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
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Genetics & Genomics (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Biophysics (AREA)
- Wood Science & Technology (AREA)
- Molecular Biology (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Toxicology (AREA)
- Physics & Mathematics (AREA)
- Crystallography & Structural Chemistry (AREA)
- Plant Pathology (AREA)
- Bioinformatics & Computational Biology (AREA)
- Microbiology (AREA)
- Medicinal Chemistry (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP07117059.1 | 2007-09-24 | ||
| EP07117059 | 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 (enExample) |
| EP (1) | EP2198022B1 (enExample) |
| JP (1) | JP2010539915A (enExample) |
| CA (1) | CA2700391A1 (enExample) |
| WO (1) | WO2009040338A1 (enExample) |
Families Citing this family (66)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US9433684B2 (en) | 2008-08-19 | 2016-09-06 | Nektar Therapeutics | Conjugates of small-interfering nucleic acids |
| TWI510246B (zh) | 2010-04-30 | 2015-12-01 | Molecular Partners Ag | 抑制vegf-a受體交互作用的經修飾結合性蛋白質 |
| US9284361B2 (en) | 2010-11-26 | 2016-03-15 | Molecular Partners Ag | Designed repeat proteins binding to serum albumin |
| SG191955A1 (en) | 2011-02-15 | 2013-08-30 | Immunogen Inc | Cytotoxic benzodiazepine derivatives |
| JP6209159B2 (ja) | 2011-06-21 | 2017-10-04 | イミュノジェン・インコーポレーテッド | ペプチドリンカーを有する新規メイタンシノイド誘導体およびその結合体 |
| WO2014031566A1 (en) | 2012-08-22 | 2014-02-27 | 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 |
| WO2014194030A2 (en) | 2013-05-31 | 2014-12-04 | Immunogen, Inc. | Conjugates comprising cell-binding agents and cytotoxic agents |
| WO2014191574A1 (en) | 2013-05-31 | 2014-12-04 | Molecular Partners Ag | Designed ankyrin repeat proteins binding to hepatocyte growth factor |
| CN105873952A (zh) | 2013-10-31 | 2016-08-17 | 弗莱德哈钦森癌症研究中心 | 经修饰的造血干细胞/祖细胞和非t效应细胞及其用途 |
| PL3083671T3 (pl) | 2013-12-20 | 2021-03-22 | Fred Hutchinson Cancer Center | Znakowane chimeryczne cząsteczki efektorowe i ich receptory |
| US10665324B2 (en) | 2014-07-07 | 2020-05-26 | Yeda Research And Development Co. Ltd. | Method of computational protein design |
| MX2017002758A (es) | 2014-09-03 | 2017-10-20 | Immunogen Inc | Derivados de benzodiazepina citotoxicos. |
| JP2017527562A (ja) | 2014-09-03 | 2017-09-21 | イミュノジェン・インコーポレーテッド | 細胞毒性ベンゾジアゼピン誘導体 |
| HK1246317A1 (zh) | 2015-03-05 | 2018-09-07 | Fred Hutchinson Cancer Center | 免疫调节融合蛋白及其用途 |
| SG11201707606RA (en) | 2015-04-02 | 2017-10-30 | Molecular Partners Ag | Designed ankyrin repeat domains with binding specificity for serum albumin |
| 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 |
| WO2016176652A2 (en) | 2015-04-29 | 2016-11-03 | Fred Hutchinson Cancer Research Center | Modified stem cells and uses thereof |
| WO2017106728A2 (en) * | 2015-12-16 | 2017-06-22 | University Of Washington | Repeat protein architectures |
| CR20180503A (es) | 2016-04-14 | 2018-12-21 | Hutchinson Fred Cancer Res | Composiciones y métodos para programar células terapéuticas utilizando nanoportadores de ácidos nucleicos dirigidos |
| KR102270315B1 (ko) | 2016-09-22 | 2021-06-29 | 몰리큘라 파트너스 아게 | 재조합 결합 단백질 및 그의 용도 |
| CA3052779A1 (en) | 2017-02-17 | 2018-08-23 | Fred Hutchinson Cancer Research Center | Combination therapies for treatment of bcma-related cancers and autoimmune disorders |
| SG10202109376YA (en) | 2017-02-28 | 2021-10-28 | Immunogen Inc | Maytansinoid derivatives with self-immolative peptide linkers and conjugates thereof |
| 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 |
| WO2019133652A1 (en) | 2017-12-28 | 2019-07-04 | Immunogen, Inc. | Benzodiazepine derivatives |
| US12398402B2 (en) | 2018-09-12 | 2025-08-26 | Fred Hutchinson Cancer Center | Reducing CD33 expression to selectively protect therapeutic cells |
| CA3133802A1 (en) | 2019-03-21 | 2020-09-24 | Immunogen, Inc. | Methods of preparing cell-binding agent-drug conjugates |
| CN113661172A (zh) | 2019-03-29 | 2021-11-16 | 伊缪诺金公司 | 用于抑制异常细胞生长或治疗增生性疾病的细胞毒性双苯并二氮杂䓬衍生物及其与细胞结合剂的缀合物 |
| CN119119176A (zh) | 2019-04-26 | 2024-12-13 | 伊缪诺金公司 | 喜树碱衍生物 |
| AU2020286715A1 (en) | 2019-06-04 | 2021-12-23 | Molecular Partners Ag | Recombinant 4-1 BB binding proteins and their use |
| CN114269366A (zh) | 2019-06-04 | 2022-04-01 | 分子伴侣公司 | 重组fap结合蛋白及其用途 |
| CA3138805A1 (en) | 2019-06-04 | 2020-12-10 | Johannes Schilling | Designed ankyrin repeat domain with improved stability |
| SG11202111943UA (en) | 2019-07-02 | 2021-11-29 | Hutchinson Fred Cancer Res | Recombinant ad35 vectors and related gene therapy improvements |
| US20230041822A1 (en) | 2019-12-11 | 2023-02-09 | Molecular Partners Ag | Recombinant peptide-mhc complex binding proteins and their generation and use |
| CA3161326A1 (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 |
| BR112022023049A2 (pt) | 2020-05-14 | 2022-12-20 | Molecular Partners Ag | Proteínas multiespecíficas |
| JP2023528207A (ja) | 2020-05-14 | 2023-07-04 | 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cd40結合タンパク質及びそれらの使用 |
| US20240108746A1 (en) | 2020-12-16 | 2024-04-04 | Molecular Partners Ag | Novel slow-release prodrugs |
| WO2022129428A1 (en) | 2020-12-16 | 2022-06-23 | Molecular Partners Ag | Recombinant cd3 binding proteins and their use |
| CA3211248A1 (en) | 2021-03-09 | 2022-09-15 | Nina RESCHKE | Novel darpin based cd33 engagers |
| EP4305063A1 (en) | 2021-03-09 | 2024-01-17 | Molecular Partners AG | Protease cleavable prodrugs |
| WO2022190016A1 (en) | 2021-03-09 | 2022-09-15 | Molecular Partners Ag | Novel darpin based multi-specific t-cell engagers |
| CA3211368A1 (en) | 2021-03-09 | 2022-09-15 | Molecular Partners Ag | Novel darpin based cd123 engagers |
| WO2023110983A1 (en) | 2021-12-14 | 2023-06-22 | Molecular Partners Ag | Designed repeat domains with dual binding specificity and their use |
| US20250368704A1 (en) * | 2022-01-07 | 2025-12-04 | 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 |
| CA3262553A1 (en) | 2022-08-01 | 2024-02-08 | Molecular Partners Ag | REHEARSAL AREAS DESIGNED WITH MODIFIED CHARGES AND THEIR USE |
| WO2024179981A1 (en) | 2023-02-27 | 2024-09-06 | Molecular Partners Ag | Darpins for use in reducing renal accumulation of drugs |
| WO2024251695A1 (en) | 2023-06-06 | 2024-12-12 | Molecular Partners Ag | Recombinant cd47 binding proteins and their use |
| WO2024251628A1 (en) | 2023-06-06 | 2024-12-12 | Molecular Partners Ag | Recombinant cd16a 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 |
| WO2025146491A1 (en) | 2024-01-05 | 2025-07-10 | Molecular Partners Ag | Designed repeat domains with dual binding specificity for cd117 and cd47-binding agent |
| 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 |
| WO2025163082A1 (en) | 2024-01-31 | 2025-08-07 | Molecular Partners Ag | Dll3-specific binding constructs and their use in radiotherapy |
| WO2025163144A1 (en) | 2024-01-31 | 2025-08-07 | Molecular Partners Ag | Recombinant mesothelin binding proteins and their use |
| 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 |
|---|---|---|---|---|
| US7417130B2 (en) * | 2000-09-08 | 2008-08-26 | University Of Zurich | Collection of repeat proteins comprising repeat modules |
| US20060115813A1 (en) * | 2001-06-08 | 2006-06-01 | Incyte Corporation | 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 US US12/733,836 patent/US9365629B2/en active Active
- 2008-09-23 CA CA2700391A patent/CA2700391A1/en not_active Abandoned
- 2008-09-23 EP EP08804590.1A patent/EP2198022B1/en active Active
- 2008-09-23 JP JP2010526268A patent/JP2010539915A/ja active Pending
- 2008-09-23 WO PCT/EP2008/062671 patent/WO2009040338A1/en not_active Ceased
Also Published As
| Publication number | Publication date |
|---|---|
| EP2198022B1 (en) | 2024-03-06 |
| WO2009040338A1 (en) | 2009-04-02 |
| EP2198022C0 (en) | 2024-03-06 |
| US9365629B2 (en) | 2016-06-14 |
| US20110224100A1 (en) | 2011-09-15 |
| EP2198022A1 (en) | 2010-06-23 |
| JP2010539915A (ja) | 2010-12-24 |
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 | |
| AU2007218045B2 (en) | Method of constructing and screening libraries of peptide structures | |
| 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 | |
| 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 | |
| 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 | |
| Kumar | Structure, Function and Folding of Three Finger Toxins |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FZDE | Discontinued |
Effective date: 20140923 |