Discovery of potent anilide inhibitors against the severe acute respiratory syndrome 3CL protease.
Identifieur interne : 002675 ( PubMed/Curation ); précédent : 002674; suivant : 002676Discovery of potent anilide inhibitors against the severe acute respiratory syndrome 3CL protease.
Auteurs : Jiun-Jie Shie [Taïwan] ; Jim-Min Fang ; Chih-Jung Kuo ; Tun-Hsun Kuo ; Po-Huang Liang ; Hung-Jyun Huang ; Wen-Bin Yang ; Chun-Hung Lin ; Jiun-Ling Chen ; Yin-Ta Wu ; Chi-Huey WongSource :
- Journal of medicinal chemistry [ 0022-2623 ] ; 2005.
Descripteurs français
- KwdFr :
- Anilides (), Anilides (pharmacologie), Anilides (synthèse chimique), Antiviraux (), Antiviraux (pharmacologie), Antiviraux (synthèse chimique), Cinétique, Conformation des protéines, Cysteine endopeptidases, Endopeptidases (), Endopeptidases (métabolisme), Inhibiteurs de protéases (), Inhibiteurs de protéases (pharmacologie), Inhibiteurs de protéases (synthèse chimique), Modèles moléculaires, Protéines virales (), Protéines virales (métabolisme), Relation structure-activité, Syndrome respiratoire aigu sévère (traitement médicamenteux), Virus du SRAS (), Virus du SRAS (enzymologie).
- MESH :
- enzymologie : Virus du SRAS.
- métabolisme : Endopeptidases, Protéines virales.
- pharmacologie : Anilides, Antiviraux, Inhibiteurs de protéases.
- synthèse chimique : Anilides, Antiviraux, Inhibiteurs de protéases.
- traitement médicamenteux : Syndrome respiratoire aigu sévère.
- Anilides, Antiviraux, Cinétique, Conformation des protéines, Cysteine endopeptidases, Endopeptidases, Inhibiteurs de protéases, Modèles moléculaires, Protéines virales, Relation structure-activité, Virus du SRAS.
English descriptors
- KwdEn :
- Anilides (chemical synthesis), Anilides (chemistry), Anilides (pharmacology), Antiviral Agents (chemical synthesis), Antiviral Agents (chemistry), Antiviral Agents (pharmacology), Cysteine Endopeptidases, Endopeptidases (chemistry), Endopeptidases (drug effects), Endopeptidases (metabolism), Kinetics, Models, Molecular, Protease Inhibitors (chemical synthesis), Protease Inhibitors (chemistry), Protease Inhibitors (pharmacology), Protein Conformation, SARS Virus (drug effects), SARS Virus (enzymology), Severe Acute Respiratory Syndrome (drug therapy), Structure-Activity Relationship, Viral Proteins (chemistry), Viral Proteins (drug effects), Viral Proteins (metabolism).
- MESH :
- chemical , chemical synthesis : Anilides, Antiviral Agents, Protease Inhibitors.
- chemical , chemistry : Anilides, Antiviral Agents, Endopeptidases, Protease Inhibitors, Viral Proteins.
- chemical , drug effects : Endopeptidases, Viral Proteins.
- chemical , metabolism : Endopeptidases, Viral Proteins.
- chemical , pharmacology : Anilides, Antiviral Agents, Protease Inhibitors.
- chemical : Cysteine Endopeptidases.
- drug effects : SARS Virus.
- drug therapy : Severe Acute Respiratory Syndrome.
- enzymology : SARS Virus.
- Kinetics, Models, Molecular, Protein Conformation, Structure-Activity Relationship.
Abstract
A diversified library of peptide anilides was prepared, and their inhibition activities against the SARS-CoV 3CL protease were examined by a fluorogenic tetradecapeptide substrate. The most potent inhibitor is an anilide derived from 2-chloro-4-nitroaniline, l-phenylalanine and 4-(dimethylamino)benzoic acid. This anilide is a competitive inhibitor of the SARS-CoV 3CL protease with K(i) = 0.03 muM. The molecular docking experiment indicates that the P1 residue of this anilide inhibitor is distant from the nucleophilic SH of Cys145 in the active site.
DOI: 10.1021/jm050184y
PubMed: 15974598
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pubmed:15974598Le document en format XML
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<term>Severe Acute Respiratory Syndrome (drug therapy)</term>
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<term>Viral Proteins (drug effects)</term>
<term>Viral Proteins (metabolism)</term>
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<term>Antiviraux (synthèse chimique)</term>
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<term>Conformation des protéines</term>
<term>Cysteine endopeptidases</term>
<term>Endopeptidases ()</term>
<term>Endopeptidases (métabolisme)</term>
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<term>Inhibiteurs de protéases (pharmacologie)</term>
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<term>Modèles moléculaires</term>
<term>Protéines virales ()</term>
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<term>Syndrome respiratoire aigu sévère (traitement médicamenteux)</term>
<term>Virus du SRAS ()</term>
<term>Virus du SRAS (enzymologie)</term>
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<term>Antiviral Agents</term>
<term>Protease Inhibitors</term>
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<keywords scheme="MESH" qualifier="drug therapy" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term>
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</keywords>
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<term>Models, Molecular</term>
<term>Protein Conformation</term>
<term>Structure-Activity Relationship</term>
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<term>Antiviraux</term>
<term>Cinétique</term>
<term>Conformation des protéines</term>
<term>Cysteine endopeptidases</term>
<term>Endopeptidases</term>
<term>Inhibiteurs de protéases</term>
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<front><div type="abstract" xml:lang="en">A diversified library of peptide anilides was prepared, and their inhibition activities against the SARS-CoV 3CL protease were examined by a fluorogenic tetradecapeptide substrate. The most potent inhibitor is an anilide derived from 2-chloro-4-nitroaniline, l-phenylalanine and 4-(dimethylamino)benzoic acid. This anilide is a competitive inhibitor of the SARS-CoV 3CL protease with K(i) = 0.03 muM. The molecular docking experiment indicates that the P1 residue of this anilide inhibitor is distant from the nucleophilic SH of Cys145 in the active site.</div>
</front>
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<Abstract><AbstractText>A diversified library of peptide anilides was prepared, and their inhibition activities against the SARS-CoV 3CL protease were examined by a fluorogenic tetradecapeptide substrate. The most potent inhibitor is an anilide derived from 2-chloro-4-nitroaniline, l-phenylalanine and 4-(dimethylamino)benzoic acid. This anilide is a competitive inhibitor of the SARS-CoV 3CL protease with K(i) = 0.03 muM. The molecular docking experiment indicates that the P1 residue of this anilide inhibitor is distant from the nucleophilic SH of Cys145 in the active site.</AbstractText>
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<ForeName>Jiun-Jie</ForeName>
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