Fluorescence spectrometric study on the interaction of tamibarotene with bovine serum albumin |
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Authors: | Ye Huazhen Qiu Bin Lin Zhenyu Chen Guonan |
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Institution: | Ministry of Education Key Laboratory of Analysis and Detection for Food Safety, Fujian Provincial Key Laboratory of Analysis and Detection for Food Safety, Department of Chemistry, Fuzhou University, Fuzhou, Fujian 350002, China. |
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Abstract: | The interaction between tamibarotene and bovine serum albumin (BSA) was studied using fluorescence quenching technique and ultraviolet–visible spectrophotometry. The results of experiments showed that tamibarotene could strongly quench the intrinsic fluorescence of BSA by a dynamic quenching mechanism. The apparent binding constant, number of binding site and corresponding thermodynamic parameters at different temperatures were calculated respectively, and the main interaction force between tamibarotene and BSA was proved to be hydrophobic force. Synchronous fluorescence spectra showed that tamibarotene changed the molecular conformation of BSA. When BSA concentration was 1.00 × 10?6 mol L?1, the quenched fluorescence ΔF had a good linear relationship with the concentration of tamibarotene in the range 1.00 × 10?6 to 12.00 × 10?6 mol L?1 with the detection limit of 6.52 × 10?7 mol L?1. Copyright © 2010 John Wiley & Sons, Ltd. |
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Keywords: | tamibarotene bovine serum albumin interaction fluorescence |
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