Zhao Mingming, Tang Ruiren, Xu Shuai
School of Chemistry and Chemical Engineering, Central South University, Changsha 410083, PR China; Hunan Police Academy, Changsha 410138, PR China.
School of Chemistry and Chemical Engineering, Central South University, Changsha 410083, PR China.
Spectrochim Acta A Mol Biomol Spectrosc. 2015 Jan 25;135:953-8. doi: 10.1016/j.saa.2014.07.089. Epub 2014 Aug 9.
A novel ligand, 2-methyl-6-(8-quinolinyl)-dicarboxylate pyridine (L), and its corresponding Tb (III) complex, Na4Tb(L)2Cl4·3H2O, were successfully prepared and characterized. The luminescence spectra showed that the ligand L was an efficient sensitizer for Tb (III) luminescence. The interaction of the complex with bovine serum albumin (BSA) was investigated through fluorescence spectroscopy under physiological conditions. The Stern-Volmer analysis indicated that the fluorescence quenching was resulted from static mechanism. The binding sites (n) approximated 1.0 and this meant that interaction of Na4Tb(L)2Cl4·3H2O with BSA had single binding site. The results showed van der Waals interactions and hydrogen bonds played major roles in the binding reaction. Furthermore, circular dichroism (CD) spectra indicated that the conformation of BSA was changed.
成功制备并表征了一种新型配体2-甲基-6-(8-喹啉基)-吡啶二羧酸酯（L）及其相应的铽（III）配合物Na4Tb(L)2Cl4·3H2O。发光光谱表明配体L是铽（III）发光的有效敏化剂。在生理条件下通过荧光光谱研究了该配合物与牛血清白蛋白（BSA）的相互作用。Stern-Volmer分析表明荧光猝灭是由静态机制引起的。结合位点（n）约为1.0，这意味着Na4Tb(L)2Cl4·3H2O与BSA的相互作用具有单一结合位点。结果表明范德华相互作用和氢键在结合反应中起主要作用。此外，圆二色性（CD）光谱表明BSA的构象发生了变化。
