【作者】 胡敏； 张镇西； 陈国军；

【Author】 HU Min~1,ZHANG Zhen-xi~2,CHEN Guo-jun~(2*) 1.Department of Applied Chemistry,School of Science,Xi’an Jiaotong University,Xi’an 710049,China 2.The Key Laboratory of Biomedical Information Engineering of Ministry of Education,Institute of Biomedical Engineering, Xi’an Jiaotong University,Xi’an 710049,China

【机构】 西安交通大学理学院应用化学系； 西安交通大学生命学院,生物医学信息工程教育部重点实验室,生物医学工程研究所；

【摘要】 本文研究两亲性配合物四甘氨酸锌酞菁（ZnAAPc）与牛血清白蛋白（BSA）的相互作用。研究表明ZnAAPc在DMF等有机溶剂中呈现出典型的酞菁的吸收光谱特征,Q吸收带>700 nm。ZnAAPc对BSA有较强的亲和作用。ZnAAPc对BSA的荧光猝灭以静态猝灭为主,结合常数为2.35×10⁴ L·mol^-1。ZnAAPc与BSA结合时是通过分子间非辐射能量转移机制而促使蛋白质的荧光猝灭,对BSA构象影响小。热力学数据表明ZnAAPc与BSA作用为疏水作用和静电作用。更多还原

【Abstract】 The interactions of ZnAApc with bovine serum albumin(BSA) were studied by using Fluorescence spectra.Fluorescence emission spectra of BSA in the presence of the investigated compounds clearly showed that the ZnAApc quenched the fluorescence of BSA.The binding constants and the number of binding sites of ZnAApc with BSA were obtained.And the results indicated that there existed strongly binding affinity between ZnAApc and BSA.The mechanism of the Forster energy transference efficiency between the ZnAApc and BSA were found.更多还原