Spectroscopic analysis of the binding interaction between tinidazole and bovine serum albumin (BSA) |
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Authors: | Shi Xin Yu Cao Hui Ren Feng Lian Xu Ming |
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Affiliation: | School of Chemistry and Chemical Engineering, Nantong University, Nantong, Jiangsu 226000, PR China. |
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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 F?rster'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. |
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Keywords: | Fluorescence spectroscopy Tinidazole Bovine serum albumin Resonance light scattering |
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