Characterization and inhibition of SARS-coronavirus main protease.
Identifieur interne : 003F59 ( Main/Exploration ); précédent : 003F58; suivant : 003F60Characterization and inhibition of SARS-coronavirus main protease.
Auteurs : Po-Huang Liang [Taïwan]Source :
- Current topics in medicinal chemistry [ 1568-0266 ] ; 2006.
Descripteurs français
- KwdFr :
- Chromatographie en phase liquide à haute performance, Conformation des protéines, Cysteine endopeptidases (), Dimérisation, Données de séquences moléculaires, Inhibiteurs de protéases (pharmacologie), Modèles moléculaires, Similitude de séquences d'acides aminés, Spectrométrie de fluorescence, Séquence d'acides aminés.
- MESH :
- pharmacologie : Inhibiteurs de protéases.
- Chromatographie en phase liquide à haute performance, Conformation des protéines, Cysteine endopeptidases, Dimérisation, Données de séquences moléculaires, Modèles moléculaires, Similitude de séquences d'acides aminés, Spectrométrie de fluorescence, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Chromatography, High Pressure Liquid, Cysteine Endopeptidases (chemistry), Cysteine Endopeptidases (drug effects), Dimerization, Models, Molecular, Molecular Sequence Data, Protease Inhibitors (pharmacology), Protein Conformation, Sequence Homology, Amino Acid, Spectrometry, Fluorescence.
- MESH :
- chemical , chemistry : Cysteine Endopeptidases.
- chemical , drug effects : Cysteine Endopeptidases.
- chemical , pharmacology : Protease Inhibitors.
- Amino Acid Sequence, Chromatography, High Pressure Liquid, Dimerization, Models, Molecular, Molecular Sequence Data, Protein Conformation, Sequence Homology, Amino Acid, Spectrometry, Fluorescence.
Abstract
Severe acute respiratory syndrome (SARS) is an emerging infectious disease caused by a novel human coronavirus (CoV). During the 2003 epidemic, the disease rapidly spread from its origin in southern China to other countries and affected almost 8000 patients, which resulted in about 800 fatalities. A chymotrypsin-like cysteine protease named 3C-like protease (3CLpro) is essential for the life cycle of the SARS-CoV. This main protease is responsible for maturation of functional proteins and represents a key anti-viral target. HPLC and fluorescence-based assays have been used to characterize the protease and to determine the potency of the inhibitors. The fluorogenic method monitoring the increase of fluorescence from the cleavage of a peptide substrate containing an Edans-Dabcyl fluorescence quenching pair at two ends has enabled the use of high throughput screening to speed up the drug discovery process. Several groups of inhibitors have been identified through high throughput screening and rational drug design approaches. Thus, alpha,beta-unsaturated peptidomimetics, anilides, metal-conjugated compounds, boronic acids, quinolinecarboxylate derivatives, thiophenecarboxylates, phthalhydrazide-substituted ketoglutamine analogues, isatin and natural products have been identified as potent inhibitors of the SARS-CoV main protease. The different classes of inhibitors reported in these studies are summarized in this review. Some of these inhibitors could be developed into potential drug candidates, which may provide a solution to combat possible reoccurrence of the SARS and other life-threatening viruses with 3CL proteases.
DOI: 10.2174/156802606776287090
PubMed: 16611148
Affiliations:
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Le document en format XML
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<term>Cysteine Endopeptidases (drug effects)</term>
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<term>Molecular Sequence Data</term>
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<term>Modèles moléculaires</term>
<term>Similitude de séquences d'acides aminés</term>
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<term>Modèles moléculaires</term>
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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome (SARS) is an emerging infectious disease caused by a novel human coronavirus (CoV). During the 2003 epidemic, the disease rapidly spread from its origin in southern China to other countries and affected almost 8000 patients, which resulted in about 800 fatalities. A chymotrypsin-like cysteine protease named 3C-like protease (3CLpro) is essential for the life cycle of the SARS-CoV. This main protease is responsible for maturation of functional proteins and represents a key anti-viral target. HPLC and fluorescence-based assays have been used to characterize the protease and to determine the potency of the inhibitors. The fluorogenic method monitoring the increase of fluorescence from the cleavage of a peptide substrate containing an Edans-Dabcyl fluorescence quenching pair at two ends has enabled the use of high throughput screening to speed up the drug discovery process. Several groups of inhibitors have been identified through high throughput screening and rational drug design approaches. Thus, alpha,beta-unsaturated peptidomimetics, anilides, metal-conjugated compounds, boronic acids, quinolinecarboxylate derivatives, thiophenecarboxylates, phthalhydrazide-substituted ketoglutamine analogues, isatin and natural products have been identified as potent inhibitors of the SARS-CoV main protease. The different classes of inhibitors reported in these studies are summarized in this review. Some of these inhibitors could be developed into potential drug candidates, which may provide a solution to combat possible reoccurrence of the SARS and other life-threatening viruses with 3CL proteases.</div>
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