硝酸咪康唑与牛血清白蛋白作用的热力学特征研究  

Studies on the Thermodynamics Features of the Interactionbetween Miconazole Nitrate and Bovine Serum Albumin

作　　者：吴刚珂[1] 李素丽[2] 颜承农[2] 刘义[3] 

机构地区：[1]荆州市中心医院检验科,湖北荆州434020 [2]长江大学工程技术学院,湖北荆州434020 [3]武汉大学化学与分子科学学院,湖北武汉430072

出　　处：《分析科学学报》2010年第2期157-161,共5页Journal of Analytical Science

基　　金：国家自然科学基金(No.30570015;20373051);湖北省自然科学基金(No.2005ABA067)

摘　　要：在模拟动物体生理条件和不同温度下,用荧光猝灭光谱、同步荧光光谱、三维荧光光谱和紫外可见吸收光谱等,研究了不同温度下硝酸咪康唑(Miconazole Nitrate,MIN)与牛血清白蛋白(BSA)相互作用的光谱行为。用Stern-Volmer方程、Lineweav-er-Burk双倒数方程和热力学方程等处理实验数据,得到在16～37℃温度范围内的作用常数KLB及热力学参数;发现MIN与BSA可结合形成具有一定结构的复合物,其荧光猝灭作用更符合静态猝灭作用特征,作用力可能主要是静电力;同时探讨了MIN对BSA构象的影响。为研究MIN的治病机制和生物学效应等提供了重要信息。Under the imitated physiological condition of animals and different temperatures,the interaction of miconazole nitratel（MIN） to bovine serum albumin（BSA） was studied by means of the fluorescence quenching spectrum,synchronous fluorescence spectrum,three-dimensional fluorescence spectrum and ultro-violet spectrum.The average value of bonding constant（KLB：2.077×104 L／5mol-1）,thermodynamic parameters （△Hθ：-13.23 kJ／5mol-1,△Gθ：-24.74 kJ／5mol-1,△Sθ：38.41 J／5K-1） and number of bonding sites（0.9167） were obtained. It has been proved that BSA interacted with miconazole nitrate and form a new compound by analyzing the fluorescence quenching data by Stern-Volmer equation,Lineweaver-Burk equation and thermodynamic equation,and the decrease of fluorescence of BSA was caused by a static quenching mechanism possibly owing to the electrostatic forces between BSA and MIN. The comformational modification of BSA was also investigated. It would provide important information for the study of the mechanism of disease and the biological effects.

关 键 词：硝酸咪康唑 牛血清白蛋白 荧光光谱 紫外吸收光谱 热力学参数 

分 类 号：O657.39[理学—分析化学]