手性钌配合物与牛血清白蛋白的相互作用
首发时间:2011-06-15
摘要:在模拟人体生理pH条件下,通过荧光和圆二色光谱研究了手性钌配合物Ru(bpy)2(p-mopip)]2+ (1)、∧- [Ru(bpy)2(p-mopip)]2+ (∧-1)和△- Ru(bpy)2(p-mopip)]2+ (△-1)与牛血清白蛋白(BSA)之间的相互作用。荧光光谱表明钌配合物∧-1、1和△-1对BSA的荧光猝灭机制为静态猝灭。∧-1、1和△-1与BSA的结合常数分别为6.72×103、5.87×103、 3.74×103 L•mol−1,结合位点数均为1。圆二色谱结果表明随着配合物浓度的增加,BSA的二级结构发生改变,由α-螺旋向β-折叠转化。
For information in English, please click here
Interaction between chiral ruthenium complex and bovine serum albumin
Abstract:The interactions of ruthenium(II) complexes Ru(bpy)2(p-mopip)]2+(1)、∧- [Ru(bpy)2(p-mopip)]2+(∧-1) and △- Ru(bpy)2(p-mopip)]2+(△-1) with bovine serum albumin (BSA) were investigated by fluorescence and circular dichroism (CD) spectra. The fluorescence quenching mechanism of BSA by ruthenium complexes ∧-1, 1, △-1, was determined to be a static process. The binding constant K for complexes ∧-1, 1, △-1, measured by fluorescence quenching method, were 6.72×10 3, 5.87×10 3 and 3.74×10 3 L•mol−1, respectively. The number of binding sites n for all these complexes was 1. The result of CD showed that the secondary structure of BSA molecules was changed in the presence of the ruthenium(II) complex. The reduction of the α-helix in favor of the β-sheet structure is indicative of a partial unfolding of protein.
Keywords: Chiral ruthenium complex Bovine serum albumin Interaction
基金:
论文图表:
引用
No.4431414595229130****
同行评议
共计0人参与
勘误表
手性钌配合物与牛血清白蛋白的相互作用
评论
全部评论0/1000