Investigation of the interaction between trazodone hydrochloride and bovine serum albumin

In this paper, the binding of trazodone hydrochloride (TZH) to bovine serum albumin (BSA) was investigated by spectroscopic (fluorescence, spectrophotometry and circular dichroism) techniques under simulative physiological conditions. A strong fluorescence quenching reaction of TZH to BSA was observed and the quenching mechanism was suggested as dynamic quenching according to the Stern-Volmer equation. The binding constants of TZH with BSA at 288, 302 and 309 K were calculated as (1.56±0.003)×104, (2.31±0.002)×104 and (5.44±0.004)×104 M−1, respectively. The thermodynamic parameters, ΔH0 and ΔS0 were obtained to be 39.86±0.008 kJ mol−1 and 217.89±0.011 J mol−1 K−1, respectively, which indicated the presence of hydrophobic forces between TZH and BSA. The spectral results observed showed that the binding of TZH to BSA induced conformational changes in BSA. Based on the Förster's theory of non-radiation energy transfer, the binding average distance, r between donor (BSA) and acceptor (TZH) was found to be 2.4 nm. The effect of common ions on binding of TZH to BSA was also examined.