Investigation of interaction between atazanvir sulphate and bovine serum albumin by using fluorescence spectroscopy

Abstract

The fluorescence spectroscopic technique has been capably employed to investigate the interaction between bovine serum albumin (BSA) and atazanvir sulphate (AS) under the physiological pH 7.4 condition. The binding constant, number of binding site, thermodynamic parameters such as ∆G, ∆H, ∆S and nature of binding forces between BSA-AS were obtained by measuring the steady state fluorescence quenching of BSA by AS. The static quenching was confirmed from Stern-Volmer quenching constant at different temperature. The effect of AS on the conformation of BSA was analyzed using synchronous and three-dimensional fluorescence spectroscopy.