手性钌配合物与牛血清白蛋白的相互作用

he 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.