Investigation on the pH-dependent binding of Eosin Y and bovine serum albumin by spectral methods |
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Authors: | Dejiang Gao Fanghui Liang Yanhua Chen Aimin Yu |
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Institution: | a College of Chemistry, Jilin University, Changchun 130012, China b Changchun Medical College, Changchun 130031, China |
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Abstract: | In this paper, the pH-dependent binding of Eosin Y and bovine serum albumin (BSA) was investigated by spectral methods, including resonance light scattering (RLS), absorption and fluorescence spectrometry. Due to the pH-dependent structure of Eosin Y and BSA, the interaction of BSA and Eosin Y depended on the solution pH value. Especially at pH 2.6 and 9.2, the RLS intensity of BSA was obviously enhanced in the presence of Eosin Y. However, the fluorescence intensity of BSA was quenched in the presence of Eosin Y. To fully understand the pH-dependent binding of BSA and Eosin Y, fluorescence quenching technique was introduced. Based on the fluorescence data obtained, the style of binding, the binding constant, the binding site number and the thermodynamic parameters for the interaction of BSA and Eosin Y were studied. Based on Förster non-radiation energy transfer theory, the distance between donor BSA and acceptor Eosin Y was obtained. |
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Keywords: | Bovine serum albumin Eosin Y Resonance light scattering Absorption spectrometry Fluorescence quenching technique |
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