In-Silico Evaluation of 10 Structurally Different Glucosinolates on the Key Enzyme of SARS-CoV-2

ABSTRACT

The novel coronavirus (2019-nCoV) triggered a worldwide rise in the prevalence of the coronavirus outbreak (COVID-19) and surfaced as a universal wellbeing matter. Analogous with SARS-CoV and MERS-CoV, the main 3-chymotrypsin-alike cysteine protease (3CL(Pro)) virus enzyme that manages the replications of 2019-nCoV and regulates its existence span, possibly will be considered like a medication break through focus. In this study, the binding potential of 10 glucosinolates (Glu) having a variety of structures was studied with the catalytic dyad remains of 2019-nCoV-3CL(Pro ) by molecular cutting developing. The outcomes have shown that Glu containing sinigrin (SN) have been shown to be realistically bound to the 2019-nCoV-3CL(Pro) receptor and catalytic dyad binding sites (Cys145 and His41). Our simulation results have shown that sinigrin have a potential activity against 2019-nCoV and could be further used for drug production and optimization in the battle against COVID-19. In details, SN-SARS-CoV-2-3CL(Pro)-facilityacted without exhibit whichever observable variations, with reference to the constancy of Glu-enzyme complexes by means of average RMSD of 1.5 +/- 0.02 angstrom. Meanwhile, the ordinary behavior of a SN-SARS-CoV-2-3CL(Pro) complex continued as compact and steady during (50 ns) MD simulations. Current investigation has revealed that Glu with a specific structure could be successful against COVID-19 as natural components.