Mechanistic investigation on binding interaction of bioactive imidazole with protein bovine serum albumin - A biophysical study

摘要

The interaction between bioactive imidazole derivative (PPP) and bovine serum albumin (BSA) was investigated using fluorescence and UV-vis spectral studies. The experimental results showed that the fluorescence quenching of BSA by imidazole derivative was the result of the formation of BSA-PPP complex and the effective quenching constants (K_(SV)) were 2.66 × 10 ~4, 2.56 × 10~4, and 2.10 × 10~4 at 301, 310 and 318 K, respectively. Static quenching and non-radiative energy transfer were confirmed to the result in the fluorescence quenching. The binding site number n, apparent binding constant K_A and corresponding thermodynamic parameters (ΔG, ΔH and ΔS) were measured at different temperatures. The process of binding of PPP molecule on BSA was a spontaneous molecular interaction procedure in which entropy increased and Gibbs free energy decreased.