The present study evaluated the efficacy of eupalitin compounds against the target protein, dihydrofolate reductase of bacterial and fungal pathogens using in silico approach. Structure based docking studies was performed using Schrodinger (Version: 1.8) tool to retrieve potential candidates with high affinities binding against eupalitin models with several targeted proteins repositories. The specific targets were selected from susceptible organisms which include bacterial (Escherichia coli, Staphylococcus aureus and Bacillus anthracis) and fungal strains (Candida albicans and Candida glabirata). The selected target proteins were 4PSS, 3F0Q, 3S9U, 4HOG and 4HOE, respectively. Molecular docking was carried out using eupalitin compound with different target proteins of microorganisms. Free energy of binding was recorded for the compound with its target. One compound was docked with five different receptors of microorganisms, out of which, 4PSS of Escherichia coli (-6.90 kcal/mol) showed good score for binding with receptor by forming strong hydrogen bonding with respective connected amino acid chains. Therefore, the present study plays a guiding role in developing new inhibitors with better binding affinities with the virulent protein of pathogens, followed by invention of novel drug to treat bacterial infections.

Keywords: Eupalitin, target proteins, antimicrobials, docking.