JP4293292B2 - トランスフェクション活性を有するインテグリン−ターゲッティングベクター - Google Patents
トランスフェクション活性を有するインテグリン−ターゲッティングベクター Download PDFInfo
- Publication number
- JP4293292B2 JP4293292B2 JP55077198A JP55077198A JP4293292B2 JP 4293292 B2 JP4293292 B2 JP 4293292B2 JP 55077198 A JP55077198 A JP 55077198A JP 55077198 A JP55077198 A JP 55077198A JP 4293292 B2 JP4293292 B2 JP 4293292B2
- Authority
- JP
- Japan
- Prior art keywords
- complex
- peptide
- nucleic acid
- transfection
- component
- 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.)
- Expired - Fee Related
Links
- 238000001890 transfection Methods 0.000 title abstract description 123
- 230000000694 effects Effects 0.000 title abstract description 22
- 239000013598 vector Substances 0.000 title description 21
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 96
- 108010044426 integrins Proteins 0.000 claims abstract description 78
- 102000006495 integrins Human genes 0.000 claims abstract description 78
- 230000027455 binding Effects 0.000 claims abstract description 68
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 64
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 64
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 64
- 150000002632 lipids Chemical class 0.000 claims abstract description 61
- 125000002091 cationic group Chemical group 0.000 claims abstract description 23
- 210000004027 cell Anatomy 0.000 claims description 106
- 239000000203 mixture Substances 0.000 claims description 40
- 108090000623 proteins and genes Proteins 0.000 claims description 40
- 150000001413 amino acids Chemical group 0.000 claims description 39
- 238000000034 method Methods 0.000 claims description 34
- LDGWQMRUWMSZIU-LQDDAWAPSA-M 2,3-bis[(z)-octadec-9-enoxy]propyl-trimethylazanium;chloride Chemical compound [Cl-].CCCCCCCC\C=C/CCCCCCCCOCC(C[N+](C)(C)C)OCCCCCCCC\C=C/CCCCCCCC LDGWQMRUWMSZIU-LQDDAWAPSA-M 0.000 claims description 25
- 102000004169 proteins and genes Human genes 0.000 claims description 21
- IYMAXBFPHPZYIK-BQBZGAKWSA-N Arg-Gly-Asp Chemical compound NC(N)=NCCC[C@H](N)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(O)=O IYMAXBFPHPZYIK-BQBZGAKWSA-N 0.000 claims description 20
- 230000000692 anti-sense effect Effects 0.000 claims description 20
- 238000002560 therapeutic procedure Methods 0.000 claims description 18
- 238000004519 manufacturing process Methods 0.000 claims description 12
- 239000012528 membrane Substances 0.000 claims description 11
- 238000001727 in vivo Methods 0.000 claims description 9
- 239000002131 composite material Substances 0.000 claims description 8
- 238000000338 in vitro Methods 0.000 claims description 7
- 230000000799 fusogenic effect Effects 0.000 claims description 6
- 230000001225 therapeutic effect Effects 0.000 claims description 6
- 239000003814 drug Substances 0.000 claims description 5
- 230000007935 neutral effect Effects 0.000 claims description 5
- 230000002265 prevention Effects 0.000 claims description 5
- 230000000069 prophylactic effect Effects 0.000 claims description 5
- KSXTUUUQYQYKCR-LQDDAWAPSA-M 2,3-bis[[(z)-octadec-9-enoyl]oxy]propyl-trimethylazanium;chloride Chemical compound [Cl-].CCCCCCCC\C=C/CCCCCCCC(=O)OCC(C[N+](C)(C)C)OC(=O)CCCCCCC\C=C/CCCCCCCC KSXTUUUQYQYKCR-LQDDAWAPSA-M 0.000 claims description 3
- 238000002649 immunization Methods 0.000 claims description 3
- 230000003053 immunization Effects 0.000 claims description 3
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 claims description 3
- 150000008104 phosphatidylethanolamines Chemical class 0.000 claims description 3
- JZNWSCPGTDBMEW-UHFFFAOYSA-N Glycerophosphorylethanolamin Natural products NCCOP(O)(=O)OCC(O)CO JZNWSCPGTDBMEW-UHFFFAOYSA-N 0.000 claims description 2
- 230000007812 deficiency Effects 0.000 claims description 2
- 230000001687 destabilization Effects 0.000 claims description 2
- 230000036039 immunity Effects 0.000 claims description 2
- 239000008194 pharmaceutical composition Substances 0.000 claims description 2
- 150000001768 cations Chemical class 0.000 claims 2
- 210000005260 human cell Anatomy 0.000 claims 2
- 108010039918 Polylysine Proteins 0.000 claims 1
- 229940009098 aspartate Drugs 0.000 claims 1
- 238000012217 deletion Methods 0.000 claims 1
- 230000037430 deletion Effects 0.000 claims 1
- MWRBNPKJOOWZPW-CLFAGFIQSA-N dioleoyl phosphatidylethanolamine Chemical compound CCCCCCCC\C=C/CCCCCCCC(=O)OCC(COP(O)(=O)OCCN)OC(=O)CCCCCCC\C=C/CCCCCCCC MWRBNPKJOOWZPW-CLFAGFIQSA-N 0.000 claims 1
- 229920000656 polylysine Polymers 0.000 claims 1
- 239000002502 liposome Substances 0.000 abstract description 8
- HMNZFMSWFCAGGW-XPWSMXQVSA-N [3-[hydroxy(2-hydroxyethoxy)phosphoryl]oxy-2-[(e)-octadec-9-enoyl]oxypropyl] (e)-octadec-9-enoate Chemical compound CCCCCCCC\C=C\CCCCCCCC(=O)OCC(COP(O)(=O)OCCO)OC(=O)CCCCCCC\C=C\CCCCCCCC HMNZFMSWFCAGGW-XPWSMXQVSA-N 0.000 description 100
- 108020004414 DNA Proteins 0.000 description 66
- 239000013612 plasmid Substances 0.000 description 64
- 235000001014 amino acid Nutrition 0.000 description 33
- 101100297345 Caenorhabditis elegans pgl-2 gene Proteins 0.000 description 26
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 24
- 102000004196 processed proteins & peptides Human genes 0.000 description 24
- 238000002156 mixing Methods 0.000 description 23
- 239000003446 ligand Substances 0.000 description 19
- 230000001404 mediated effect Effects 0.000 description 19
- 238000001415 gene therapy Methods 0.000 description 18
- 230000014509 gene expression Effects 0.000 description 17
- 239000002245 particle Substances 0.000 description 17
- 235000018102 proteins Nutrition 0.000 description 17
- 229960005486 vaccine Drugs 0.000 description 17
- XULFJDKZVHTRLG-JDVCJPALSA-N DOSPA trifluoroacetate Chemical compound [O-]C(=O)C(F)(F)F.CCCCCCCC\C=C/CCCCCCCCOCC(C[N+](C)(C)CCNC(=O)C(CCCNCCCN)NCCCN)OCCCCCCCC\C=C/CCCCCCCC XULFJDKZVHTRLG-JDVCJPALSA-N 0.000 description 12
- 239000000463 material Substances 0.000 description 12
- 230000004568 DNA-binding Effects 0.000 description 11
- 108060001084 Luciferase Proteins 0.000 description 10
- 239000005089 Luciferase Substances 0.000 description 10
- 230000004570 RNA-binding Effects 0.000 description 10
- 108700008625 Reporter Genes Proteins 0.000 description 10
- 125000000217 alkyl group Chemical group 0.000 description 10
- 238000011282 treatment Methods 0.000 description 10
- 206010029260 Neuroblastoma Diseases 0.000 description 9
- 230000003321 amplification Effects 0.000 description 9
- 238000004630 atomic force microscopy Methods 0.000 description 9
- 238000003199 nucleic acid amplification method Methods 0.000 description 9
- 239000000243 solution Substances 0.000 description 9
- 102000013462 Interleukin-12 Human genes 0.000 description 8
- 108010065805 Interleukin-12 Proteins 0.000 description 8
- 108090000190 Thrombin Proteins 0.000 description 8
- 210000003958 hematopoietic stem cell Anatomy 0.000 description 8
- 229940117681 interleukin-12 Drugs 0.000 description 8
- 239000002953 phosphate buffered saline Substances 0.000 description 8
- 230000008569 process Effects 0.000 description 8
- 229960004072 thrombin Drugs 0.000 description 8
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 7
- 210000004072 lung Anatomy 0.000 description 7
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 7
- 239000000074 antisense oligonucleotide Substances 0.000 description 6
- 238000012230 antisense oligonucleotides Methods 0.000 description 6
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 6
- 238000005516 engineering process Methods 0.000 description 6
- 238000002474 experimental method Methods 0.000 description 6
- 230000008685 targeting Effects 0.000 description 6
- 239000013603 viral vector Substances 0.000 description 6
- OPIFSICVWOWJMJ-AEOCFKNESA-N 5-bromo-4-chloro-3-indolyl beta-D-galactoside Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1OC1=CNC2=CC=C(Br)C(Cl)=C12 OPIFSICVWOWJMJ-AEOCFKNESA-N 0.000 description 5
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 5
- 239000012124 Opti-MEM Substances 0.000 description 5
- 210000004413 cardiac myocyte Anatomy 0.000 description 5
- 230000000368 destabilizing effect Effects 0.000 description 5
- 201000010099 disease Diseases 0.000 description 5
- 210000002889 endothelial cell Anatomy 0.000 description 5
- -1 neutral lipids Chemical class 0.000 description 5
- 238000002255 vaccination Methods 0.000 description 5
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 4
- 206010028980 Neoplasm Diseases 0.000 description 4
- 108091034117 Oligonucleotide Proteins 0.000 description 4
- 102000005936 beta-Galactosidase Human genes 0.000 description 4
- 108010005774 beta-Galactosidase Proteins 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- 239000003153 chemical reaction reagent Substances 0.000 description 4
- 108010045325 cyclic arginine-glycine-aspartic acid peptide Proteins 0.000 description 4
- 210000001163 endosome Anatomy 0.000 description 4
- 210000002919 epithelial cell Anatomy 0.000 description 4
- 210000002950 fibroblast Anatomy 0.000 description 4
- 239000001963 growth medium Substances 0.000 description 4
- 230000001177 retroviral effect Effects 0.000 description 4
- 210000000329 smooth muscle myocyte Anatomy 0.000 description 4
- 230000032258 transport Effects 0.000 description 4
- 230000003612 virological effect Effects 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 3
- 201000003883 Cystic fibrosis Diseases 0.000 description 3
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 3
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 3
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 3
- 239000004472 Lysine Substances 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 230000006041 cell recruitment Effects 0.000 description 3
- 239000003795 chemical substances by application Substances 0.000 description 3
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 3
- 231100000673 dose–response relationship Toxicity 0.000 description 3
- 210000000871 endothelium corneal Anatomy 0.000 description 3
- 229940088598 enzyme Drugs 0.000 description 3
- 210000000981 epithelium Anatomy 0.000 description 3
- 125000001495 ethyl group Chemical group [H]C([H])([H])C([H])([H])* 0.000 description 3
- 239000012894 fetal calf serum Substances 0.000 description 3
- 238000009472 formulation Methods 0.000 description 3
- 230000004927 fusion Effects 0.000 description 3
- 230000002068 genetic effect Effects 0.000 description 3
- 208000015181 infectious disease Diseases 0.000 description 3
- 238000003670 luciferase enzyme activity assay Methods 0.000 description 3
- 230000007246 mechanism Effects 0.000 description 3
- 239000002609 medium Substances 0.000 description 3
- 201000001441 melanoma Diseases 0.000 description 3
- 238000011275 oncology therapy Methods 0.000 description 3
- 244000052769 pathogen Species 0.000 description 3
- 230000008782 phagocytosis Effects 0.000 description 3
- 150000003904 phospholipids Chemical class 0.000 description 3
- 230000035755 proliferation Effects 0.000 description 3
- 238000010186 staining Methods 0.000 description 3
- 210000001519 tissue Anatomy 0.000 description 3
- 238000012546 transfer Methods 0.000 description 3
- 108020004491 Antisense DNA Proteins 0.000 description 2
- 108020000948 Antisense Oligonucleotides Proteins 0.000 description 2
- OBMZMSLWNNWEJA-XNCRXQDQSA-N C1=CC=2C(C[C@@H]3NC(=O)[C@@H](NC(=O)[C@H](NC(=O)N(CC#CCN(CCCC[C@H](NC(=O)[C@@H](CC4=CC=CC=C4)NC3=O)C(=O)N)CC=C)NC(=O)[C@@H](N)C)CC3=CNC4=C3C=CC=C4)C)=CNC=2C=C1 Chemical compound C1=CC=2C(C[C@@H]3NC(=O)[C@@H](NC(=O)[C@H](NC(=O)N(CC#CCN(CCCC[C@H](NC(=O)[C@@H](CC4=CC=CC=C4)NC3=O)C(=O)N)CC=C)NC(=O)[C@@H](N)C)CC3=CNC4=C3C=CC=C4)C)=CNC=2C=C1 OBMZMSLWNNWEJA-XNCRXQDQSA-N 0.000 description 2
- 241000282693 Cercopithecidae Species 0.000 description 2
- 108010069514 Cyclic Peptides Proteins 0.000 description 2
- 102000001189 Cyclic Peptides Human genes 0.000 description 2
- 102000004127 Cytokines Human genes 0.000 description 2
- 108090000695 Cytokines Proteins 0.000 description 2
- 238000002965 ELISA Methods 0.000 description 2
- 241000931304 Eriachne Species 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 108091028043 Nucleic acid sequence Proteins 0.000 description 2
- 108010088535 Pep-1 peptide Proteins 0.000 description 2
- 101710176384 Peptide 1 Proteins 0.000 description 2
- 101710121440 Proteinase-activated receptor 1 Proteins 0.000 description 2
- 241000700159 Rattus Species 0.000 description 2
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 2
- 239000003875 Wang resin Substances 0.000 description 2
- 230000000840 anti-viral effect Effects 0.000 description 2
- 239000000427 antigen Substances 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
- 108091007433 antigens Proteins 0.000 description 2
- 239000003816 antisense DNA Substances 0.000 description 2
- 208000006673 asthma Diseases 0.000 description 2
- 238000006664 bond formation reaction Methods 0.000 description 2
- 210000001185 bone marrow Anatomy 0.000 description 2
- 230000021164 cell adhesion Effects 0.000 description 2
- 230000033077 cellular process Effects 0.000 description 2
- 210000002806 clathrin-coated vesicle Anatomy 0.000 description 2
- 230000009918 complex formation Effects 0.000 description 2
- 210000000805 cytoplasm Anatomy 0.000 description 2
- 230000003247 decreasing effect Effects 0.000 description 2
- 230000007547 defect Effects 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 239000012634 fragment Substances 0.000 description 2
- 238000011239 genetic vaccination Methods 0.000 description 2
- 230000036541 health Effects 0.000 description 2
- 230000006872 improvement Effects 0.000 description 2
- 230000003834 intracellular effect Effects 0.000 description 2
- 230000010189 intracellular transport Effects 0.000 description 2
- 150000002500 ions Chemical class 0.000 description 2
- 210000001985 kidney epithelial cell Anatomy 0.000 description 2
- SRCAXTIBNLIRHU-JJKPAIEPSA-N lantibiotic pep5 Chemical compound N([C@@H](C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@H](CS)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N\C(=C/C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N\C(=C/C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N\C(=C(/C)S)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CS)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)NCC(=O)N[C@@H](CS)C(=O)N[C@@H](CCCCN)C(O)=O)C(=O)[C@@H]1CCCN1C(=O)CNC(=O)[C@H](C)NC(=O)C(=O)CC SRCAXTIBNLIRHU-JJKPAIEPSA-N 0.000 description 2
- 208000032839 leukemia Diseases 0.000 description 2
- 230000010534 mechanism of action Effects 0.000 description 2
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 2
- 239000000178 monomer Substances 0.000 description 2
- 210000003205 muscle Anatomy 0.000 description 2
- 210000004940 nucleus Anatomy 0.000 description 2
- 108700025694 p53 Genes Proteins 0.000 description 2
- 238000002823 phage display Methods 0.000 description 2
- 239000013600 plasmid vector Substances 0.000 description 2
- 230000010837 receptor-mediated endocytosis Effects 0.000 description 2
- 102000005962 receptors Human genes 0.000 description 2
- 108020003175 receptors Proteins 0.000 description 2
- 239000011347 resin Substances 0.000 description 2
- 229920005989 resin Polymers 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 208000037803 restenosis Diseases 0.000 description 2
- 238000004007 reversed phase HPLC Methods 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- 210000000130 stem cell Anatomy 0.000 description 2
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 238000002054 transplantation Methods 0.000 description 2
- 210000004881 tumor cell Anatomy 0.000 description 2
- 210000003606 umbilical vein Anatomy 0.000 description 2
- 101150099695 vps11 gene Proteins 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- QGVLYPPODPLXMB-UBTYZVCOSA-N (1aR,1bS,4aR,7aS,7bS,8R,9R,9aS)-4a,7b,9,9a-tetrahydroxy-3-(hydroxymethyl)-1,1,6,8-tetramethyl-1,1a,1b,4,4a,7a,7b,8,9,9a-decahydro-5H-cyclopropa[3,4]benzo[1,2-e]azulen-5-one Chemical compound C1=C(CO)C[C@]2(O)C(=O)C(C)=C[C@H]2[C@@]2(O)[C@H](C)[C@@H](O)[C@@]3(O)C(C)(C)[C@H]3[C@@H]21 QGVLYPPODPLXMB-UBTYZVCOSA-N 0.000 description 1
- WHTVZRBIWZFKQO-AWEZNQCLSA-N (S)-chloroquine Chemical compound ClC1=CC=C2C(N[C@@H](C)CCCN(CC)CC)=CC=NC2=C1 WHTVZRBIWZFKQO-AWEZNQCLSA-N 0.000 description 1
- DHBXNPKRAUYBTH-UHFFFAOYSA-N 1,1-ethanedithiol Chemical compound CC(S)S DHBXNPKRAUYBTH-UHFFFAOYSA-N 0.000 description 1
- XFZYPCNLVHSQTG-UHFFFAOYSA-N 2,2,5,7,8-pentamethyl-3,4-dihydrochromene Chemical compound C1CC(C)(C)OC2=C(C)C(C)=CC(C)=C21 XFZYPCNLVHSQTG-UHFFFAOYSA-N 0.000 description 1
- WOGWYSWDBYCVDY-UHFFFAOYSA-N 2-chlorocyclohexa-2,5-diene-1,4-dione Chemical compound ClC1=CC(=O)C=CC1=O WOGWYSWDBYCVDY-UHFFFAOYSA-N 0.000 description 1
- TWJNQYPJQDRXPH-UHFFFAOYSA-N 2-cyanobenzohydrazide Chemical compound NNC(=O)C1=CC=CC=C1C#N TWJNQYPJQDRXPH-UHFFFAOYSA-N 0.000 description 1
- 125000000954 2-hydroxyethyl group Chemical group [H]C([*])([H])C([H])([H])O[H] 0.000 description 1
- 241000251468 Actinopterygii Species 0.000 description 1
- 241000271566 Aves Species 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 108010077805 Bacterial Proteins Proteins 0.000 description 1
- 108090000565 Capsid Proteins Proteins 0.000 description 1
- 101710169873 Capsid protein G8P Proteins 0.000 description 1
- 102100023321 Ceruloplasmin Human genes 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 101800001224 Disintegrin Proteins 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 201000008808 Fibrosarcoma Diseases 0.000 description 1
- 241000724791 Filamentous phage Species 0.000 description 1
- 241000710198 Foot-and-mouth disease virus Species 0.000 description 1
- 208000010412 Glaucoma Diseases 0.000 description 1
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 1
- 102000004457 Granulocyte-Macrophage Colony-Stimulating Factor Human genes 0.000 description 1
- 108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 description 1
- 241000700721 Hepatitis B virus Species 0.000 description 1
- 208000026350 Inborn Genetic disease Diseases 0.000 description 1
- 102100022337 Integrin alpha-V Human genes 0.000 description 1
- 108010008212 Integrin alpha4beta1 Proteins 0.000 description 1
- 108010040765 Integrin alphaV Proteins 0.000 description 1
- 101710198693 Invasin Proteins 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
- 229930182816 L-glutamine Natural products 0.000 description 1
- 101710125418 Major capsid protein Proteins 0.000 description 1
- 101710156564 Major tail protein Gp23 Proteins 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- TUNFSRHWOTWDNC-UHFFFAOYSA-N Myristic acid Natural products CCCCCCCCCCCCCC(O)=O TUNFSRHWOTWDNC-UHFFFAOYSA-N 0.000 description 1
- 235000021360 Myristic acid Nutrition 0.000 description 1
- 208000022873 Ocular disease Diseases 0.000 description 1
- 229930182555 Penicillin Natural products 0.000 description 1
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
- 206010057249 Phagocytosis Diseases 0.000 description 1
- 101100428706 Schizosaccharomyces pombe (strain 972 / ATCC 24843) vps26 gene Proteins 0.000 description 1
- 102100028904 Serine/threonine-protein kinase MARK2 Human genes 0.000 description 1
- 108010008038 Synthetic Vaccines Proteins 0.000 description 1
- 102000003790 Thrombin receptors Human genes 0.000 description 1
- 108090000166 Thrombin receptors Proteins 0.000 description 1
- 239000007984 Tris EDTA buffer Substances 0.000 description 1
- 108020005202 Viral DNA Proteins 0.000 description 1
- 108700005077 Viral Genes Proteins 0.000 description 1
- 208000036142 Viral infection Diseases 0.000 description 1
- 208000025087 Yersinia pseudotuberculosis infectious disease Diseases 0.000 description 1
- CLZISMQKJZCZDN-UHFFFAOYSA-N [benzotriazol-1-yloxy(dimethylamino)methylidene]-dimethylazanium Chemical compound C1=CC=C2N(OC(N(C)C)=[N+](C)C)N=NC2=C1 CLZISMQKJZCZDN-UHFFFAOYSA-N 0.000 description 1
- 230000005856 abnormality Effects 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 150000001370 alpha-amino acid derivatives Chemical class 0.000 description 1
- 235000008206 alpha-amino acids Nutrition 0.000 description 1
- 238000002399 angioplasty Methods 0.000 description 1
- 210000002159 anterior chamber Anatomy 0.000 description 1
- 238000011319 anticancer therapy Methods 0.000 description 1
- 210000003433 aortic smooth muscle cell Anatomy 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 108010072041 arginyl-glycyl-aspartic acid Proteins 0.000 description 1
- 210000004507 artificial chromosome Anatomy 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 239000012298 atmosphere Substances 0.000 description 1
- 230000003416 augmentation Effects 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 210000000621 bronchi Anatomy 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 210000000234 capsid Anatomy 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 230000008614 cellular interaction Effects 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 229960003677 chloroquine Drugs 0.000 description 1
- WHTVZRBIWZFKQO-UHFFFAOYSA-N chloroquine Natural products ClC1=CC=C2C(NC(C)CCCN(CC)CC)=CC=NC2=C1 WHTVZRBIWZFKQO-UHFFFAOYSA-N 0.000 description 1
- 239000013065 commercial product Substances 0.000 description 1
- 238000009833 condensation Methods 0.000 description 1
- 230000005494 condensation Effects 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 210000004087 cornea Anatomy 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 239000006059 cover glass Substances 0.000 description 1
- 125000004122 cyclic group Chemical group 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- 208000035475 disorder Diseases 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 238000005538 encapsulation Methods 0.000 description 1
- 230000012202 endocytosis Effects 0.000 description 1
- 230000003511 endothelial effect Effects 0.000 description 1
- 238000010195 expression analysis Methods 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 210000002744 extracellular matrix Anatomy 0.000 description 1
- 208000030533 eye disease Diseases 0.000 description 1
- 230000001605 fetal effect Effects 0.000 description 1
- 238000002073 fluorescence micrograph Methods 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 238000012637 gene transfection Methods 0.000 description 1
- 230000009395 genetic defect Effects 0.000 description 1
- 208000016361 genetic disease Diseases 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 229960002743 glutamine Drugs 0.000 description 1
- XMBWDFGMSWQBCA-UHFFFAOYSA-N hydrogen iodide Chemical compound I XMBWDFGMSWQBCA-UHFFFAOYSA-N 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 230000005847 immunogenicity Effects 0.000 description 1
- 238000009169 immunotherapy Methods 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 102000029719 integrin binding proteins Human genes 0.000 description 1
- 108091009291 integrin binding proteins Proteins 0.000 description 1
- 230000008611 intercellular interaction Effects 0.000 description 1
- 230000001788 irregular Effects 0.000 description 1
- 238000011694 lewis rat Methods 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 239000012139 lysis buffer Substances 0.000 description 1
- 230000036210 malignancy Effects 0.000 description 1
- 230000003211 malignant effect Effects 0.000 description 1
- 238000001840 matrix-assisted laser desorption--ionisation time-of-flight mass spectrometry Methods 0.000 description 1
- 239000010445 mica Substances 0.000 description 1
- 229910052618 mica group Inorganic materials 0.000 description 1
- 238000000386 microscopy Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 210000004165 myocardium Anatomy 0.000 description 1
- 210000003757 neuroblast Anatomy 0.000 description 1
- 210000000633 nuclear envelope Anatomy 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 229940049954 penicillin Drugs 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- QGVLYPPODPLXMB-QXYKVGAMSA-N phorbol Natural products C[C@@H]1[C@@H](O)[C@]2(O)[C@H]([C@H]3C=C(CO)C[C@@]4(O)[C@H](C=C(C)C4=O)[C@@]13O)C2(C)C QGVLYPPODPLXMB-QXYKVGAMSA-N 0.000 description 1
- 125000001095 phosphatidyl group Chemical group 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 125000006239 protecting group Chemical group 0.000 description 1
- 238000002731 protein assay Methods 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 150000003242 quaternary ammonium salts Chemical group 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 229940124551 recombinant vaccine Drugs 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000007363 ring formation reaction Methods 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 230000019491 signal transduction Effects 0.000 description 1
- 239000003998 snake venom Substances 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 239000012798 spherical particle Substances 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 239000011550 stock solution Substances 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 229960005322 streptomycin Drugs 0.000 description 1
- 239000003104 tissue culture media Substances 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- ZGYICYBLPGRURT-UHFFFAOYSA-N tri(propan-2-yl)silicon Chemical compound CC(C)[Si](C(C)C)C(C)C ZGYICYBLPGRURT-UHFFFAOYSA-N 0.000 description 1
- 125000002221 trityl group Chemical group [H]C1=C([H])C([H])=C([H])C([H])=C1C([*])(C1=C(C(=C(C(=C1[H])[H])[H])[H])[H])C1=C([H])C([H])=C([H])C([H])=C1[H] 0.000 description 1
- 210000005239 tubule Anatomy 0.000 description 1
- 241000701161 unidentified adenovirus Species 0.000 description 1
- 241001529453 unidentified herpesvirus Species 0.000 description 1
- 230000009385 viral infection Effects 0.000 description 1
Images
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K48/00—Medicinal preparations containing genetic material which is inserted into cells of the living body to treat genetic diseases; Gene therapy
-
- 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
- C12N15/87—Introduction of foreign genetic material using processes not otherwise provided for, e.g. co-transformation
- C12N15/88—Introduction of foreign genetic material using processes not otherwise provided for, e.g. co-transformation using microencapsulation, e.g. using amphiphile liposome vesicle
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S977/00—Nanotechnology
- Y10S977/902—Specified use of nanostructure
- Y10S977/904—Specified use of nanostructure for medical, immunological, body treatment, or diagnosis
- Y10S977/906—Drug delivery
- Y10S977/907—Liposome
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Chemical & Material Sciences (AREA)
- Biotechnology (AREA)
- Organic Chemistry (AREA)
- Molecular Biology (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Health & Medical Sciences (AREA)
- Biomedical Technology (AREA)
- General Engineering & Computer Science (AREA)
- Plant Pathology (AREA)
- Epidemiology (AREA)
- Biophysics (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Microbiology (AREA)
- Physics & Mathematics (AREA)
- Pharmacology & Pharmacy (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Medicinal Preparation (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Enzymes And Modification Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Electrotherapy Devices (AREA)
- Compression Or Coding Systems Of Tv Signals (AREA)
- Ultra Sonic Daignosis Equipment (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB9711115.7 | 1997-05-29 | ||
| GBGB9711115.7A GB9711115D0 (en) | 1997-05-29 | 1997-05-29 | Integrin-targeting vectors having enhanced transfection activity |
| PCT/GB1998/001577 WO1998054347A1 (en) | 1997-05-29 | 1998-05-29 | Integrin-targeting vectors having transfection activity |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2002502243A JP2002502243A (ja) | 2002-01-22 |
| JP2002502243A5 JP2002502243A5 (https=) | 2005-12-08 |
| JP4293292B2 true JP4293292B2 (ja) | 2009-07-08 |
Family
ID=10813246
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP55077198A Expired - Fee Related JP4293292B2 (ja) | 1997-05-29 | 1998-05-29 | トランスフェクション活性を有するインテグリン−ターゲッティングベクター |
Country Status (9)
| Country | Link |
|---|---|
| US (2) | US6458026B1 (https=) |
| EP (1) | EP1003898B1 (https=) |
| JP (1) | JP4293292B2 (https=) |
| AT (1) | ATE301722T1 (https=) |
| AU (1) | AU7667398A (https=) |
| CA (1) | CA2288840A1 (https=) |
| DE (1) | DE69831156T2 (https=) |
| GB (1) | GB9711115D0 (https=) |
| WO (1) | WO1998054347A1 (https=) |
Families Citing this family (27)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1230441C (zh) | 2000-04-12 | 2005-12-07 | 安盛药业有限公司 | 结合整联蛋白的肽衍生物 |
| AU2001258659A1 (en) * | 2000-05-30 | 2001-12-11 | Ich Productions Limited | Improved methods of transfection |
| EP1178117A1 (en) * | 2000-08-02 | 2002-02-06 | Erasmus Universiteit Rotterdam | Targeting through integrins |
| NO20004795D0 (no) | 2000-09-26 | 2000-09-26 | Nycomed Imaging As | Peptidbaserte forbindelser |
| US8613907B2 (en) * | 2000-10-12 | 2013-12-24 | University Of Rochester | Compositions that inhibit proliferation of cancer cells |
| GB0106315D0 (en) | 2001-03-14 | 2001-05-02 | Ich Productions Ltd | Transfection complexes |
| CA2449054C (en) * | 2001-05-30 | 2011-01-04 | The Scripps Research Institute | Integrin targeting liposome for nucleic acid delivery |
| WO2003006491A2 (en) | 2001-07-10 | 2003-01-23 | Amersham Health As | Peptide-based compounds for targeting intergin receptors |
| US7598421B2 (en) | 2002-05-08 | 2009-10-06 | Ucl Biomedica Plc | Materials for the delivery of biologically-active material to cells |
| GB0210538D0 (en) * | 2002-05-08 | 2002-06-19 | Univ London | Lipids and gene delivery |
| WO2004096140A2 (en) * | 2003-04-25 | 2004-11-11 | The Penn State Research Foundation | Method and system for systemic delivery of growth arresting, lipid-derived bioactive compounds |
| GB0313132D0 (en) * | 2003-06-06 | 2003-07-09 | Ich Productions Ltd | Peptide ligands |
| US8133733B2 (en) | 2003-10-24 | 2012-03-13 | Gencia Corporation | Nonviral vectors for delivering polynucleotides to target tissues |
| EP1687017B1 (en) | 2003-10-24 | 2013-03-06 | Gencia Corporation | Methods and compositions for delivering polynucleotides |
| US8507277B2 (en) | 2003-10-24 | 2013-08-13 | Gencia Corporation | Nonviral vectors for delivering polynucleotides |
| US20090123468A1 (en) | 2003-10-24 | 2009-05-14 | Gencia Corporation | Transducible polypeptides for modifying metabolism |
| US8062891B2 (en) | 2003-10-24 | 2011-11-22 | Gencia Corporation | Nonviral vectors for delivering polynucleotides to plants |
| AU2007211334A1 (en) * | 2006-02-01 | 2007-08-09 | Board Of Supervisors Of Louisiana State University And Agricultural And Mechanical College | Polypeptide-nucleic acid conjugate for immunoprophylaxis or immunotherapy for neoplastic or infectious disorders |
| US10034674B2 (en) * | 2006-02-02 | 2018-07-31 | Steven C Chudik | Universal anterior cruciate ligament repair and reconstruction system |
| GB0610636D0 (en) * | 2006-05-30 | 2006-07-05 | Univ London | Materials and complexes for the delivery of biologically-active material to cells |
| RU2010107199A (ru) * | 2007-07-31 | 2011-09-10 | Дзе Джонс Хопкинс Юниверсити (Us) | Конъюгат полипептид-нуклеиновая кислота для иммунопрофилактики или иммунотерапии для неопластических или инфекционных нарушений |
| PT2252627T (pt) * | 2008-01-24 | 2017-07-24 | Esperance Pharmaceuticals | Constructos de fusão de domínio lítico e métodos para produzir e utilizar os mesmos |
| US20110256055A1 (en) | 2008-12-23 | 2011-10-20 | Ge Healthcare Limited | Application of 99mtc peptide-based compound as a bone marrow imaging agent |
| EP4710943A3 (en) | 2015-08-28 | 2026-04-29 | Molecular Transfer, Inc. | Transfection complexes and methods of using the same |
| CN108779074A (zh) | 2016-03-01 | 2018-11-09 | 分子传递有限公司 | 植物病毒移动蛋白和其使用方法 |
| GB201604235D0 (en) | 2016-03-11 | 2016-04-27 | Ucl Business Plc | Lipids and complexes for the delivery of biologically-active material to cells |
| GB201803419D0 (en) * | 2018-03-02 | 2018-04-18 | Ucl Business Plc | Complex for the delivery of cas9 proteins guide RNA to cells |
Family Cites Families (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5981478A (en) | 1993-11-24 | 1999-11-09 | La Jolla Cancer Research Foundation | Integrin-binding peptides |
| CA2204254C (en) | 1994-11-17 | 2010-02-16 | Stephen Lewis Hart | Internalisation of dna, using conjugates of poly-l-lysine and an integrin receptor ligand |
| US5736392A (en) * | 1995-06-07 | 1998-04-07 | Life Technologies, Inc. | Peptide-enhanced cationic lipid transfections |
| US5908777A (en) | 1995-06-23 | 1999-06-01 | University Of Pittsburgh | Lipidic vector for nucleic acid delivery |
-
1997
- 1997-05-29 GB GBGB9711115.7A patent/GB9711115D0/en active Pending
-
1998
- 1998-05-29 DE DE69831156T patent/DE69831156T2/de not_active Expired - Lifetime
- 1998-05-29 AU AU76673/98A patent/AU7667398A/en not_active Abandoned
- 1998-05-29 CA CA002288840A patent/CA2288840A1/en not_active Abandoned
- 1998-05-29 US US09/424,656 patent/US6458026B1/en not_active Expired - Lifetime
- 1998-05-29 AT AT98924478T patent/ATE301722T1/de not_active IP Right Cessation
- 1998-05-29 EP EP98924478A patent/EP1003898B1/en not_active Expired - Lifetime
- 1998-05-29 JP JP55077198A patent/JP4293292B2/ja not_active Expired - Fee Related
- 1998-05-29 WO PCT/GB1998/001577 patent/WO1998054347A1/en not_active Ceased
-
2002
- 2002-05-03 US US10/137,435 patent/US20030013644A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| WO1998054347A1 (en) | 1998-12-03 |
| US20030013644A1 (en) | 2003-01-16 |
| DE69831156T2 (de) | 2006-06-08 |
| US6458026B1 (en) | 2002-10-01 |
| DE69831156D1 (de) | 2005-09-15 |
| ATE301722T1 (de) | 2005-08-15 |
| AU7667398A (en) | 1998-12-30 |
| US20020042384A1 (en) | 2002-04-11 |
| CA2288840A1 (en) | 1998-12-03 |
| EP1003898A1 (en) | 2000-05-31 |
| GB9711115D0 (en) | 1997-07-23 |
| EP1003898B1 (en) | 2005-08-10 |
| JP2002502243A (ja) | 2002-01-22 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP4293292B2 (ja) | トランスフェクション活性を有するインテグリン−ターゲッティングベクター | |
| AU722700B2 (en) | Lipophilic peptides for macromolecule delivery | |
| Wyman et al. | Design, synthesis, and characterization of a cationic peptide that binds to nucleic acids and permeabilizes bilayers | |
| Hart | Multifunctional nanocomplexes for gene transfer and gene therapy | |
| Cryan et al. | Increased intracellular targeting to airway cells using octaarginine-coated liposomes: in vitro assessment of their suitability for inhalation | |
| CA2222550A1 (en) | Nucleic acid transporters for delivery of nucleic acids into a cell | |
| Aschmann et al. | Lipid-based nanoparticle functionalization with coiled-coil peptides for in vitro and in vivo drug delivery | |
| Welser et al. | Gene delivery using ternary lipopolyplexes incorporating branched cationic peptides: the role of peptide sequence and branching | |
| JPH10505242A (ja) | キメラペントンベースタンパク質を含有する組換えアデノウイルス | |
| US20030220264A1 (en) | Reversible modification of membrane interaction | |
| JP2021502380A (ja) | ｍＲＮＡを細胞に送達するための改善した脂質−ペプチドナノ複合体製剤 | |
| Anwer et al. | Peptide-mediated gene transfer of cationic lipid/plasmid DNA complexes to endothelial cells | |
| Mustapa et al. | Stabilized integrin-targeting ternary LPD (lipopolyplex) vectors for gene delivery designed to disassemble within the target cell | |
| US7741431B2 (en) | Liposomes containing novel targeting and/or fusogenic peptides, preparations containing them and therapeutic use thereof | |
| JP2002541125A (ja) | エアロゾル送達のためのポリエチレンイミン：ｄｎａ製剤 | |
| WO2001092542A2 (en) | Integrin-targeting vectors having enhanced transfection activity | |
| EP1007549B1 (en) | Compositions and methods for highly efficient transfection | |
| US20040014217A1 (en) | Methods of transfection | |
| Midoux et al. | Peptide-based gene delivery systems | |
| JP2004508341A (ja) | Ｖｐ２２タンパク質／核酸凝集体とその使用 | |
| Smith et al. | DNA DELIVERY SYSTEMS BASED ON SYNTHETIC PEPTIDES | |
| Peluffo | Modular multifunctional protein vectors for gene therapy | |
| Nwachuku | An investigation of peptide-based translocating systems and their potential for gene therapy | |
| Subramanian | Rate limiting steps in nonviral gene transfer and the design of nuclear targeting scaffolds for the improved transfection of endothelium |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A711 | Notification of change in applicant |
Free format text: JAPANESE INTERMEDIATE CODE: A711 Effective date: 20040914 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20050513 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20050513 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20071023 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20080123 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20080303 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20080222 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20080331 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20080319 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20080701 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20081001 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20081110 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20081104 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20081215 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20081201 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20090119 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20081226 |
|
| TRDD | Decision of grant or rejection written | ||
| A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 Effective date: 20090303 |
|
| A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 |
|
| A61 | First payment of annual fees (during grant procedure) |
Free format text: JAPANESE INTERMEDIATE CODE: A61 Effective date: 20090331 |
|
| FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20120417 Year of fee payment: 3 |
|
| R150 | Certificate of patent or registration of utility model |
Free format text: JAPANESE INTERMEDIATE CODE: R150 |
|
| LAPS | Cancellation because of no payment of annual fees |