Tannins inhibit SARS‐CoV‐2 through binding with catalytic dyad residues of 3CLpro: An in silico approach with 19 structural different hydrolysable tannins. Issue 10 (11th August 2020)

• Record Type: Journal Article
• Authors: Khalifa, Ibrahim; Zhu, Wei; Mohammed, Hammad Hamed Hammad; Dutta, Kunal; Li, Chunmei
• Is Part Of: Journal of food biochemistry. Volume 44:Issue 10(2020)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2020-08-11
• Subjects: COVID‐19 -- hydrolysable tannins -- main 3‐chymotrypsin‐like cysteine protease -- molecular docking -- structural‐relationship activity; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; Biochemistry -- Periodicals; 664.024
• DOI: 10.1111/jfbc.13432
• Languages: English
• ISSNs: 0145-8884

Abstract

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 molecules for additional optimization and drug development process to combat COVID‐19. This study unleashed that tannins with specific structure could be utilized as natural inhibitors against COVID‐19. Practical applications: The 3CL Pro controls SARS‐CoV‐2 copying and manages its life series, which was targeted in case of SARS‐CoV and MERS‐CoV coronavirus. About 19 hydrolysable tannins were computed against 3CL pro of SARS‐CoV‐2. Pedunculagin, tercatain, and castalin interacted with Cys145 and His41 of SARS‐CoV‐2‐3CL pro . Pedunculagin‐SARS‐CoV‐2‐3CL pro remain stable, with no obvious fluctuations. We predicted that the understandings gained in the current research may evidence valued for discovering and unindustrialized innovative natural inhibitors for COVID‐19 in the nearby future. Abstract : About 19 hydrolyzable tannins were computed against 3CLpro enzyme of 2019‐nCoV. It was found that pedunculagin, tercatain, and castalin interacted with Cys145 and His41 of 2019‐nCoV‐3CLpro. Likewise, pedunculagin‐2019‐nCoV‐3CLpro remain stable, with no obvious fluctuations. We predicted that the understandings obtained in the current study may evidence valued for discovering and unindustrialized novel natural anti‐COVID‐19 therapeutic agents in the near future.