Spectroscopic, voltammetry and molecular docking study of binding interaction of antipsychotic drug with bovine serum albumin

Abstract

The interaction between perazine dimaleate (PDM) and bovine serum albumin (BSA) was investigated by voltammetry, fluorescence spectroscopy, UV–vis spectroscopy, molecular docking and viscometric methods. The study was carried out in acetate buffer solution of pH 7.2, which was prepared by using 0.1 M sodium acetate and adjusting pH using 0.1 M hydrochloric acid. The voltammetric study of PDM shows a pair of well redox peaks at 0.538 and 0.471 V (versus SCE) on a GCE in acetate buffer of pH 7.2 at 50 mV s-1. After the addition of BSA into the PDM solution, the redox peak currents decreased gradually, and peak potentials shifted towards negative direction. The results of voltammetry, fluorescence quenching and UV–vis absorption spectra experiments indicated the formation BSA–PDM complex. The binding parameters like binding con­stant and binding free energy were determined from voltammetric data. The binding constant and binding energy was also determined from UV–vis and fluorescence spectroscopy with a value quite close to that obtained from CV.

Keywords

• Bovine serum albumin
• Perazine dimaleate
• Cyclic Voltammetry
• Spectroscopy
• Molecular docking
• Binding Constant