413 amino acids Chemical class 0.000 claims abstract description 74
- 230000027455 binding Effects 0.000 claims abstract description 72
- 238000009739 binding Methods 0.000 claims abstract description 72
- 238000000034 method Methods 0.000 claims abstract description 55
- 108091035707 Consensus sequence Proteins 0.000 claims abstract description 51
- 125000000539 amino acid group Chemical group 0.000 claims description 80
- 210000004899 c-terminal region Anatomy 0.000 claims description 49
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 38
- 150000007523 nucleic acids Chemical class 0.000 claims description 36
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 36
- 102000039446 nucleic acids Human genes 0.000 claims description 30
- 108020004707 nucleic acids Proteins 0.000 claims description 30
- 229910052739 hydrogen Inorganic materials 0.000 claims description 21
- 229910052700 potassium Inorganic materials 0.000 claims description 21
- 229910052757 nitrogen Inorganic materials 0.000 claims description 18
- 229920001184 polypeptide Polymers 0.000 claims description 17
- 102000054078 gamma Catenin Human genes 0.000 claims description 11
- 108010084448 gamma Catenin Proteins 0.000 claims description 11
- 238000012216 screening Methods 0.000 claims description 10
- 229910052698 phosphorus Inorganic materials 0.000 claims description 8
- 101001059240 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) Site-specific recombinase Flp Proteins 0.000 claims description 4
- 102000015735 Beta-catenin Human genes 0.000 claims description 3
- 108060000903 Beta-catenin Proteins 0.000 claims description 3
- 102000009899 alpha Karyopherins Human genes 0.000 claims description 3
- 108010077099 alpha Karyopherins Proteins 0.000 claims description 3
- 108010016626 Dipeptides Proteins 0.000 abstract description 11
- 108091008324 binding proteins Proteins 0.000 abstract description 2
- 102000023732 binding proteins Human genes 0.000 abstract 1
- 235000018102 proteins Nutrition 0.000 description 291
- 235000001014 amino acid Nutrition 0.000 description 77
- 229940024606 amino acid Drugs 0.000 description 68
- 230000002209 hydrophobic effect Effects 0.000 description 63
- 230000003993 interaction Effects 0.000 description 38
- 102000053602 DNA Human genes 0.000 description 23
- 108020004414 DNA Proteins 0.000 description 23
- 108091034117 Oligonucleotide Proteins 0.000 description 23
- 230000015572 biosynthetic process Effects 0.000 description 23
- 230000035772 mutation Effects 0.000 description 23
- 238000001542 size-exclusion chromatography Methods 0.000 description 23
- 108091028043 Nucleic acid sequence Proteins 0.000 description 21
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 20
- 230000003321 amplification Effects 0.000 description 20
- 238000003199 nucleic acid amplification method Methods 0.000 description 20
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 18
- 102000011781 Karyopherins Human genes 0.000 description 18
- 108010062228 Karyopherins Proteins 0.000 description 18
- 210000004027 cell Anatomy 0.000 description 17
- 238000013461 design Methods 0.000 description 17
- 239000013078 crystal Substances 0.000 description 16
- 238000000569 multi-angle light scattering Methods 0.000 description 16
- 102000016362 Catenins Human genes 0.000 description 13
- 108010067316 Catenins Proteins 0.000 description 13
- 239000000203 mixture Substances 0.000 description 12
- 239000002904 solvent Substances 0.000 description 12
- 238000002983 circular dichroism Methods 0.000 description 11
- 238000010367 cloning Methods 0.000 description 11
- 238000004925 denaturation Methods 0.000 description 11
- 230000036425 denaturation Effects 0.000 description 11
- 239000013598 vector Substances 0.000 description 11
- 241000384062 Armadillo Species 0.000 description 10
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 10
- 238000013459 approach Methods 0.000 description 10
- 238000003786 synthesis reaction Methods 0.000 description 10
- 108020004705 Codon Proteins 0.000 description 9
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 9
- 238000002474 experimental method Methods 0.000 description 9
- 125000001165 hydrophobic group Chemical group 0.000 description 9
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 9
- 108010087904 neutravidin Proteins 0.000 description 9
- 239000013612 plasmid Substances 0.000 description 9
- 230000008569 process Effects 0.000 description 9
- 239000011734 sodium Substances 0.000 description 9
- 241000588724 Escherichia coli Species 0.000 description 8
- 108091092878 Microsatellite Proteins 0.000 description 8
- 108010077850 Nuclear Localization Signals Proteins 0.000 description 8
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 8
- 239000011230 binding agent Substances 0.000 description 8
- 238000001142 circular dichroism spectrum Methods 0.000 description 8
- 230000004048 modification Effects 0.000 description 8
- 238000012986 modification Methods 0.000 description 8
- 238000000746 purification Methods 0.000 description 8
- 238000005070 sampling Methods 0.000 description 8
- 230000007704 transition Effects 0.000 description 8
- 238000004458 analytical method Methods 0.000 description 7
- 230000029087 digestion Effects 0.000 description 7
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 6
- 239000004471 Glycine Substances 0.000 description 6
- 238000005481 NMR spectroscopy Methods 0.000 description 6
- 108091081062 Repeated sequence (DNA) Proteins 0.000 description 6
- 125000001931 aliphatic group Chemical group 0.000 description 6
- 238000007845 assembly PCR Methods 0.000 description 6
- 230000001580 bacterial effect Effects 0.000 description 6
- 239000000872 buffer Substances 0.000 description 6
- 235000018417 cysteine Nutrition 0.000 description 6
- 238000010438 heat treatment Methods 0.000 description 6
- 238000005259 measurement Methods 0.000 description 6
- 239000000178 monomer Substances 0.000 description 6
- 238000005381 potential energy Methods 0.000 description 6
- 108020001580 protein domains Proteins 0.000 description 6
- 108091008146 restriction endonucleases Proteins 0.000 description 6
- 108700010070 Codon Usage Proteins 0.000 description 5
- 102100038195 Exonuclease mut-7 homolog Human genes 0.000 description 5
- 101000958030 Homo sapiens Exonuclease mut-7 homolog Proteins 0.000 description 5
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 5
- 230000002378 acidificating effect Effects 0.000 description 5
- 238000000978 circular dichroism spectroscopy Methods 0.000 description 5
- 238000012217 deletion Methods 0.000 description 5
- 230000037430 deletion Effects 0.000 description 5
- 239000001257 hydrogen Substances 0.000 description 5
- 238000003780 insertion Methods 0.000 description 5
- 230000037431 insertion Effects 0.000 description 5
- 235000013930 proline Nutrition 0.000 description 5
- 230000002441 reversible effect Effects 0.000 description 5
- 238000002702 ribosome display Methods 0.000 description 5
- 239000000523 sample Substances 0.000 description 5
- 108091026890 Coding region Proteins 0.000 description 4
- 238000002965 ELISA Methods 0.000 description 4
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 4
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 4
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 4
- 239000000539 dimer Substances 0.000 description 4
- 238000010828 elution Methods 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- 230000009870 specific binding Effects 0.000 description 4
- 230000000087 stabilizing effect Effects 0.000 description 4
- FWEOQOXTVHGIFQ-UHFFFAOYSA-N 8-anilinonaphthalene-1-sulfonic acid Chemical compound C=12C(S(=O)(=O)O)=CC=CC2=CC=CC=1NC1=CC=CC=C1 FWEOQOXTVHGIFQ-UHFFFAOYSA-N 0.000 description 3
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 3
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 3
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 3
- 102100033615 Nucleoprotein TPR Human genes 0.000 description 3
- 239000012505 Superdex™ Substances 0.000 description 3
- -1 WD40) Proteins 0.000 description 3
- 238000002835 absorbance Methods 0.000 description 3
- 238000001042 affinity chromatography Methods 0.000 description 3
- 230000002776 aggregation Effects 0.000 description 3
- 238000004220 aggregation Methods 0.000 description 3
- 235000004279 alanine Nutrition 0.000 description 3
- 229960000723 ampicillin Drugs 0.000 description 3
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 3
- 125000003118 aryl group Chemical group 0.000 description 3
- 238000005452 bending Methods 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 238000004587 chromatography analysis Methods 0.000 description 3
- 239000000287 crude extract Substances 0.000 description 3
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 3
- 150000001945 cysteines Chemical class 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 239000012149 elution buffer Substances 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 239000013604 expression vector Substances 0.000 description 3
- 230000006870 function Effects 0.000 description 3
- 239000002609 medium Substances 0.000 description 3
- 229910021645 metal ion Inorganic materials 0.000 description 3
- 238000012856 packing Methods 0.000 description 3
- 102000023856 peptide binding proteins Human genes 0.000 description 3
- 108091008399 peptide binding proteins Proteins 0.000 description 3
- 150000008300 phosphoramidites Chemical class 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 230000004850 protein–protein interaction Effects 0.000 description 3
- 238000002708 random mutagenesis Methods 0.000 description 3
- 238000007670 refining Methods 0.000 description 3
- 238000012163 sequencing technique Methods 0.000 description 3
- 238000001228 spectrum Methods 0.000 description 3
- 238000006467 substitution reaction Methods 0.000 description 3
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical group N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 2
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 2
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 2
- NLXLAEXVIDQMFP-UHFFFAOYSA-N Ammonia chloride Chemical compound [NH4+].[Cl-] NLXLAEXVIDQMFP-UHFFFAOYSA-N 0.000 description 2
- 102000008102 Ankyrins Human genes 0.000 description 2
- 108010049777 Ankyrins Proteins 0.000 description 2
- 108700022150 Designed Ankyrin Repeat Proteins Proteins 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- 239000007836 KH2PO4 Substances 0.000 description 2
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- 101100103787 Oryza sativa subsp. japonica Y14A gene Proteins 0.000 description 2
- 229910019142 PO4 Inorganic materials 0.000 description 2
- 102220500883 Phospholipid-transporting ATPase ABCA1_Y14A_mutation Human genes 0.000 description 2
- 229920001213 Polysorbate 20 Polymers 0.000 description 2
- 230000021736 acetylation Effects 0.000 description 2
- 238000006640 acetylation reaction Methods 0.000 description 2
- 238000007792 addition Methods 0.000 description 2
- 150000001408 amides Chemical group 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- AFYNADDZULBEJA-UHFFFAOYSA-N bicinchoninic acid Chemical compound C1=CC=CC2=NC(C=3C=C(C4=CC=CC=C4N=3)C(=O)O)=CC(C(O)=O)=C21 AFYNADDZULBEJA-UHFFFAOYSA-N 0.000 description 2
- 238000013378 biophysical characterization Methods 0.000 description 2
- 238000004364 calculation method Methods 0.000 description 2
- 229910052799 carbon Inorganic materials 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 238000007385 chemical modification Methods 0.000 description 2
- 238000005520 cutting process Methods 0.000 description 2
- 238000006731 degradation reaction Methods 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 230000018109 developmental process Effects 0.000 description 2
- 239000003085 diluting agent Substances 0.000 description 2
- 230000009977 dual effect Effects 0.000 description 2
- 239000006167 equilibration buffer Substances 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- ZRALSGWEFCBTJO-UHFFFAOYSA-O guanidinium Chemical compound NC(N)=[NH2+] ZRALSGWEFCBTJO-UHFFFAOYSA-O 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 2
- 210000004901 leucine-rich repeat Anatomy 0.000 description 2
- 238000004949 mass spectrometry Methods 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 2
- 230000011987 methylation Effects 0.000 description 2
- 238000007069 methylation reaction Methods 0.000 description 2
- 238000000329 molecular dynamics simulation Methods 0.000 description 2
- 229910000402 monopotassium phosphate Inorganic materials 0.000 description 2
- 235000019796 monopotassium phosphate Nutrition 0.000 description 2
- 239000002773 nucleotide Substances 0.000 description 2
- 125000003729 nucleotide group Chemical group 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 2
- 239000010452 phosphate Substances 0.000 description 2
- 239000008363 phosphate buffer Substances 0.000 description 2
- 230000026731 phosphorylation Effects 0.000 description 2
- 238000006366 phosphorylation reaction Methods 0.000 description 2
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 2
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 2
- GNSKLFRGEWLPPA-UHFFFAOYSA-M potassium dihydrogen phosphate Chemical compound [K+].OP(O)([O-])=O GNSKLFRGEWLPPA-UHFFFAOYSA-M 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 239000012460 protein solution Substances 0.000 description 2
- 230000017854 proteolysis Effects 0.000 description 2
- 238000010791 quenching Methods 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 230000000717 retained effect Effects 0.000 description 2
- 229920002477 rna polymer Polymers 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 238000002864 sequence alignment Methods 0.000 description 2
- 238000000527 sonication Methods 0.000 description 2
- 238000010561 standard procedure Methods 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 239000013076 target substance Substances 0.000 description 2
- 230000014616 translation Effects 0.000 description 2
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 2
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- 108010039224 Amidophosphoribosyltransferase Proteins 0.000 description 1
- BUVNWKQBMZLCDW-UGYAYLCHSA-N Asp-Asn-Ile Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)CC)C(O)=O BUVNWKQBMZLCDW-UGYAYLCHSA-N 0.000 description 1
- JHFNSBBHKSZXKB-VKHMYHEASA-N Asp-Gly Chemical compound OC(=O)C[C@H](N)C(=O)NCC(O)=O JHFNSBBHKSZXKB-VKHMYHEASA-N 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 102000003846 Carbonic anhydrases Human genes 0.000 description 1
- 108090000209 Carbonic anhydrases Proteins 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 241000255601 Drosophila melanogaster Species 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 241001596967 Escherichia coli M15 Species 0.000 description 1
- 102100040870 Glycine amidinotransferase, mitochondrial Human genes 0.000 description 1
- 101000893303 Homo sapiens Glycine amidinotransferase, mitochondrial Proteins 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-N L-arginine Chemical compound OC(=O)[C@@H](N)CCCN=C(N)N ODKSFYDXXFIFQN-BYPYZUCNSA-N 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- 101150118523 LYS4 gene Proteins 0.000 description 1
- 108010006444 Leucine-Rich Repeat Proteins Proteins 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 101100238610 Mus musculus Msh3 gene Proteins 0.000 description 1
- 102000008300 Mutant Proteins Human genes 0.000 description 1
- 108010021466 Mutant Proteins Proteins 0.000 description 1
- 238000012408 PCR amplification Methods 0.000 description 1
- 101150004094 PRO2 gene Proteins 0.000 description 1
- 102000003753 Plakophilins Human genes 0.000 description 1
- 108010057275 Plakophilins Proteins 0.000 description 1
- 101100070542 Podospora anserina het-s gene Proteins 0.000 description 1
- 101100412093 Schizosaccharomyces pombe (strain 972 / ATCC 24843) rec16 gene Proteins 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- 101000677856 Stenotrophomonas maltophilia (strain K279a) Actin-binding protein Smlt3054 Proteins 0.000 description 1
- 101000865057 Thermococcus litoralis DNA polymerase Proteins 0.000 description 1
- JZRWCGZRTZMZEH-UHFFFAOYSA-N Thiamine Natural products CC1=C(CCO)SC=[N+]1CC1=CN=C(C)N=C1N JZRWCGZRTZMZEH-UHFFFAOYSA-N 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 102000001742 Tumor Suppressor Proteins Human genes 0.000 description 1
- 108010040002 Tumor Suppressor Proteins Proteins 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 238000001261 affinity purification Methods 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 235000019270 ammonium chloride Nutrition 0.000 description 1
- 238000012436 analytical size exclusion chromatography Methods 0.000 description 1
- 238000005349 anion exchange Methods 0.000 description 1
- 238000000137 annealing Methods 0.000 description 1
- 238000000149 argon plasma sintering Methods 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 125000000613 asparagine group Chemical group N[C@@H](CC(N)=O)C(=O)* 0.000 description 1
- 229940009098 aspartate Drugs 0.000 description 1
- 108010047857 aspartylglycine Proteins 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- 230000008033 biological extinction Effects 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 238000004422 calculation algorithm Methods 0.000 description 1
- 244000309466 calf Species 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 230000021164 cell adhesion Effects 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 210000001072 colon Anatomy 0.000 description 1
- 238000000205 computational method Methods 0.000 description 1
- 238000004590 computer program Methods 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 230000009260 cross reactivity Effects 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 230000000368 destabilizing effect Effects 0.000 description 1
- 238000006471 dimerization reaction Methods 0.000 description 1
- VIYFPAMJCJLZKD-UHFFFAOYSA-L disodium;(4-nitrophenyl) phosphate Chemical compound [Na+].[Na+].[O-][N+](=O)C1=CC=C(OP([O-])([O-])=O)C=C1 VIYFPAMJCJLZKD-UHFFFAOYSA-L 0.000 description 1
- 239000006185 dispersion Substances 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 238000009510 drug design Methods 0.000 description 1
- 239000000975 dye Substances 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 238000000295 emission spectrum Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 230000005284 excitation Effects 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 239000007850 fluorescent dye Substances 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 102000034238 globular proteins Human genes 0.000 description 1
- 108091005896 globular proteins Proteins 0.000 description 1
- 229930195712 glutamate Natural products 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 238000003505 heat denaturation Methods 0.000 description 1
- 238000005570 heteronuclear single quantum coherence Methods 0.000 description 1
- 230000005660 hydrophilic surface Effects 0.000 description 1
- 230000005661 hydrophobic surface Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 239000002198 insoluble material Substances 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000012804 iterative process Methods 0.000 description 1
- 229930027917 kanamycin Natural products 0.000 description 1
- 229960000318 kanamycin Drugs 0.000 description 1
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 1
- 229930182823 kanamycin A Natural products 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 239000012139 lysis buffer Substances 0.000 description 1
- 238000002824 mRNA display Methods 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 150000002739 metals Chemical class 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 238000010606 normalization Methods 0.000 description 1
- 230000006849 nucleocytoplasmic transport Effects 0.000 description 1
- 230000030648 nucleus localization Effects 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 230000010412 perfusion Effects 0.000 description 1
- 238000002823 phage display Methods 0.000 description 1
- 239000008194 pharmaceutical composition Substances 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 238000011197 physicochemical method 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
- 208000015768 polyposis Diseases 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 150000003148 prolines Chemical class 0.000 description 1
- 238000003157 protein complementation Methods 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 229930182852 proteinogenic amino acid Natural products 0.000 description 1
- 238000001472 pulsed field gradient Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 210000003705 ribosome Anatomy 0.000 description 1
- 239000012146 running buffer Substances 0.000 description 1
- 238000007789 sealing Methods 0.000 description 1
- 230000011218 segmentation Effects 0.000 description 1
- 238000010187 selection method Methods 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 230000006641 stabilisation Effects 0.000 description 1
- 238000011105 stabilization Methods 0.000 description 1
- 238000012916 structural analysis Methods 0.000 description 1
- 230000007847 structural defect Effects 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 229910052717 sulfur Inorganic materials 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 235000019157 thiamine Nutrition 0.000 description 1
- KYMBYSLLVAOCFI-UHFFFAOYSA-N thiamine Chemical compound CC1=C(CCO)SCN1CC1=CN=C(C)N=C1N KYMBYSLLVAOCFI-UHFFFAOYSA-N 0.000 description 1
- 229960003495 thiamine Drugs 0.000 description 1
- 239000011721 thiamine Substances 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 238000010200 validation analysis Methods 0.000 description 1
- 238000011179 visual inspection Methods 0.000 description 1
- 238000012800 visualization Methods 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 238000002424 x-ray crystallography Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4702—Regulators; Modulating activity
- C07K14/4703—Inhibitors; Suppressors
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1034—Isolating an individual clone by screening libraries
- C12N15/1044—Preparation or screening of libraries displayed on scaffold proteins
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Wood Science & Technology (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biochemistry (AREA)
- Physics & Mathematics (AREA)
- Crystallography & Structural Chemistry (AREA)
- Microbiology (AREA)
- Plant Pathology (AREA)
- Bioinformatics & Computational Biology (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP07117059 | 2007-09-24 | ||
| EP07117059.1 | 2007-09-24 | ||
| PCT/EP2008/062671 WO2009040338A1 (en) | 2007-09-24 | 2008-09-23 | Designed armadillo repeat proteins |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2700391A1 true CA2700391A1 (en) | 2009-04-02 |
Family
ID=38962601
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA2700391A Abandoned CA2700391A1 (en) | 2007-09-24 | 2008-09-23 | Designed armadillo repeat proteins |
Country Status (5)
| Country | Link |
|---|---|
| US (1) | US9365629B2 (cg-RX-API-DMAC7.html) |
| EP (1) | EP2198022B1 (cg-RX-API-DMAC7.html) |
| JP (1) | JP2010539915A (cg-RX-API-DMAC7.html) |
| CA (1) | CA2700391A1 (cg-RX-API-DMAC7.html) |
| WO (1) | WO2009040338A1 (cg-RX-API-DMAC7.html) |
Families Citing this family (66)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US9089610B2 (en) | 2008-08-19 | 2015-07-28 | Nektar Therapeutics | Complexes of small-interfering nucleic acids |
| AR081361A1 (es) | 2010-04-30 | 2012-08-29 | Molecular Partners Ag | Proteinas de union modificadas que inhiben la interaccion de receptor del factor de crecimiento endotelial vascular de glicoproteina a vegf-a |
| DK2643349T3 (da) | 2010-11-26 | 2019-11-25 | Molecular Partners Ag | Designede repeat-proteiner, der binder til serumalbumin |
| RS58620B1 (sr) | 2011-02-15 | 2019-05-31 | Immunogen Inc | Metodi pripremanja konjugata |
| EA029797B1 (ru) | 2011-06-21 | 2018-05-31 | Иммуноджен, Инк. | Новые производные майтанзиноида с пептидным линкером и их конъюгаты |
| EP2887965A1 (en) | 2012-08-22 | 2015-07-01 | ImmunoGen, Inc. | Cytotoxic benzodiazepine derivatives |
| EP2738180A1 (en) | 2012-11-30 | 2014-06-04 | Molecular Partners AG | Binding proteins comprising at least two binding domains against HER2. |
| JP6423804B2 (ja) | 2013-02-28 | 2018-11-14 | イミュノジェン・インコーポレーテッド | 細胞結合剤及び細胞毒性剤を含む複合体 |
| WO2014134483A2 (en) | 2013-02-28 | 2014-09-04 | Immunogen, Inc. | Conjugates comprising cell-binding agents and cytotoxic agents |
| US11453708B2 (en) | 2013-05-31 | 2022-09-27 | Molecular Partners Ag | Designed ankyrin repeat proteins binding to hepatocyte growth factor |
| WO2014194030A2 (en) | 2013-05-31 | 2014-12-04 | Immunogen, Inc. | Conjugates comprising cell-binding agents and cytotoxic agents |
| MX389160B (es) | 2013-10-31 | 2025-03-20 | Hutchinson Fred Cancer Res | Células no t efectoras y madre/progenitoras hematopoyéticas modificadas y usos de estas. |
| CA2933707A1 (en) | 2013-12-20 | 2015-06-25 | Fred Hutchinson Cancer Research Center | Tagged chimeric effector molecules and receptors thereof |
| CN106605228B (zh) | 2014-07-07 | 2019-08-16 | 耶达研究及发展有限公司 | 计算蛋白质设计的方法 |
| KR20240023671A (ko) | 2014-09-03 | 2024-02-22 | 이뮤노젠 아이엔씨 | 세포독성 벤조다이아제핀 유도체 |
| TW201613930A (en) | 2014-09-03 | 2016-04-16 | Immunogen Inc | Cytotoxic benzodiazepine derivatives |
| ES2979088T3 (es) | 2015-03-05 | 2024-09-24 | Fred Hutchinson Cancer Center | Proteínas de fusión inmunomoduladoras y usos de las mismas |
| WO2016156596A1 (en) | 2015-04-02 | 2016-10-06 | Molecular Partners Ag | Designed ankyrin repeat domains with binding specificity for serum albumin |
| EP3288570A4 (en) | 2015-04-29 | 2018-11-21 | Fred Hutchinson Cancer Research Center | Modified stem cells and uses thereof |
| EP3288569A4 (en) | 2015-04-29 | 2018-12-19 | Fred Hutchinson Cancer Research Center | Modified hematopoietic stem/progenitor and non-t effector cells, and uses thereof |
| WO2017106728A2 (en) * | 2015-12-16 | 2017-06-22 | University Of Washington | Repeat protein architectures |
| NZ748378A (en) | 2016-04-14 | 2025-08-29 | Fred Hutchinson Cancer Center | Compositions and methods to program therapeutic cells using targeted nucleic acid nanocarriers |
| MX377424B (es) | 2016-09-22 | 2025-03-10 | Molecular Partners Ag | Proteinas de union recombinantes y sus usos |
| IL268349B2 (en) | 2017-02-17 | 2024-08-01 | Hutchinson Fred Cancer Res | Combination therapies for treatment of bcma-related cancers and autoimmune disorders |
| CN116785450A (zh) | 2017-02-28 | 2023-09-22 | 伊缪诺金公司 | 具有自分解肽接头的类美登素衍生物和其缀合物 |
| WO2018165046A1 (en) | 2017-03-07 | 2018-09-13 | Igc Bio, Inc. | A computational pipeline for antibody modeling and design |
| JP2020511136A (ja) | 2017-03-17 | 2020-04-16 | フレッド ハッチンソン キャンサー リサーチ センター | 免疫調節性融合タンパク質およびその使用 |
| WO2018195243A1 (en) | 2017-04-20 | 2018-10-25 | Immunogen, Inc. | Cytotoxic benzodiazepine derivatives and conjugates thereof |
| EP3732178A1 (en) | 2017-12-28 | 2020-11-04 | ImmunoGen, Inc. | Benzodiazepine derivatives |
| EP4268831A3 (en) | 2018-09-12 | 2024-05-22 | Fred Hutchinson Cancer Center | Reducing cd33 expression to selectively protect therapeutic cells |
| AU2020240310A1 (en) | 2019-03-21 | 2021-10-07 | Immunogen, Inc. | Methods of preparing cell-binding agent-drug conjugates |
| EP3947395A1 (en) | 2019-03-29 | 2022-02-09 | ImmunoGen, Inc. | Cytotoxic bis-benzodiazepine derivatives and conjugates thereof with cell-binding agents for inhibiting abnormal cell growth or for treating proliferative diseases |
| EP3958977B1 (en) | 2019-04-26 | 2023-09-13 | ImmunoGen, Inc. | Camptothecin derivatives |
| CA3139164A1 (en) | 2019-06-04 | 2020-12-10 | Molecular Partners Ag | Recombinant fap binding proteins and their use |
| CN114206908B (zh) | 2019-06-04 | 2025-12-23 | 分子伴侣公司 | 具有改善的稳定性的经设计的锚蛋白重复结构域 |
| EP3980452A1 (en) | 2019-06-04 | 2022-04-13 | Molecular Partners AG | Recombinant 4-1bb binding proteins and their use |
| BR112021026832A2 (pt) | 2019-07-02 | 2022-05-10 | Hutchinson Fred Cancer Res | Vetores ad35 recombinantes e aprimoramentos da terapia gênica relacionada |
| JP2023506763A (ja) | 2019-12-11 | 2023-02-20 | モレキュラー パートナーズ アクチェンゲゼルシャフト | 組換えペプチド－ｍｈｃ複合体結合タンパク質並びにそれらの生成及び使用 |
| WO2021116462A1 (en) | 2019-12-11 | 2021-06-17 | Molecular Partners Ag | Designed ankyrin repeat domains with altered surface residues |
| US20230142283A1 (en) * | 2020-03-05 | 2023-05-11 | University Of Washington | Rigid helical junctions for modular repeat protein sculpting and methods of use |
| TW202208404A (zh) | 2020-05-06 | 2022-03-01 | 瑞士商分子組合公司 | 新穎錨蛋白重複結合蛋白質及其用途 |
| CN115768786A (zh) | 2020-05-14 | 2023-03-07 | 分子合作伙伴股份公司 | 多特异性蛋白质 |
| US20240279309A1 (en) | 2020-05-14 | 2024-08-22 | Molecular Partners Ag | Recombinant cd40 binding proteins and their use |
| EP4263608A1 (en) | 2020-12-16 | 2023-10-25 | Molecular Partners AG | Recombinant cd3 binding proteins and their use |
| CA3202358A1 (en) | 2020-12-16 | 2022-06-23 | Andreas BOSSHART | Novel slow-release prodrugs |
| JP2024509904A (ja) | 2021-03-09 | 2024-03-05 | モレキュラー パートナーズ アクチェンゲゼルシャフト | 新規なＤＡＲＰｉｎに基づく多重特異性Ｔ細胞エンゲージャ |
| US20240150475A1 (en) | 2021-03-09 | 2024-05-09 | Molecular Partners Ag | Novel darpin based cd123 engagers |
| WO2022190008A1 (en) | 2021-03-09 | 2022-09-15 | Molecular Partners Ag | Protease cleavable prodrugs |
| CA3211248A1 (en) | 2021-03-09 | 2022-09-15 | Nina RESCHKE | Novel darpin based cd33 engagers |
| AU2022413461A1 (en) | 2021-12-14 | 2024-06-06 | Molecular Partners Ag | Designed repeat domains with dual binding specificity and their use |
| EP4460511A1 (en) * | 2022-01-07 | 2024-11-13 | Universität Zürich | Stabilizing n-cap sequences for armadillo repeat proteins |
| WO2023215725A1 (en) | 2022-05-02 | 2023-11-09 | Fred Hutchinson Cancer Center | Compositions and methods for cellular immunotherapy |
| CN119731200A (zh) | 2022-08-01 | 2025-03-28 | 分子合作伙伴股份公司 | 经电荷修饰设计的重复结构域及其用途 |
| WO2024179981A1 (en) | 2023-02-27 | 2024-09-06 | Molecular Partners Ag | Darpins for use in reducing renal accumulation of drugs |
| WO2024251628A1 (en) | 2023-06-06 | 2024-12-12 | Molecular Partners Ag | Recombinant cd16a binding proteins and their use |
| WO2024251695A1 (en) | 2023-06-06 | 2024-12-12 | Molecular Partners Ag | Recombinant cd47 binding proteins and their use |
| WO2024251742A1 (en) | 2023-06-06 | 2024-12-12 | Molecular Partners Ag | Recombinant cd2 binding proteins and their use |
| WO2025068607A1 (en) * | 2023-09-29 | 2025-04-03 | Universität Zürich | Modular armadillo repeat proteins |
| WO2025101820A1 (en) | 2023-11-08 | 2025-05-15 | Fred Hutchinson Cancer Center | Compositions and methods for cellular immunotherapy |
| WO2025146487A1 (en) | 2024-01-05 | 2025-07-10 | Molecular Partners Ag | Multispecific binding proteins |
| WO2025146490A1 (en) | 2024-01-05 | 2025-07-10 | Molecular Partners Ag | Recombinant cd117 binding proteins and their use |
| WO2025146491A1 (en) | 2024-01-05 | 2025-07-10 | Molecular Partners Ag | Designed repeat domains with dual binding specificity for cd117 and cd47-binding agent |
| WO2025163144A1 (en) | 2024-01-31 | 2025-08-07 | Molecular Partners Ag | Recombinant mesothelin binding proteins and their use |
| US20250332297A1 (en) | 2024-01-31 | 2025-10-30 | Molecular Partners Ag | Dll3-specific binding constructs and their use in radiotherapy |
| WO2025181039A1 (en) | 2024-03-01 | 2025-09-04 | Molecular Partners Ag | Therapeutic combinations comprising a multi-specific t cell engager |
| WO2025245169A1 (en) | 2024-05-21 | 2025-11-27 | Fred Hutchinson Cancer Center | Immunotherapy cells equipped with a collagen-targeting payload |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ES2335861T3 (es) | 2000-09-08 | 2010-04-06 | Universitat Zurich | Grupos de proteinas repetitivas que comprenden modulos repetitivos. |
| WO2002101008A2 (en) * | 2001-06-08 | 2002-12-19 | Incyte Genomics Inc. | Intracellular signaling molecules |
| US7049482B1 (en) * | 2004-11-30 | 2006-05-23 | Korea Kumho Petrochemical Co., Ltd. | Nucleic acid molecule encoding an armadillo repeat protein, aria and a method utilizing aria to generate salt tolerant plants |
-
2008
- 2008-09-23 WO PCT/EP2008/062671 patent/WO2009040338A1/en not_active Ceased
- 2008-09-23 EP EP08804590.1A patent/EP2198022B1/en active Active
- 2008-09-23 JP JP2010526268A patent/JP2010539915A/ja active Pending
- 2008-09-23 CA CA2700391A patent/CA2700391A1/en not_active Abandoned
- 2008-09-23 US US12/733,836 patent/US9365629B2/en active Active
Also Published As
| Publication number | Publication date |
|---|---|
| US20110224100A1 (en) | 2011-09-15 |
| US9365629B2 (en) | 2016-06-14 |
| EP2198022B1 (en) | 2024-03-06 |
| EP2198022C0 (en) | 2024-03-06 |
| JP2010539915A (ja) | 2010-12-24 |
| EP2198022A1 (en) | 2010-06-23 |
| WO2009040338A1 (en) | 2009-04-02 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US9365629B2 (en) | Designed armadillo repeat proteins | |
| McKnight et al. | A thermostable 35-residue subdomain within villin headpiece | |
| CN103403024B (zh) | 设计的锚蛋白重复蛋白的改进的n‑端加帽模块 | |
| Pérez-Cañadillas et al. | The highly refined solution structure of the cytotoxic ribonuclease α-sarcin reveals the structural requirements for substrate recognition and ribonucleolytic activity | |
| Tamburro et al. | Localizing α-helices in human tropoelastin: assembly of the elastin “puzzle” | |
| HUE031800T2 (en) | Modified Stefin A framework proteins | |
| JP2014205669A (ja) | ペプチド構造のライブラリーの構築およびスクリーニング方法 | |
| EP2161278B1 (en) | Single-chain coiled coil scaffold | |
| EP4192851B1 (en) | N-terminal capping modules of ankyrin repeat domains | |
| Chen et al. | Effects of turn residues in directing the formation of the β‐sheet and in the stability of the β‐sheet | |
| EP4323388B1 (en) | N-terminal capping modules of ankyrin repeat domains | |
| Gururaja et al. | A novel artificial loop scaffold for the noncovalent constraint of peptides | |
| US20210284695A1 (en) | Folded and protease-resistant polypeptides | |
| US20240247036A1 (en) | N-Terminal Capping Modules of Ankyrin Repeat Domains | |
| Donovan et al. | Total synthesis of bovine pancreatic trypsin inhibitor and the protein diastereomer [Gly37D‐Ala] BPTI using Boc chemistry solid phase peptide synthesis | |
| Vetter et al. | Phosphorylation of serine residues affects the conformation of the calmodulin binding domain of human protein 4.1 | |
| Jeon et al. | Evidence for binary Smc complexes lacking kite subunits in archaea | |
| Aoki-Shioi et al. | Isolation and functional diversity of Bowman–Birk type serine proteinase inhibitors from Hyacinthus orientalis | |
| Kim et al. | Designed leucine‐rich repeat proteins bind two muramyl dipeptide ligands | |
| Stewart et al. | Redesign of a WW domain peptide for selective recognition of single-stranded DNA | |
| Rao | Structural and functional studies of cysteine-rich proteomimetic scaffolds | |
| Skwierawska et al. | Conformational studies of the α‐helical 28–43 fragment of the B3 domain of the immunoglobulin binding protein G from Streptococcus | |
| Dutta et al. | De novo design, synthesis and solution conformational study of two didehydroundecapeptides: effect of nature and number of amino acids interspersed between Phe residues | |
| Kang et al. | Recombinant preparation and characterization of interactions for a calmodulin‐binding chromogranin A peptide and calmodulin | |
| Tököli | Design Strategies for Protein-Protein Interaction Inhibitors Using Non-Natural Amino Acids |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FZDE | Discontinued |
Effective date: 20140923 |