title: Spectroscopic analysis of the binding interaction between tinidazole and bovine serum albumin (BSA).
abstract: The interaction between bovine serum albumin (BSA) and tinidazole (Tindamax; 1) in aqueous solution was investigated in detail by means of UV/VIS and fluorescence spectroscopy, as well as through resonance light-scattering (RLS) spectroscopy. The apparent binding constant and number of binding sites were determined at three different temperatures, as well as the average binding distances between 1 and the nearest amino acid residue(s) of BSA, as analyzed by means of Förster's theory of non-radiation energy transfer. Compound 1 was found to quench the inner fluorescence of BSA by forming a tight 1:1 aggregate, based on both static quenching and non-radiation energy transfer. The entropy change upon complexation was positive, and the enthalpy change was negative, indicating that the observed spontaneous binding is mainly driven by electrostatic interactions.
authors: School of Chemistry and Chemical Engineering, Nantong University, Nantong, Jiangsu 226000, PR China.
authors: Xin Yu
authors: XY
authors: Shi
authors: Hui
authors: H
authors: Cao
authors: Feng Lian
authors: FL
authors: Ren
authors: Ming
authors: M
authors: Xu
mesh_terms: D000818:Animals; D001665:Binding Sites; D002417:Cattle; D015394:Molecular Structure; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D012996:Solutions / Q000737:chemistry; D013057:Spectrum Analysis; D013696:Temperature; D013816:Thermodynamics; D014011:Tinidazole / Q000737:chemistry*
chemical_list: D012996:Solutions; D014011:Tinidazole; D012710:Serum Albumin, Bovine