| 荧光光谱法研究橙皮素与牛血清白蛋白的相互作用 |
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| 引用本文： | 尚永辉.荧光光谱法研究橙皮素与牛血清白蛋白的相互作用[J].化学工程师,2011(1):12-13,17. |
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| 作者姓名： | 尚永辉 |
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| 作者单位： | 咸阳师范学院,化学与化工学院,陕西,咸阳,712000 |
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| 基金项目： | 国家自然科学基金，陕西省教育厅科研计划项目，西北大学研究生交叉学科资助项目 |
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| 摘 要： | 采用荧光光谱技术研究了橙皮素与牛血清白蛋白(BSA)的相互作用.研究发现橙皮素对BSA的荧光猝灭属于静态猝灭过程,由热力学参数焓变△rHm=-60.543 kJ·mol<'-1>,熵变△rSm-114.121J-mol<'-1>均小于零,判断橙皮素与BSA之间主要靠氧键和范德华力相结合,生成自由能变(△rGm)为负值,...
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| 关 键 词： | 橙皮素 牛血清白蛋白 荧光光谱 |
Study on the interaction between hesperetin and bovine serum albumin by fluorescence spectroscopy |
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| SHANG Yong-hui.Study on the interaction between hesperetin and bovine serum albumin by fluorescence spectroscopy[J].Chemical Engineer,2011(1):12-13,17. |
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| Authors: | SHANG Yong-hui |
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| Affiliation: | SHANG Yong-hui(School of Chemistry & Chemical Engineering,Xianyang Normal University,Xianyang 712000,China) |
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| Abstract: | The interaction behavior between Hesperetin and Bovine Serum Albumin（BSA） was studied by fluorescence spectroscopy.The quenching constants were obtained at 292K,299 K,311K and 315t K,the results indicated that the fluorescence quenching mechanism for BSA through Hesperetin binding is likely a static quenching process.The thermodynamic parameters,enthalpy change（△rHm） and entropy change（△rSm）,were calculated to be-60.543 kJ·mol-10,and-114.121J·mol-10,respectively,which indicated that the interaction of Hesperetin with BSA was driven mainly by hydrogen bond and Van der Walls force.The process of binding was a spontaneous process in which Gibbs free energy change（△rGm） was negative.The effect of Hesperetin on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy. |
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| Keywords: | Hesperetin Bovine Serum Albumin(BSA) fluorescence spectroscopy |
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