Biophysical Insight into the Interaction of Human Lysozyme with Anticancer Drug Anastrozole: A Multitechnique Approach

Abstract

In the present study, we employ fluorescence spectroscopy, dynamic light scattering, and molecular docking methods. Binding of anticancer drug anastrozole with human lysozyme (HL) is studied. Binding of anastrozole to HL is moderate but spontaneous. There is anastrozole persuaded hydrodynamic change in HL, leading to molecular compaction. Binding of anastrozole to HL also decreased in vitro lytic activity of HL. Molecular docking results suggest the electrostatic interactions and van der Waals forces played key role in binding interaction of anastrozole near the catalytic site. Binding interaction of anastrozole to proteins other than major transport proteins in blood can significantly affect pharmacokinetics of this molecule. Hence, rationalizing drug dosage is important. This study also points to unrelated effects that small molecules bring in the body that are considerable and need thorough investigation.

Lysozyme and Human Serum Albumin Proteins as Potential Nitric Oxide Cardiovascular Drug Carriers: Theoretical and Experimental Investigation

“…Comparison of the binding free energy predicted from the current study was performed with the previous theoretical and experimental studies for binding of any ligand with the studied proteins. For instance, an experimental and computational study showed the binding of anticancer drug anastrozole to lysozyme with −5.65 kcal/mol experimentally and predicted −6.64 kcal/mol through modeling techniques . A spectroscopic and molecular docking investigation predicted the binding of safranal to lysozyme with −24.1 kJ/mol .…”