Liu Bing-Mi, Ma Ping, Wang Xin, Kong Yu-Mei, Zhang Li-Ping, Liu Bin
College of Pharmacy , Liaoning University, Shenyang 110036, P . R . China .
Department of Clinical Pharmacology, General Hospital of the Rocket Force, Beijing 100088, P.R.China.
Iran J Pharm Res. 2014 Fall;13(4):1183-90.
Three new rimantadine Schiff bases (RSBs) were prepared, and then the interaction of RSBs with bovine serum albumin (BSA) was investigated using fluorescence, synchronous fluorescence, UV-vis absorption spectroscopy under physiological conditions. The results showed that the three RSBs effectively quenched the intrinsic fluorescence of BSA via static quenching. Binding constant (K a), number of binding sites (n), and the binding distance (r) between three RSBs and BSA were calculated by Stern-Volmer equation and Förster's theory in this study. According to the results of displacement experiments of site probes, it was considered that the binding sites were located in hydrophobic cavities in sub-domains IIA of BSA. What is more, synchronous fluorescence studies indicated that the hydrophobicity around tryptophan residues was increased with the addition of rimantadine-o-vanillin (ROV) and rimantadine-4-methoxy-salicylaldehyde (RMS), while there was no apparent change with the addition of rimantadine-salicylaldehyde (RS).
制备了三种新型金刚烷胺席夫碱（RSBs），然后在生理条件下利用荧光、同步荧光、紫外可见吸收光谱研究了RSBs与牛血清白蛋白（BSA）的相互作用。结果表明，三种RSBs通过静态猝灭有效地猝灭了BSA的固有荧光。本研究通过Stern-Volmer方程和Förster理论计算了三种RSBs与BSA之间的结合常数（Ka）、结合位点数（n）和结合距离（r）。根据位点探针的置换实验结果，认为结合位点位于BSA亚结构域IIA的疏水腔内。此外，同步荧光研究表明，添加金刚烷胺邻香草醛（ROV）和金刚烷胺4-甲氧基水杨醛（RMS）后，色氨酸残基周围的疏水性增加，而添加金刚烷胺水杨醛（RS）后没有明显变化。
