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荧光光谱法研究橙皮甙与牛血清白蛋白的相互作用
引用本文:尚永辉,孙家娟,刘静,耿薇.荧光光谱法研究橙皮甙与牛血清白蛋白的相互作用[J].化学分析计量,2011,20(1):32-34.
作者姓名:尚永辉  孙家娟  刘静  耿薇
作者单位:咸阳师范学院化学与化工学院,咸阳,712000
基金项目:国家自然科学基金项目,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
摘    要:在pH7.40的Tris-HCl 缓冲体系中,采用荧光光谱技术研究了橙皮甙与牛血清白蛋白(BSA)的相互作用.随着温度升高,橙皮甙与BSA 的猝灭常数逐渐增加.实验表明:橙皮甙对BSA的荧光猝灭为动态猝灭过程.由热力学参数焓变(△H=70.71 kJ/mol)大于零和熵变△S=316.29J/(mol·K)]大于零,...

关 键 词:橙皮甙  牛血清白蛋白  荧光光谱

STUDY ON THE INTERACTION BETWEEN HESPERIDINUM AND BOVINE SERUM ALBUMIN BY FLUORESCENCE SPECTROSCOPY
Shang Yonghui,Sun Jiajuan,Liu Jing,Geng Wei.STUDY ON THE INTERACTION BETWEEN HESPERIDINUM AND BOVINE SERUM ALBUMIN BY FLUORESCENCE SPECTROSCOPY[J].Chemical Analysis And Meterage,2011,20(1):32-34.
Authors:Shang Yonghui  Sun Jiajuan  Liu Jing  Geng Wei
Institution:Shang Yonghui,Sun Jiajuan,Liu Jing,Geng Wei (School of Chemistry & Chemical Engineering,Xianyang Normal University,Xianyang712000,China)
Abstract:The interaction behavior between hesperidinum and bovine serum albumin(BSA) in phYsiological buffer( pH 7.4) was studied by fluorescence spectroscopy. The quenching constants were obtained at 295K, 303K, 310K and 315K. The results indicated that the fluorescence quenching mechanism for BSA through hesperidinum binding was likely a dynamic quenching process. The thermodynamic parameters, enthalpy change (AH) and entropy change (AS) were calculated to be 70.71 kJ/mol and 316.29 J/(mol·K), respectively, which indicated that the interachon of hesperidinum with BSA was driven mainly by hydrophobic interaction. The process of binding was a spontaneous process in which Gibbs free energy change was negative. The effect of hesperidinum on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy.
Keywords:hesperidinum  bovine serum albumin(BSA)  fluorescence spectroscopy  
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