| 光谱法研究儿茶素与牛血清白蛋白的相互作用 |
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| 引用本文： | 张海蓉,边贺东,潘英明,田建嬝,于青,梁宏,陈振锋.光谱法研究儿茶素与牛血清白蛋白的相互作用[J].光谱学与光谱分析,2009,29(11):3052-3056. |
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| 作者姓名： | 张海蓉 边贺东 潘英明 田建嬝 于青 梁宏 陈振锋 |
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| 作者单位： | 广西师范大学药用资源化学与药物分子工程教育部蕈点实验窀,广西,桂林,541004 |
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| 基金项目： | 国家自然科学基金项目，广西自然科学基金项目;广西高校自然科学基金以及教育部重点基金项目，药用资源化学与药物分子工程教育部重点实验室项目资助 |
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| 摘 要： | 运用荧光猝灭光谱、傅里叶红外光谱(FTIR)等光谱手段研究了模拟人体牛理条件下儿茶素与牛血清白蛋白(bovine serum albumin,BSA)的相互作用,求出了儿茶素与BSA结合的结合常数、结合位置、结合类型等参数,并研究了共存离子对儿茶素与BSA的结合常数的影响.实验结果表明:儿茶素与BsA形成复合物从而猝灭BSA的内源荧光,且其荧光猝灭机理符合静态机制.296,303,310 K下儿茶素与BSA结合的结合常数分别为:2.368,2.249,2.152×106 L·mol-1.热力学数据表明儿茶素与BsA主要靠疏水作用力和静电作用力结合,探针实验表明儿茶素与BSA在结合位点Site Ⅰ发生结合.F(o)ster偶极一偶极非辐射能量转移机理确定了儿茶素在BSA中与第214位色氨酸残基之间的距离r=1.93 nm.FTIR光谱显示,儿茶素诱导BSA的二级结构发生了变化.
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| 关 键 词： | 儿茶素 牛血清白蛋白 荧光光谱 傅里叶红外光谱 |
| 收稿时间： | 2008/11/26 |
Investigation of Interaction between Catechin and Bovine Serum Albumin by Spectroscopic Methods |
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| ZHANG Hai-rong,BIAN He-dong,PAN Ying-ming,TIAN Jian-niao,YU Qing,LIANG Hong,CHEN Zhen-feng Key Laboratory for Chemistry , Molecular Engineering of Medicinal Resources,Ministry of Education,Guangxi Normal University,Guilin ,China.Investigation of Interaction between Catechin and Bovine Serum Albumin by Spectroscopic Methods[J].Spectroscopy and Spectral Analysis,2009,29(11):3052-3056. |
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| Authors: | ZHANG Hai-rong BIAN He-dong PAN Ying-ming TIAN Jian-niao YU Qing LIANG Hong CHEN Zhen-feng Key Laboratory for Chemistry Molecular Engineering of Medicinal Resources Ministry of Education Guangxi Normal University Guilin China |
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| Institution: | ZHANG Hai-rong,BIAN He-dong,PAN Ying-ming,TIAN Jian-niao,YU Qing,LIANG Hong,CHEN Zhen-feng Key Laboratory for Chemistry and Molecular Engineering of Medicinal Resources,Ministry of Education,Guangxi Normal University,Guilin 541004,China |
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| Abstract: | In the present work,the interaction of catechin with bovine serum albumin (BSA) under physiological condition was studied by fluorescence quenching spectra in combination with Fourier transform infrared (FTIR) spectroscopy. The binding constants,the drug-binding mode,the binding site between catechin and BSA in aqueous solution at pH 7.40,and the effect of common ions were studied. The results show that catechin has the ability to quench the intrinsic fluorescence of BSA because of a complex formed,and the ... |
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| Keywords: | Catechin Bovine serum albumin (BSA) Fluorescence spectra FTIR spectra |
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