The potential chemical structure of anti-SARS-CoV-2 RNA-dependent RNA polymerase.
Identifieur interne : 000D76 ( Ncbi/Merge ); précédent : 000D75; suivant : 000D77The potential chemical structure of anti-SARS-CoV-2 RNA-dependent RNA polymerase.
Auteurs : Jrhau Lung [Taïwan] ; Yu-Shih Lin [Taïwan] ; Yao-Hsu Yang [Taïwan] ; Yu-Lun Chou ; Li-Hsin Shu [Taïwan] ; Yu-Ching Cheng [Taïwan] ; Hung Te Liu [Taïwan] ; Ching-Yuan Wu [Taïwan]Source :
- Journal of medical virology [ 1096-9071 ] ; 2020.
Abstract
An outbreak of corona virus disease 2019 (COVID-19) occurred in Wuhan and it has rapidly spread to almost all parts of the world. For coronaviruses, RNA-dependent RNA polymerase (RdRp) is an important protease that catalyze the replication of RNA from RNA template and is an attractive therapeutic target. In this study, we screened these chemical structures from traditional Chinese medicinal compounds proven to show anti-viral activity in SARS-CoV and the similar chemical structures through a molecular docking study to target RdRp of SARS-CoV-2, SARS-CoV and MERS-CoV. We found that theaflavin has a lower idock score in the catalytic pocket of RdRp in SARS-CoV-2 (-9.11 kcal/mol), SARS-CoV (-8.03 kcal/mol) and MERS-CoV (-8.26 kcal/mol) from idock. To confirm the result, we discovered that theaflavin has a lower binding energy of -8.8 kcal/mol when it docks in the catalytic pocket of SARS-CoV-2 RdRp by using the Blind Docking server. Regarding contact modes, hydrophobic interactions contribute significantly in binding and additional hydrogen bonds were found between theaflavin and RdRp. Moreover, one π-cation interaction was formed between theaflavin and Arg553 from the Blind Docking server. Our results suggest that theaflavin could be potential SARS-CoV-2 RdRp inhibitor for further study. This article is protected by copyright. All rights reserved.
DOI: 10.1002/jmv.25761
PubMed: 32167173
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<front><div type="abstract" xml:lang="en">An outbreak of corona virus disease 2019 (COVID-19) occurred in Wuhan and it has rapidly spread to almost all parts of the world. For coronaviruses, RNA-dependent RNA polymerase (RdRp) is an important protease that catalyze the replication of RNA from RNA template and is an attractive therapeutic target. In this study, we screened these chemical structures from traditional Chinese medicinal compounds proven to show anti-viral activity in SARS-CoV and the similar chemical structures through a molecular docking study to target RdRp of SARS-CoV-2, SARS-CoV and MERS-CoV. We found that theaflavin has a lower idock score in the catalytic pocket of RdRp in SARS-CoV-2 (-9.11 kcal/mol), SARS-CoV (-8.03 kcal/mol) and MERS-CoV (-8.26 kcal/mol) from idock. To confirm the result, we discovered that theaflavin has a lower binding energy of -8.8 kcal/mol when it docks in the catalytic pocket of SARS-CoV-2 RdRp by using the Blind Docking server. Regarding contact modes, hydrophobic interactions contribute significantly in binding and additional hydrogen bonds were found between theaflavin and RdRp. Moreover, one π-cation interaction was formed between theaflavin and Arg553 from the Blind Docking server. Our results suggest that theaflavin could be potential SARS-CoV-2 RdRp inhibitor for further study. This article is protected by copyright. All rights reserved.</div>
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<Abstract><AbstractText>An outbreak of corona virus disease 2019 (COVID-19) occurred in Wuhan and it has rapidly spread to almost all parts of the world. For coronaviruses, RNA-dependent RNA polymerase (RdRp) is an important protease that catalyze the replication of RNA from RNA template and is an attractive therapeutic target. In this study, we screened these chemical structures from traditional Chinese medicinal compounds proven to show anti-viral activity in SARS-CoV and the similar chemical structures through a molecular docking study to target RdRp of SARS-CoV-2, SARS-CoV and MERS-CoV. We found that theaflavin has a lower idock score in the catalytic pocket of RdRp in SARS-CoV-2 (-9.11 kcal/mol), SARS-CoV (-8.03 kcal/mol) and MERS-CoV (-8.26 kcal/mol) from idock. To confirm the result, we discovered that theaflavin has a lower binding energy of -8.8 kcal/mol when it docks in the catalytic pocket of SARS-CoV-2 RdRp by using the Blind Docking server. Regarding contact modes, hydrophobic interactions contribute significantly in binding and additional hydrogen bonds were found between theaflavin and RdRp. Moreover, one π-cation interaction was formed between theaflavin and Arg553 from the Blind Docking server. Our results suggest that theaflavin could be potential SARS-CoV-2 RdRp inhibitor for further study. This article is protected by copyright. All rights reserved.</AbstractText>
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