title: Mechanistic investigation on binding interaction of bioactive imidazole with protein bovine serum albumin--a biophysical study.
abstract: 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.
authors.affiliation: Department of Chemistry, Annamalai University, Annamalainagar, Tamilnadu 608002, India. jtchalam2005@yahoo.co.in
authors.forename: Jayaraman
authors.initials: J
authors.lastname: Jayabharathi
authors.forename: Venugopal
authors.initials: V
authors.lastname: Thanikachalam
authors.forename: Marimuthu
authors.initials: M
authors.lastname: Venkatesh Perumal
mesh_terms: D000818:Animals; D002417:Cattle; D031541:Fluorescence Resonance Energy Transfer; D007093:Imidazoles / Q000378:metabolism*; D011485:Protein Binding; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D017550:Spectroscopy, Fourier Transform Infrared; D013816:Thermodynamics
chemical_list: D007093:Imidazoles; D012710:Serum Albumin, Bovine; C029899:imidazole