Phenolic N-acyl hydrazone derivatives: In silico assessment of potential antibacterial activity against selected G+ and G- strains

Abstract

In this work, a series of phenolic N-acyl hydrazones was investigated in silico against six selected E. coli and S. aureus bacterial proteins. Generally, the obtained molecular docking results revealed significantly higher binding affinities of analogs a–n towards selected enzymes in comparison to standard compounds. In the case of E. coli proteins 1hnj, 1c14, and 6ntw, the lowest binding energies were calculated for derivatives l (-8.5 kcal/mol), d (-9.0 kcal/mol), and k (-8.2 kcal/mol), respectively. On the other hand, the highest binding affinity towards the S. aureus 3u2d, 1mwu, and 1jij enzymes was expressed by derivatives a, d, and j, with binding energies of -8.3, -8.4, and -9.4 kcal/mol, respectively. The obtained in silico results indicate the potential inhibitory activity of selected phenolic N-acyl hydrazone derivatives against E. coli and S. aureus bacterial proteins and represent a valuable ground base for future in vitro experiments.