表面活性荧光探针分子与牛血清蛋白的相互作用

Interaction of Surface Active Fluorescence Probes and Bovine Serum Albumin

研究了两种表面活性荧光探针分子2(对十二烷基氨基)苯基3,3二甲基5乙酯基3H吲哚基甲基二十六烷基碘化铵(1)和2(对十二烷基氨基)苯基3,3二甲基5乙酯基3H吲哚基二甲基十八烷基碘化铵(2)与牛血清蛋白(BSA)之间的相互作用。根据结合反应的温度效应求得热力学函数并推断探针分子与BSA结合的作用力类型;分子1和2与牛血清蛋白之间存在能量转移现象,根据Frster非辐射能量转移理论计算得到给体受体之间的距离分别为2.90和4.02nm。

The binding between two surface-active substituted 3H-indole fluorescence probes, i.e. , iodo-dihexadecyl methyl-2-（ p-do- decyl amino phenyl）-3, 3-dimethyl-5-carboethoxy-3H-indole ammonium and iodo-dimethyloctadecyl-2-（ p-dodecyl amino phenyl）-3,3- dimethyl-5-carboethoxy-3H-indole ammonium, and bovine serum albumin （BSA） in aqueous solution was studied using fluorescence. The binding constant and binding site number of molecule 1 and molecule 2 with BSA were obtained. It was confirmed that electrostatic interaction is the primary driving force for the combination of BSA with molecule 1 or molecule 2. According to the Fǒrster resonance energy transfer theory, the distances between molecule 1, molecule 2 and tryptophan of BSA were calculated to be 2.90 nm and 4.02 nm, respectively.