Probing the Binding of Valacyclovir Hydrochloride to the Human Serum Albumin

UV-visible and Fluorescence spectroscopic methods were employed to study the interaction of human serum albumin (HSA) with Valacyclovir Hydrochloride. Additionally, molecular dynamics and molecular docking simulations were used to visualize and specify the binding site of Valacyclovir Hydrochloride. The Stern-Volmer and van't Hoff equations along with spectroscopic observations, were used to determine the binding and thermodynamic parameters. Overall obtained results revealed the presence of dynamic type of quenching mechanism in binding of Valacyclovir Hydrochloride to HSA, while the interaction was found to be entropy driven at domain III of HSA. Analyzing the protein ligand interactions with LIGPLOT, confirmed the dominance of hydrophobic interactions, while the hydrogen bonding interactions play the minor role.