Electrochemical and Theoretical Investigations on the Binding of Anticancer Drug Olaparib to Human Serum Albumin

Abstract

This article explores the interaction between Olaparib (OLA), an anticancer drug, and human serum albumin (HSA) on a glassy carbon electrode using cyclic voltammetry and differential pulse voltammetry methods. The study investigates the alterations in the electrochemical behavior of [Fe(CN)6]3–/4– redox pairs in a physiological pH buffer solution due to the OLA-HSA interaction. The electrochemical and kinetic parameters of the redox probe were calculated in the presence of both the drug and protein. Notable variations in these parameters were observed, which can be attributed to the formation of an electro-inactive complex between the protein and drug. The study determined the parameters describing the OLA-HSA complex, including the binding constant and complex stoichiometry. The results revealed the formation of a strong singular drug-albumin complex with a binding constant of 1.12 × 105 M–1. Molecular docking studies supported the experimental findings and provided insights into the binding interactions of OLA with HSA. This study provides valuable insights for future research aimed at enhancing drug delivery systems.