Binding of bioactive esculin and esculetin with hen egg white lysozyme: Spectroscopic and computational methods to comprehensively elucidate the binding affinities, interacting forces, and conformational alterations at molecular level

The binding of bioactive esculin and esculetin with lysozyme have been studied using multi-spectroscopic and computational methods. Intrinsic fluorescence of lysozyme was quenched via static quenching mechanism by these ligands and binding was observed to be moderate in nature. Structural alteration of the protein was noted upon ligand binding and enzymatic activity of lysozyme was also influenced in vitro.