In silico antibiofilm potency of phenolic N-acyl hydrazones against selected bacterial strains

Abstract

In the present work, fourteen phenolic hydrazone derivatives were evaluated for their in silico inhibitory activity against selected P. aeruginosa and S. maltophilia proteins involved in drug resistance and biofilm formation. Molecular docking analysis revealed the highest binding affinity of analogs n (-8.4 kcal/mol) and h (-7.3 kcal/mol) towards P. aeruginosa 7m1m and 7m1l proteins, respectively. In the case of S. maltophilia, analog k (-8.4 kcal/mol) expressed the highest binding affinity to 6qw7, whereas for 6uaf, the lowest binding energy was calculated for derivative d (-8.1 kcal/mol). The obtained in silico results highlight the potential inhibition potency of the selected hydrazone analogs against investigated proteins and represent a good basis for future in vitro antibiofilm investigations.