Mechanistic insights into Zika virus NS3 helicase inhibition by Epigallocatechin-3-gallate: Supplementary Files

Deepak Kumar; Nitin Sharma; Murali Aarthy; Sanjeev Singh; Rajanish Giri

Binding energy calculations for ligand binding at protein active sites were estimated by a molecular mechanics-based approach (MM-GBSA) which employs the forcefield methods to analyze the difference in free energies of ligand, protein and the complex. The glide XP docking poses of EGCG and helicase protein at both binding sites (NTPase and RNA binding site) were used for estimating binding energies by using the Prime suite. In table1, binding energies for EGCG at RNA binding site (-51.312 kcal/mol) was shown which seems slightly higher than at ATPase site (-47.324 kcal/mol). These results show that EGCG molecule can bind at both active sites of NS3 helicase. Further, ADME properties for EGCG molecules were calculated as reported previously by Sharma et al., (2017) (17) . Except, low oral absorption value, rest of the ADME properties of EGCG were within range to declare this molecule as a safe drug candidate. In support of this, a study on cell lines has reported that EGCG is only cytotoxic at concentrations greater than 200uM (16) .