Spectroscopic analysis of the interaction between bilirubin and bovine serum albumin |
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Authors: | Juan Chen Gongwu Song Yu He Qiujun Yan |
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Affiliation: | (1) Ministry-of-Education Key Laboratory for the Synthesis and Application of Organic Functional Molecules, Hubei University, 430062 Wuhan City, Hubei Province, P.R. China |
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Abstract: | The interactions between bilirubin (BR) and bovine serum albumin (BSA) have been studied by fluorescence spectroscopy. The association constant between BR and BSA was obtained by fluorescence enhancement titration. Furthermore, fluorescence quenching was studied at different temperatures, and the binding constant was also determined by the method of fluorescence quenching. The two methods yielded similar results. It indicated that the former method could be successfully applied to the determination of BR. The results showed that the binding of BR to BSA induced conformational changes in BSA. Based on the theory of F?rster energy transfer, the distance between BR and protein were calculated. According to the thermodynamic parameters, the main binding force could be judged. The experimental results revealed that BSA and BR had strong interactions. The mechanism of quenching belonged to static quenching and the main sort of binding force was van der Waals interactions and hydrogen bonds. |
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Keywords: | : Bovine serum albumin bilirubin fluorescence spectrum binding constant energy transfer. |
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