Virtual screening identification of novel severe acute respiratory syndrome 3C-like protease inhibitors and in vitro confirmation.
Identifieur interne : 001526 ( PubMed/Corpus ); précédent : 001525; suivant : 001527Virtual screening identification of novel severe acute respiratory syndrome 3C-like protease inhibitors and in vitro confirmation.
Auteurs : Thi Thanh Hanh Nguyen ; Hwa-Ja Ryu ; Se-Hoon Lee ; Soonwook Hwang ; Vincent Breton ; Joon Haeng Rhee ; Doman KimSource :
- Bioorganic & medicinal chemistry letters [ 1464-3405 ] ; 2011.
English descriptors
- KwdEn :
- Binding, Competitive, Computer Simulation, Cysteine Endopeptidases (genetics), Drug Delivery Systems, Enzyme Activation (drug effects), Escherichia coli (genetics), Escherichia coli (metabolism), Inhibitory Concentration 50, Models, Molecular, Molecular Structure, Protease Inhibitors (chemistry), Protease Inhibitors (pharmacology), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), SARS Virus (drug effects), SARS Virus (enzymology), Small Molecule Libraries, Viral Proteins (antagonists & inhibitors), Viral Proteins (genetics).
- MESH :
- chemical , antagonists & inhibitors : Viral Proteins.
- chemical , chemistry : Protease Inhibitors, Recombinant Proteins.
- chemical , genetics : Cysteine Endopeptidases, Recombinant Proteins, Viral Proteins.
- drug effects : Enzyme Activation, SARS Virus.
- enzymology : SARS Virus.
- genetics : Escherichia coli.
- metabolism : Escherichia coli.
- chemical , pharmacology : Protease Inhibitors.
- Binding, Competitive, Computer Simulation, Drug Delivery Systems, Inhibitory Concentration 50, Models, Molecular, Molecular Structure, Small Molecule Libraries.
Abstract
The 3C-like protease (3CL(pro)) of severe acute respiratory syndrome associated coronavirus (SARS-CoV) is vital for SARS-CoV replication and is a promising drug target. Structure based virtual screening of 308307 chemical compounds was performed using the computation tool Autodock 3.0.5 on a WISDOM Production Environment. The top 1468 ranked compounds with free binding energy ranging from -14.0 to -17.09 kcal mol(-1) were selected to check the hydrogen bond interaction with amino acid residues in the active site of 3CL(pro). Fifty-three compounds from 35 main groups were tested in an in vitro assay for inhibition of 3CL(pro) expressed by Escherichia coli. Seven of the 53 compounds were selected; their IC(50) ranged from 38.57±2.41 to 101.38±3.27 μM. Two strong 3CL(pro) inhibitors were further identified as competitive inhibitors of 3CL(pro) with K(i) values of 9.11±1.6 and 9.93±0.44 μM. Hydrophobic and hydrogen bond interactions of compound with amino acid residues in the active site of 3CL(pro) were also identified.
DOI: 10.1016/j.bmcl.2011.03.034
PubMed: 21470860
Links to Exploration step
pubmed:21470860Le document en format XML
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<author><name sortKey="Ryu, Hwa Ja" sort="Ryu, Hwa Ja" uniqKey="Ryu H" first="Hwa-Ja" last="Ryu">Hwa-Ja Ryu</name>
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<author><name sortKey="Lee, Se Hoon" sort="Lee, Se Hoon" uniqKey="Lee S" first="Se-Hoon" last="Lee">Se-Hoon Lee</name>
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<author><name sortKey="Hwang, Soonwook" sort="Hwang, Soonwook" uniqKey="Hwang S" first="Soonwook" last="Hwang">Soonwook Hwang</name>
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<author><name sortKey="Breton, Vincent" sort="Breton, Vincent" uniqKey="Breton V" first="Vincent" last="Breton">Vincent Breton</name>
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<author><name sortKey="Rhee, Joon Haeng" sort="Rhee, Joon Haeng" uniqKey="Rhee J" first="Joon Haeng" last="Rhee">Joon Haeng Rhee</name>
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<series><title level="j">Bioorganic & medicinal chemistry letters</title>
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<term>Enzyme Activation (drug effects)</term>
<term>Escherichia coli (genetics)</term>
<term>Escherichia coli (metabolism)</term>
<term>Inhibitory Concentration 50</term>
<term>Models, Molecular</term>
<term>Molecular Structure</term>
<term>Protease Inhibitors (chemistry)</term>
<term>Protease Inhibitors (pharmacology)</term>
<term>Recombinant Proteins (chemistry)</term>
<term>Recombinant Proteins (genetics)</term>
<term>SARS Virus (drug effects)</term>
<term>SARS Virus (enzymology)</term>
<term>Small Molecule Libraries</term>
<term>Viral Proteins (antagonists & inhibitors)</term>
<term>Viral Proteins (genetics)</term>
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<term>Recombinant Proteins</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term>
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<front><div type="abstract" xml:lang="en">The 3C-like protease (3CL(pro)) of severe acute respiratory syndrome associated coronavirus (SARS-CoV) is vital for SARS-CoV replication and is a promising drug target. Structure based virtual screening of 308307 chemical compounds was performed using the computation tool Autodock 3.0.5 on a WISDOM Production Environment. The top 1468 ranked compounds with free binding energy ranging from -14.0 to -17.09 kcal mol(-1) were selected to check the hydrogen bond interaction with amino acid residues in the active site of 3CL(pro). Fifty-three compounds from 35 main groups were tested in an in vitro assay for inhibition of 3CL(pro) expressed by Escherichia coli. Seven of the 53 compounds were selected; their IC(50) ranged from 38.57±2.41 to 101.38±3.27 μM. Two strong 3CL(pro) inhibitors were further identified as competitive inhibitors of 3CL(pro) with K(i) values of 9.11±1.6 and 9.93±0.44 μM. Hydrophobic and hydrogen bond interactions of compound with amino acid residues in the active site of 3CL(pro) were also identified.</div>
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<Abstract><AbstractText>The 3C-like protease (3CL(pro)) of severe acute respiratory syndrome associated coronavirus (SARS-CoV) is vital for SARS-CoV replication and is a promising drug target. Structure based virtual screening of 308307 chemical compounds was performed using the computation tool Autodock 3.0.5 on a WISDOM Production Environment. The top 1468 ranked compounds with free binding energy ranging from -14.0 to -17.09 kcal mol(-1) were selected to check the hydrogen bond interaction with amino acid residues in the active site of 3CL(pro). Fifty-three compounds from 35 main groups were tested in an in vitro assay for inhibition of 3CL(pro) expressed by Escherichia coli. Seven of the 53 compounds were selected; their IC(50) ranged from 38.57±2.41 to 101.38±3.27 μM. Two strong 3CL(pro) inhibitors were further identified as competitive inhibitors of 3CL(pro) with K(i) values of 9.11±1.6 and 9.93±0.44 μM. Hydrophobic and hydrogen bond interactions of compound with amino acid residues in the active site of 3CL(pro) were also identified.</AbstractText>
<CopyrightInformation>Copyright © 2011 Elsevier Ltd. All rights reserved.</CopyrightInformation>
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