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Tannins inhibit SARS-CoV-2 through binding with catalytic dyad residues of 3CL^pro : An in silico approach with 19 structural different hydrolysable tannins.

ABSTRACT: Coronavirus epidemic 2019 (COVID-19), instigated by SARS-CoV-2 virus, is recently raising worldwide and inspiring global health worries. The main 3-chymotrypsin-like cysteine protease (3CL^Pro ) enzyme of SARS-CoV-2, which operates its replication, could be used as a medication discovery point. We therefore theoretically studied and docked the effects of 19 hydrolysable tannins on SARS-CoV-2 by assembling with the catalytic dyad residues of its 3CL^pro using molecular operating environment (MOE 09). Results discovered that pedunculagin, tercatain, and castalin intensely interacted with the receptor binding site and catalytic dyad (Cys145 and His41) of SARS-CoV-2. Our analyses estimated that the top three hits might serve as potential inhibitor of SARS-CoV-2 leading mole

SUBMITTER: Khalifa I

PROVIDER: S-EPMC7435556 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature

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Dataset Information

Tannins inhibit SARS-CoV-2 through binding with catalytic dyad residues of 3CL^pro : An in silico approach with 19 structural different hydrolysable tannins.

OmicsDI is part of the ELIXIR infrastructure

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Dataset Information

Tannins inhibit SARS-CoV-2 through binding with catalytic dyad residues of 3CLpro : An in silico approach with 19 structural different hydrolysable tannins.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Tannins inhibit SARS-CoV-2 through binding with catalytic dyad residues of 3CL^pro : An in silico approach with 19 structural different hydrolysable tannins.