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

作者：Jayabharathi Jayaraman^*; Thanikachalam Venugopal; Perumal Marimuthu Venkatesh

来源：Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy , 2011, 79(3): 502-507.

DOI：10.1016/j.saa.2011.03.020

• Bioactive imidazole
• FRET
• Stern-Volmer plot
• Thermodynamic parameters
• ROSS theory

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 x 10(4), 2.56 x 10(4), and 2.10 x 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 (Delta G, Delta H and Delta S) 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.

• 出版日期2011-8