Spectroscopic studies on the interaction between sodium ozagrel and bovine serum albumin

The mutual interaction of sodium ozagrel (SO) with bovine serum albumin (BSA) was investigated using fluorescence, UV–vis absorption and Fourier transform infrared (FT-IR) spectroscopy under physiological conditions. The fluorescence quenching mechanism of BSA by SO was analyzed. The binding constants and the corresponding thermodynamic parameters at different temperatures were calculated. The binding distance between SO and BSA was obtained based on the theory of Forester’s non-radiation energy transfer. Displacement experiments were performed to identify SO binding sites in BSA. Moreover, the effect of sodium ozagrel on the conformation of BSA was analyzed according to synchronous fluorescence, UV–vis absorption and FT-IR spectra. The effect of some common ions on the binding constant between SO and BSA was also examined.