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Spectroscopic Analysis of the Binding Interaction Between Tinidazole and Bovine Serum Albumin (BSA)

✍ Scribed by Xin Yu Shi; Hui Cao; Feng Lian Ren; Ming Xu

Publisher
John Wiley and Sons
Year
2007
Tongue
English
Weight
373 KB
Volume
4
Category
Article
ISSN
1612-1872

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✦ Synopsis

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.

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