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Structure-Based Design, Synthesis, and Biological Evaluation of Irreversible Human Rhinovirus 3C Protease Inhibitors. 1. Michael Acceptor Structure−Activity Studies

Dragovich, Peter S ; Webber, Stephen E ; Babine, Robert E ; Fuhrman, Shella A ; Patick, Amy K ; Matthews, David A ; Lee, Caroline A ; Reich, Siegfried H ; Prins, Thomas J ; Marakovits, Joseph T ; Littlefield, Ethel S ; Zhou, Ru ; Tikhe, Jayashree ; Ford, Clifford E ; Wallace, Michael B ; Meador, James W ; Ferre, Rose Ann ; Brown, Edward L ; Binford, Susan L ; Harr, James E. V ; DeLisle, Dorothy M ; Worland, Stephen T

Journal of medicinal chemistry, 1998-07, Vol.41 (15), p.2806-2818 [Periódico revisado por pares]

Washington, DC: American Chemical Society

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Título:
Structure-Based Design, Synthesis, and Biological Evaluation of Irreversible Human Rhinovirus 3C Protease Inhibitors. 1. Michael Acceptor Structure−Activity Studies
Autor: Dragovich, Peter S ; Webber, Stephen E ; Babine, Robert E ; Fuhrman, Shella A ; Patick, Amy K ; Matthews, David A ; Lee, Caroline A ; Reich, Siegfried H ; Prins, Thomas J ; Marakovits, Joseph T ; Littlefield, Ethel S ; Zhou, Ru ; Tikhe, Jayashree ; Ford, Clifford E ; Wallace, Michael B ; Meador, James W ; Ferre, Rose Ann ; Brown, Edward L ; Binford, Susan L ; Harr, James E. V ; DeLisle, Dorothy M ; Worland, Stephen T
Assuntos: 3C Viral Proteases ; 3CP ; Animals ; Antibiotics. Antiinfectious agents. Antiparasitic agents ; Antiviral agents ; Antiviral Agents - chemical synthesis ; Antiviral Agents - chemistry ; Antiviral Agents - metabolism ; Antiviral Agents - pharmacology ; Binding Sites ; Biological and medical sciences ; Cell Line, Transformed ; Crystallography, X-Ray ; Cysteine Endopeptidases - chemistry ; Cysteine Endopeptidases - metabolism ; Cysteine Proteinase Inhibitors - chemical synthesis ; Cysteine Proteinase Inhibitors - chemistry ; Cysteine Proteinase Inhibitors - metabolism ; Cysteine Proteinase Inhibitors - pharmacology ; Drug Design ; Drug Stability ; HeLa Cells ; Human rhinovirus ; Humans ; Medical sciences ; Oligopeptides - chemical synthesis ; Oligopeptides - chemistry ; Oligopeptides - metabolism ; Oligopeptides - pharmacology ; Pharmacology. Drug treatments ; Protein Conformation ; Rats ; Rats, Sprague-Dawley ; Rhinovirus - drug effects ; Rhinovirus - enzymology ; Structure-Activity Relationship ; Viral Proteins
É parte de: Journal of medicinal chemistry, 1998-07, Vol.41 (15), p.2806-2818
Notas: istex:24648893227143369FDDD2FEAFFAB0BB0842871A
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ObjectType-Article-2
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Descrição: The structure-based design, chemical synthesis, and biological evaluation of peptide-derived human rhinovirus (HRV) 3C protease (3CP) inhibitors are described. These compounds incorporate various Michael acceptor moieties and are shown to irreversibly bind to HRV serotype 14 3CP with inhibition activities (k obs/[I]) ranging from 100 to 600 000 M-1 s-1. These inhibitors are also shown to exhibit antiviral activity when tested against HRV-14-infected H1-HeLa cells with EC50's approaching 0.50 μM. Extensive structure−activity relationships developed by Michael acceptor alteration are reported along with the evaluation of several compounds against HRV serotypes other than 14. A 2.0 Å crystal structure of a peptide-derived inhibitor complexed with HRV-2 3CP is also detailed.
Editor: Washington, DC: American Chemical Society
Idioma: Inglês

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Structure-Based Design, Synthesis, and Biological Evaluation of Irreversible Human Rhinovirus 3C Protease Inhibitors. 1. Michael Acceptor Structure−Activity Studies

Washington, DC: American Chemical Society

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