谷胱甘肽-二茂铁的合成及其与牛血清白蛋白的相互作用

采用液相合成法, 以O-苯并三唑-N,N,N',N'-四甲基脲六氟磷酸酯(HBTU)和1-羟基苯并三氮唑(HOBT)为缩合剂, 将二茂铁胺和还原型谷胱甘肽(GSH)反应, 合成了具有电化学活性的谷胱甘肽-二茂铁(GSH-Fc), 其收率为23.2%, 并对目标产物进行了红外、核磁、质谱表征. 通过电化学方法研究了GSH-Fc与牛血清白蛋白(BSA)之间的相互作用特性. 电化学实验结果表明, BSA和GSH-Fc结合位点位于BSA的亚结构域IIA, 结合常数为1.71×106 L·mol-1, 结合位点数为1.30. 同时通过荧光光谱法研究了GSH-Fc与BSA相互作用是一种静态猝灭的过程, 结合常数和结合位点数分别为2.74×106 L·mol-1和1.57, 与电化学方法得到的结果相吻合.

Synthesis of Glutathionyl Ferrocene and Its Interaction with Bovine Serum Albumin

Glutathionyl ferrocene (GSH-Fc) was synthesized from glutathione and ferrocenyl amine using O-(benzotriazol-yl)-N,N,N',N'-tetramethyluronium(HBTU)/1-hydroxybenzotrizole (HOBT) as coupling agents in solution with a yield of 23.2%. The compound was characterized by 1H-NMR, IR and MS. Interactions of bovine serum albumin (BSA) with glutathionyl ferrocene were investigated by electrochemical methods. Experimental results revealed that there were specific interactions between BSA and GSH-Fc at the IIA subdomain. The binding constant and binding sites were obtained by linear sweep voltammetry and had values of 1.71×106 L·mol-1 and 1.30, respectively. Fluorescence spectroscopy methods were employed to investigate the interaction between GSH-Fc and BSA as well. Results showed that the fluorescence of BSA was quenched by GSH-Fc during a static quenching process. The binding constant and the number of binding sites were obtained and had values of 2.74×106 L·mol-1 and 1.57, respectively, which agreed well with results fromelectrochemical experiments.