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

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

Investigations on interaction between atazanvir sulphate and bovine serum albumin by fluorescence spectroscopy

820-823The interaction between bovine serum albumin (BSA) and atazanvir sulphate (AS) has been investigated under the physiological pH 7.4 condition using fluoresence spectroscopy. The binding constant, number of binding site, thermodynamic parameters such as ∆G, ∆H, ∆S and nature of binding forces between BSA-AS have been obtained from the steady state fluorescence quenching of BSA by AS. The static quenching is confirmed from Stern-Volmer quenching constant at different temperatures. The effect of AS on the conformation of BSA has been analyzed using synchronous and three-dimensional fluorescence spectroscopy