IN SILICON EVALUATION OF ARTEMISININ DERIVATIVES AS POTENTIAL INHIBITORS OF SARS-COV-2 MAIN PROTEASE
TL;DR
Four artemisinin-derived compounds namely, artesunate, artemether, artemisinin and dihydroartemisinin were evaluated as potential Mpro binders using molecular docking and post docking interaction analysis and among the tested ligands, artesunate showed the most favorable predicted binding affinity with docking score.
Abstract
. The main protease of SARS-CoV-2 (Mpro, 3CLpro) is a crucial viral enzyme required for the cleavage of viral polyproteins during coronavirus replication. Its catalytic activity relies on the conserved His41–Cys145 dyad, making the main protease (Mpro) an important molecular target for the discovery of antiviral drugs. In the present study, four artemisinin-derived compounds namely, artesunate, artemether, artemisinin and dihydroartemisinin were evaluated as potential Mpro binders using molecular docking and post docking interaction analysis . Docking simulations were performed using the crystal structure of SARS-CoV-2 Mpro and AutoDock Vina. The docking grid was centered on the catalytic pocket defined by His41 and Cys145. The generated poses were assessed based on predicted affinity, proximity to catalytic residues, hydrogen bond-like O/N contacts, hydrophobic C–C contacts, and multivariate interaction profiles. Among the tested ligands, artesunate showed the most favorable predicted binding affinity with docking score