Protein Interaction and Molecular Docking Analysis by Schiff Base Derived from 2,4-Dinitro Phenyl Hydrazine

Abstract

A novel and cost-effective 2,4-dinitrophenyl hydrazine derived from Schiff base 1-benzylidine-2-(2,4-dinitrophenyl) hydrazine ( L) was designed and characterized using various spectroscopic techniques. The interaction between L and bovine serum albumin (BSA) has been carried out using UV–Vis and fluorescence spectroscopy, DSC, SEM, and molecular docking methods. The phosphate buffer ([Formula: see text]) solution of BSA showed fluorescence emission maxima at 342[Formula: see text]nm. Upon addition of L to the BSA solution, it quenched the fluorescence emission at 342[Formula: see text]nm. The quenching of the fluorescence emission is due to the formation of a complex between L and BSA. The binding constant was calculated from the fluorescence titrations and found to be [Formula: see text][Formula: see text]M[Formula: see text]. Further, molecular docking analysis was carried out to establish the binding between L and BSA.