Polymers containing enzymatically degradable bonds, 7Part 6, cf. Biomaterials 3, 150 (1982). Design of oligopeptide side-chains in poly[N-(2-hydroxypropyl)methacrylamide] copolymers to promote efficient degradation by lysosomal enzymesDedicated to Professor Otto Wichterle on the occasion of his 70th birthday
N-(2-Hydroxypropyl)methacrylamide copolymers are considered to be a potential drug delivery system. To fulfil this role the drug-polymer linkage must be susceptible to intralysosomal hydrolysis. Taking p-nitroanilide as a drug analogue, copolymers were synthesized bearing oligopeptidyl-p-nitroanilid...
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Gespeichert in:
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| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
1983 |
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| Umfang: |
6 Ill. ; 2 Tab. 12 |
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| Reproduktion: |
Wiley InterScience Backfile Collection 1832-2000 |
|---|---|
| Übergeordnetes Werk: |
in: Die Makromolekulare Chemie - New York : Hüthig & Wepf Verlag, 184(1983) vom: Okt., Seite 1997-2008 |
| Übergeordnetes Werk: |
volume:184 ; year:1983 ; month:10 ; pages:1997-2008 ; extent:12 |
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| 520 | |a N-(2-Hydroxypropyl)methacrylamide copolymers are considered to be a potential drug delivery system. To fulfil this role the drug-polymer linkage must be susceptible to intralysosomal hydrolysis. Taking p-nitroanilide as a drug analogue, copolymers were synthesized bearing oligopeptidyl-p-nitroanilide side-chains designed to match known specificities of the lysosomal enzymes cathepsin L or cathepsin D. Degradation of side-chains by rat liver lysosomal enzymes (measured by monitoring terminal p-nitroaniline release) occurred only in the presence of reduced glutathione (5 mmol/l) and was effectively inhibited by leupeptin, indicating the involvement of thiol-proteinases in every case. Depending on side-chain composition, between 20 and more than 50% of the terminal p-nitroaniline residues were liberated during a 5 h incubation. It has also been shown that 1) a polymer molecule may contain side-chains of a single type that are nevertheless differentially susceptible to lysosomal hydrolysis; 2) two of the side-chains studied liberate only a p-nitroaniline residue, whereas the others also release amino-acyl-p-nitroanilides; 3) the cleavage of all side-chains displays a broad pH optimum pH 5 to pH 7; 4) the Michaelis-Menten constant Km for side-chain cleavage varied between 26,1 and 143,2 mg/ml, depending on the amino acid sequence of the side-chain. | ||
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(DE-627)NLEJ16385419X DE-627 ger DE-627 rakwb eng Polymers containing enzymatically degradable bonds, 7Part 6, cf. Biomaterials 3, 150 (1982). Design of oligopeptide side-chains in poly[N-(2-hydroxypropyl)methacrylamide] copolymers to promote efficient degradation by lysosomal enzymesDedicated to Professor Otto Wichterle on the occasion of his 70th birthday 1983 6 Ill. 2 Tab. 12 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier N-(2-Hydroxypropyl)methacrylamide copolymers are considered to be a potential drug delivery system. To fulfil this role the drug-polymer linkage must be susceptible to intralysosomal hydrolysis. Taking p-nitroanilide as a drug analogue, copolymers were synthesized bearing oligopeptidyl-p-nitroanilide side-chains designed to match known specificities of the lysosomal enzymes cathepsin L or cathepsin D. Degradation of side-chains by rat liver lysosomal enzymes (measured by monitoring terminal p-nitroaniline release) occurred only in the presence of reduced glutathione (5 mmol/l) and was effectively inhibited by leupeptin, indicating the involvement of thiol-proteinases in every case. Depending on side-chain composition, between 20 and more than 50% of the terminal p-nitroaniline residues were liberated during a 5 h incubation. It has also been shown that 1) a polymer molecule may contain side-chains of a single type that are nevertheless differentially susceptible to lysosomal hydrolysis; 2) two of the side-chains studied liberate only a p-nitroaniline residue, whereas the others also release amino-acyl-p-nitroanilides; 3) the cleavage of all side-chains displays a broad pH optimum pH 5 to pH 7; 4) the Michaelis-Menten constant Km for side-chain cleavage varied between 26,1 and 143,2 mg/ml, depending on the amino acid sequence of the side-chain. Wiley InterScience Backfile Collection 1832-2000 Duncan, Ruth oth Cable, Hazel C. oth Lloyd, John B. oth Rejmanová, Pavla oth Kopeček, Jindřich oth in Die Makromolekulare Chemie New York : Hüthig & Wepf Verlag 184(1983) vom: Okt., Seite 1997-2008 (DE-627)NLEJ159071488 0025-116X nnns volume:184 year:1983 month:10 pages:1997-2008 extent:12 http://dx.doi.org/10.1002/macp.1983.021841005 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 184 1983 10 1997-2008 12 |
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(DE-627)NLEJ16385419X DE-627 ger DE-627 rakwb eng Polymers containing enzymatically degradable bonds, 7Part 6, cf. Biomaterials 3, 150 (1982). Design of oligopeptide side-chains in poly[N-(2-hydroxypropyl)methacrylamide] copolymers to promote efficient degradation by lysosomal enzymesDedicated to Professor Otto Wichterle on the occasion of his 70th birthday 1983 6 Ill. 2 Tab. 12 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier N-(2-Hydroxypropyl)methacrylamide copolymers are considered to be a potential drug delivery system. To fulfil this role the drug-polymer linkage must be susceptible to intralysosomal hydrolysis. Taking p-nitroanilide as a drug analogue, copolymers were synthesized bearing oligopeptidyl-p-nitroanilide side-chains designed to match known specificities of the lysosomal enzymes cathepsin L or cathepsin D. Degradation of side-chains by rat liver lysosomal enzymes (measured by monitoring terminal p-nitroaniline release) occurred only in the presence of reduced glutathione (5 mmol/l) and was effectively inhibited by leupeptin, indicating the involvement of thiol-proteinases in every case. Depending on side-chain composition, between 20 and more than 50% of the terminal p-nitroaniline residues were liberated during a 5 h incubation. It has also been shown that 1) a polymer molecule may contain side-chains of a single type that are nevertheless differentially susceptible to lysosomal hydrolysis; 2) two of the side-chains studied liberate only a p-nitroaniline residue, whereas the others also release amino-acyl-p-nitroanilides; 3) the cleavage of all side-chains displays a broad pH optimum pH 5 to pH 7; 4) the Michaelis-Menten constant Km for side-chain cleavage varied between 26,1 and 143,2 mg/ml, depending on the amino acid sequence of the side-chain. Wiley InterScience Backfile Collection 1832-2000 Duncan, Ruth oth Cable, Hazel C. oth Lloyd, John B. oth Rejmanová, Pavla oth Kopeček, Jindřich oth in Die Makromolekulare Chemie New York : Hüthig & Wepf Verlag 184(1983) vom: Okt., Seite 1997-2008 (DE-627)NLEJ159071488 0025-116X nnns volume:184 year:1983 month:10 pages:1997-2008 extent:12 http://dx.doi.org/10.1002/macp.1983.021841005 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 184 1983 10 1997-2008 12 |
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(DE-627)NLEJ16385419X DE-627 ger DE-627 rakwb eng Polymers containing enzymatically degradable bonds, 7Part 6, cf. Biomaterials 3, 150 (1982). Design of oligopeptide side-chains in poly[N-(2-hydroxypropyl)methacrylamide] copolymers to promote efficient degradation by lysosomal enzymesDedicated to Professor Otto Wichterle on the occasion of his 70th birthday 1983 6 Ill. 2 Tab. 12 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier N-(2-Hydroxypropyl)methacrylamide copolymers are considered to be a potential drug delivery system. To fulfil this role the drug-polymer linkage must be susceptible to intralysosomal hydrolysis. Taking p-nitroanilide as a drug analogue, copolymers were synthesized bearing oligopeptidyl-p-nitroanilide side-chains designed to match known specificities of the lysosomal enzymes cathepsin L or cathepsin D. Degradation of side-chains by rat liver lysosomal enzymes (measured by monitoring terminal p-nitroaniline release) occurred only in the presence of reduced glutathione (5 mmol/l) and was effectively inhibited by leupeptin, indicating the involvement of thiol-proteinases in every case. Depending on side-chain composition, between 20 and more than 50% of the terminal p-nitroaniline residues were liberated during a 5 h incubation. It has also been shown that 1) a polymer molecule may contain side-chains of a single type that are nevertheless differentially susceptible to lysosomal hydrolysis; 2) two of the side-chains studied liberate only a p-nitroaniline residue, whereas the others also release amino-acyl-p-nitroanilides; 3) the cleavage of all side-chains displays a broad pH optimum pH 5 to pH 7; 4) the Michaelis-Menten constant Km for side-chain cleavage varied between 26,1 and 143,2 mg/ml, depending on the amino acid sequence of the side-chain. Wiley InterScience Backfile Collection 1832-2000 Duncan, Ruth oth Cable, Hazel C. oth Lloyd, John B. oth Rejmanová, Pavla oth Kopeček, Jindřich oth in Die Makromolekulare Chemie New York : Hüthig & Wepf Verlag 184(1983) vom: Okt., Seite 1997-2008 (DE-627)NLEJ159071488 0025-116X nnns volume:184 year:1983 month:10 pages:1997-2008 extent:12 http://dx.doi.org/10.1002/macp.1983.021841005 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 184 1983 10 1997-2008 12 |
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Polymers containing enzymatically degradable bonds, 7Part 6, cf. Biomaterials 3, 150 (1982). Design of oligopeptide side-chains in poly[N-(2-hydroxypropyl)methacrylamide] copolymers to promote efficient degradation by lysosomal enzymesDedicated to Professor Otto Wichterle on the occasion of his 70th birthday |
| abstract |
N-(2-Hydroxypropyl)methacrylamide copolymers are considered to be a potential drug delivery system. To fulfil this role the drug-polymer linkage must be susceptible to intralysosomal hydrolysis. Taking p-nitroanilide as a drug analogue, copolymers were synthesized bearing oligopeptidyl-p-nitroanilide side-chains designed to match known specificities of the lysosomal enzymes cathepsin L or cathepsin D. Degradation of side-chains by rat liver lysosomal enzymes (measured by monitoring terminal p-nitroaniline release) occurred only in the presence of reduced glutathione (5 mmol/l) and was effectively inhibited by leupeptin, indicating the involvement of thiol-proteinases in every case. Depending on side-chain composition, between 20 and more than 50% of the terminal p-nitroaniline residues were liberated during a 5 h incubation. It has also been shown that 1) a polymer molecule may contain side-chains of a single type that are nevertheless differentially susceptible to lysosomal hydrolysis; 2) two of the side-chains studied liberate only a p-nitroaniline residue, whereas the others also release amino-acyl-p-nitroanilides; 3) the cleavage of all side-chains displays a broad pH optimum pH 5 to pH 7; 4) the Michaelis-Menten constant Km for side-chain cleavage varied between 26,1 and 143,2 mg/ml, depending on the amino acid sequence of the side-chain. |
| abstractGer |
N-(2-Hydroxypropyl)methacrylamide copolymers are considered to be a potential drug delivery system. To fulfil this role the drug-polymer linkage must be susceptible to intralysosomal hydrolysis. Taking p-nitroanilide as a drug analogue, copolymers were synthesized bearing oligopeptidyl-p-nitroanilide side-chains designed to match known specificities of the lysosomal enzymes cathepsin L or cathepsin D. Degradation of side-chains by rat liver lysosomal enzymes (measured by monitoring terminal p-nitroaniline release) occurred only in the presence of reduced glutathione (5 mmol/l) and was effectively inhibited by leupeptin, indicating the involvement of thiol-proteinases in every case. Depending on side-chain composition, between 20 and more than 50% of the terminal p-nitroaniline residues were liberated during a 5 h incubation. It has also been shown that 1) a polymer molecule may contain side-chains of a single type that are nevertheless differentially susceptible to lysosomal hydrolysis; 2) two of the side-chains studied liberate only a p-nitroaniline residue, whereas the others also release amino-acyl-p-nitroanilides; 3) the cleavage of all side-chains displays a broad pH optimum pH 5 to pH 7; 4) the Michaelis-Menten constant Km for side-chain cleavage varied between 26,1 and 143,2 mg/ml, depending on the amino acid sequence of the side-chain. |
| abstract_unstemmed |
N-(2-Hydroxypropyl)methacrylamide copolymers are considered to be a potential drug delivery system. To fulfil this role the drug-polymer linkage must be susceptible to intralysosomal hydrolysis. Taking p-nitroanilide as a drug analogue, copolymers were synthesized bearing oligopeptidyl-p-nitroanilide side-chains designed to match known specificities of the lysosomal enzymes cathepsin L or cathepsin D. Degradation of side-chains by rat liver lysosomal enzymes (measured by monitoring terminal p-nitroaniline release) occurred only in the presence of reduced glutathione (5 mmol/l) and was effectively inhibited by leupeptin, indicating the involvement of thiol-proteinases in every case. Depending on side-chain composition, between 20 and more than 50% of the terminal p-nitroaniline residues were liberated during a 5 h incubation. It has also been shown that 1) a polymer molecule may contain side-chains of a single type that are nevertheless differentially susceptible to lysosomal hydrolysis; 2) two of the side-chains studied liberate only a p-nitroaniline residue, whereas the others also release amino-acyl-p-nitroanilides; 3) the cleavage of all side-chains displays a broad pH optimum pH 5 to pH 7; 4) the Michaelis-Menten constant Km for side-chain cleavage varied between 26,1 and 143,2 mg/ml, depending on the amino acid sequence of the side-chain. |
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Polymers containing enzymatically degradable bonds, 7Part 6, cf. Biomaterials 3, 150 (1982). Design of oligopeptide side-chains in poly[N-(2-hydroxypropyl)methacrylamide] copolymers to promote efficient degradation by lysosomal enzymesDedicated to Professor Otto Wichterle on the occasion of his 70th birthday |
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Duncan, Ruth Cable, Hazel C. Lloyd, John B. Rejmanová, Pavla Kopeček, Jindřich |
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