Green tea as SIRT1 and SIRT3 activator in COVID-19: A molecular docking approach

Abstract

This study reports docking analysis and performance of catechin and its derivatives in activating the SIRT1 and SIRT3 protein for the treatment of COVID-19. Val-412, Asp-348, Pro-271, and Ser-442 are interactions involved in hydrogen bonding and Ile-316, Ala 262, Ile-347, Val-445, Phe-297, His 363 are interactions involved in hydrophobic bonding between the various ligands and SIRT1 protein. ILE-111, Val-173, Asp-112, Phe-38 are interactions involved in hydrogen bonding and Phe-38, Ala-27, Ile-111, His-129, Phe-38 are involved in hydrophobic bonding between the various ligands and SIRT3 protein. Catechin gallate and epigallocatechin gallate show promising potential as SIRT1 activators as observed by their binding affinity ΔG=-10.9 kcal/mol and ΔG=-10.6 kcal/mol, which are lower than the binding affinity of the standard therapeutic moiety resveratrol (ΔG=-9.0 kcal/mol). All catechins show promising potential as SIRT3 activators, as revealed by their binding affinities, which are lower than the binding affinity of the standard therapeutic moiety resveratrol (ΔG=-8.4 kcal/mol). Amongst all the catechins, catechin gallate shows 61.53% binding site similarity with the native ligand in the case of SIRT1 protein. Amongst all the catechins, epicatechin and epigallocatechin show 100% binding site similarity with the native ligand for the SIRT3 protein. Therefore, we suggest that catechins can serve as SIRT1 and SIRT3 activators, which may prove to be a possible therapy for COVID-19.