Design, synthesis and antiviral efficacy of a series of potent chloropyridyl ester-derived SARS-CoV 3CLpro inhibitors.
Identifieur interne : 001B59 ( PubMed/Checkpoint ); précédent : 001B58; suivant : 001B60Design, synthesis and antiviral efficacy of a series of potent chloropyridyl ester-derived SARS-CoV 3CLpro inhibitors.
Auteurs : Arun K. Ghosh [États-Unis] ; Gangli Gong ; Valerie Grum-Tokars ; Debbie C. Mulhearn ; Susan C. Baker ; Melissa Coughlin ; Bellur S. Prabhakar ; Katrina Sleeman ; Michael E. Johnson ; Andrew D. MesecarSource :
- Bioorganic & medicinal chemistry letters [ 1464-3405 ] ; 2008.
Descripteurs français
- KwdFr :
- Animaux, Antiviraux (), Antiviraux (pharmacologie), Antiviraux (synthèse chimique), Chimie pharmaceutique (), Concentration inhibitrice 50, Conception de médicament, Conformation moléculaire, Cysteine endopeptidases (), Domaine catalytique, Esters, Humains, Liaison aux protéines, Modèles chimiques, Modèles moléculaires, Protéines virales (antagonistes et inhibiteurs), Virus du SRAS (métabolisme).
- MESH :
- antagonistes et inhibiteurs : Protéines virales.
- métabolisme : Virus du SRAS.
- pharmacologie : Antiviraux.
- synthèse chimique : Antiviraux.
- Animaux, Antiviraux, Chimie pharmaceutique, Concentration inhibitrice 50, Conception de médicament, Conformation moléculaire, Cysteine endopeptidases, Domaine catalytique, Esters, Humains, Liaison aux protéines, Modèles chimiques, Modèles moléculaires.
English descriptors
- KwdEn :
- Animals, Antiviral Agents (chemical synthesis), Antiviral Agents (chemistry), Antiviral Agents (pharmacology), Catalytic Domain, Chemistry, Pharmaceutical (methods), Cysteine Endopeptidases (chemistry), Drug Design, Esters, Humans, Inhibitory Concentration 50, Models, Chemical, Models, Molecular, Molecular Conformation, Protein Binding, SARS Virus (metabolism), Viral Proteins (antagonists & inhibitors).
- MESH :
- chemical , antagonists & inhibitors : Viral Proteins.
- chemical , chemical synthesis : Antiviral Agents.
- chemical , chemistry : Antiviral Agents, Cysteine Endopeptidases.
- chemical , pharmacology : Antiviral Agents.
- metabolism : SARS Virus.
- methods : Chemistry, Pharmaceutical.
- Animals, Catalytic Domain, Drug Design, Esters, Humans, Inhibitory Concentration 50, Models, Chemical, Models, Molecular, Molecular Conformation, Protein Binding.
Abstract
Design, synthesis and biological evaluation of a series of 5-chloropyridine ester-derived severe acute respiratory syndrome-coronavirus chymotrypsin-like protease inhibitors is described. Position of the carboxylate functionality is critical to potency. Inhibitor 10 with a 5-chloropyridinyl ester at position 4 of the indole ring is the most potent inhibitor with a SARS-CoV 3CLpro IC(50) value of 30 nM and an antiviral EC(50) value of 6.9 microM. Molecular docking studies have provided possible binding modes of these inhibitors.
DOI: 10.1016/j.bmcl.2008.08.082
PubMed: 18796354
Affiliations:
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pubmed:18796354Le document en format XML
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<front><div type="abstract" xml:lang="en">Design, synthesis and biological evaluation of a series of 5-chloropyridine ester-derived severe acute respiratory syndrome-coronavirus chymotrypsin-like protease inhibitors is described. Position of the carboxylate functionality is critical to potency. Inhibitor 10 with a 5-chloropyridinyl ester at position 4 of the indole ring is the most potent inhibitor with a SARS-CoV 3CLpro IC(50) value of 30 nM and an antiviral EC(50) value of 6.9 microM. Molecular docking studies have provided possible binding modes of these inhibitors.</div>
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<name sortKey="Gong, Gangli" sort="Gong, Gangli" uniqKey="Gong G" first="Gangli" last="Gong">Gangli Gong</name>
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