Multi-target inhibition property of Persicaria hydropiper phytochemicals against gram-positive and gram-negative bacteria by in silico approaches

Abstract

Bacterial multidrug resistance is nowadays a global concern, and it necessitates the development of effective alternative therapeutics. Targeting bacterial virulence proteins is an effective way to discover new lead molecules. The current study reports the binding affinity of Persicaria hydropiper phytochemicals (catechin, quercetin 3-sulfate, scutellarein, pinosylvin, ombuin, hyperin) against topoisomerase IV from Escherichia coli, Staphylococcus aureus gyrase-ATPase binding domain, Cvir from Chromobacterium violaceum, Glycosyl hydrolase from Pseudomonas aeruginosa, by molecular docking, which revealed -9.3 to -5.9 kcal/mol binding energy. The P. hydropiper phytochemicals displayed acceptable ADMET profiles, and obeyed Lipinski’s rule of five, except hyperin. The molecular dynamic simulation substantiated the stability of the protein-ligand (5BX9-catechin and 3QP1-catechin) complexes. Overall, the current study findings suggest the development of plant-based therapeutics, using P. hydropiper bioactive small molecules, effective against bacterial virulence, thereby combating the pathogenesis of infection caused by gram-positive and gram-negative bacteria.