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Investigation on the interaction between 3, 5-dihydroxytoluene and bovine serum albumin by fluorescence spectroscopy

机译:荧光光谱法研究3,5-二羟基甲苯与牛血清白蛋白的相互作用

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The interaction between 3, 5-dihydroxytoluene and bovine serum albumin (BSA) had been investigated by fluorescence spectroscopy. By the analysis of fluorescence spectrum and fluorescence intensity, it was observed that the 3, 5-dihydroxytoluene had a strong ability to quench the intrinsic fluorescence of BSA through a static quenching procedure. The binding constant and the number of binding sites were determined at 298 K based on fluorescence quenching results. The thermodynamic parameters such as enthalpy change (ΔH), entropy change (ΔS) and Gibbs free-energy change (ΔG) for the reactions were also calculated according to the thermodynamic equations. The negative ΔH and ΔS values in case of 3, 5-dihydroxytoluene-BSA complexes showed that van der Waals interactions and hydrogen bonds might play a major role in the binding of 3, 5-dihydroxytoluene to BSA. The distance, r, between donor (BSA) and acceptor (3, 5-dihydroxytoluene) was obtained according to the Förster''s theory of non-radiation energy transfer. The experimental results of synchronous fluorescence spectroscopy showed that the binding of 3, 5-dihydroxytoluene to BSA induced conformational changes in BSA.
机译:通过荧光光谱研究了3,5-二羟基甲苯和牛血清白蛋白(BSA)之间的相互作用。通过荧光光谱和荧光强度的分析,观察到3,5-二羟基甲苯具有通过静态猝灭程序猝灭BSA的固有荧光的强大能力。基于荧光猝灭结果,在298K下确定结合常数和结合位点数。还根据热力学方程计算了反应的热力学参数,例如焓变(ΔH),熵变(ΔS)和吉布斯自由能变化(ΔG)。在3,5-二羟基甲苯-BSA配合物的情况下,ΔH和ΔS值为负,表明范德华相互作用和氢键可能在3,5-二羟基甲苯与BSA的结合中起主要作用。供体(BSA)和受体(3,5-二羟基甲苯)之间的距离r是根据Förster的非辐射能量转移理论得出的。同步荧光光谱法的实验结果表明,3,5-二羟基甲苯与BSA的结合引起BSA的构象变化。

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