In silico molecular docking study of milk-derived peptide against biofilm forming Staphylococcus aureus and Escherichia coli

Abstract

In this in-silico study lactoferrin was docked to the active site of four receptors of Staphylococcus aureus and two receptors of Escherichia coli. The rise of antimicrobial resistance highlights the significance of bioactive compounds as crucial therapeutic agents. The current study investigated on the binding energy of lactoferrin to these receptors by stabilising their structures. The receptors taken were with PDB IDs 3FRA, 3FYV, 3VUS, 2RKZ, 3GEU and 6F86. All the binding energy was negative which indicated that lactoferrin has activity against these receptors. The results revealed that lactoferrin bound to the fibronectin binding protein of S. aureus with least binding energy as -2.70 Kcal/mol and highest binding energy with oxidoreductase of S. aureus as -8.36Kcal/mol. These evidences showed that by proper synthesis and advances in designing of the lactoferrin structure to improve its stability it could be used as potential therapeutic agent against these organisms.