An outbreak of coronavirus 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 catalyzes 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 antiviral activity in severe acute respiratory syndrome coronavirus (SARS-CoV) and the similar chemical structures through a molecular docking study to target RdRp of SARS-CoV-2, SARS-CoV, and Middle East respiratory syndrome coronavirus (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 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 a potential SARS-CoV-2 RdRp inhibitor for further study.

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rna polymerase idock score middle east respiratory syndrome coronavirus molecular docking binding energy sarscov2 911 kcalmol sarscov 803 replication catalytic pocket hydrophobic rdrp disease merscov 826

Yu‐Lun Chou, Yu‐Shih Lin,Jrhau Lung, Yao‐Hsu Yang, Ching‐Yuan Wu, Yu‐Ching Cheng, Li‐Hsin Shu, Hung Te Liu,.The potential chemical structure of anti‐SARS‐CoV‐2 RNA‐dependent RNA polymerase. (),.

Yu‐Lun Chou, et al."The potential chemical structure of anti‐SARS‐CoV‐2 RNA‐dependent RNA polymerase"

Yu‐Lun Chou, Yu‐Shih Lin,Jrhau Lung, Yao‐Hsu Yang, Ching‐Yuan Wu, Yu‐Ching Cheng, Li‐Hsin Shu, Hung Te Liu,"The potential chemical structure of anti‐SARS‐CoV‐2 RNA‐dependent RNA polymerase"