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荧光法对姜黄素与牛血清白蛋白相互作用的研究
引用本文:张晓星,何苗,刘爱林,陈伟,林新华.荧光法对姜黄素与牛血清白蛋白相互作用的研究[J].光谱实验室,2010,27(2):395-401.
作者姓名:张晓星  何苗  刘爱林  陈伟  林新华
作者单位:福建医科大学药学院,福州市台江区交通路88号,350004
基金项目:福建省自然科学基金(0710024)
摘    要:应用荧光光谱法研究了生理条件下(pH7.4)姜黄素(Curcumin)与牛血清白蛋白(BSA)的相互作用。实验结果表明,姜黄素对BSA产生荧光猝灭作用,其机理属于静态猝灭过程。T=310K时,其猝灭常数为1.388×1012L.mol-1.s-1,表观结合常数为2.387×104L.mol-1。根据Foerster非辐射能量转移理论,测得姜黄素在BSA中的结合位置与色氨酸残基间的距离为4.43nm。探讨了姜黄素对BSA构象的影响及结合机理,考察了体内某些共存金属离子对姜黄素与BSA结合作用的影响。

关 键 词:姜黄素  牛血清白蛋白  相互作用  荧光光谱法

Study on the Interaction Between Curcumin and Bovine Serum Albumin by Fluorescence Spectrometry
Zhang Xiao-Xing,He Miao,Liu Ai-Lin,Chen Wei,Lin Xin-Hua.Study on the Interaction Between Curcumin and Bovine Serum Albumin by Fluorescence Spectrometry[J].Chinese Journal of Spectroscopy Laboratory,2010,27(2):395-401.
Authors:Zhang Xiao-Xing  He Miao  Liu Ai-Lin  Chen Wei  Lin Xin-Hua
Affiliation:Fujian Medical University;Fuzhou 350004;P.R.China
Abstract:The interaction between cureumin and bovine serum albumin was studied under the physiological conditions (pH 7.4) by fluorescence spectrometry.The curcumin can quench the fluorescence of bovine serum albumin and the quenching mechanism is static quenching process.At 310K,the quenching constant is 1.388×10~(12)L·mol~(-1)·s~(-1) and the apparent binding constant is 2.387×10~4L·mol~(-1).According to the Foerster theory of non-radiation energy transferring, the binding locality of curcumin is measured to be 4.43nm away from tryptophan residues in BSA.The binding mechanism and the influence of curcumin on BSA confirmation were studied.Furthermore, the effect of some metal ions on the interaction between curcumin and BSA was also investigated.
Keywords:Curcumin  Bovine Serum Albumin (BSA)  Interaction  Fluorescence Spectrometry
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