Lin Yongxin, Jiao Genlong, Sun Guodong, Zhang Lili, Wang Shilong, Liu Hanchao, Li Zhizhong
Department of Orthopedics, the First Affiliated Hospital of Jinan University, Guangzhou, 510630, China.
Luminescence. 2014 Mar;29(2):109-17. doi: 10.1002/bio.2512. Epub 2013 Apr 22.
In this paper, the binding properties of teicoplanin and vancomycin to bovine serum albumin (BSA) were investigated using fluorescence quenching, synchronous fluorescence, Fourier transform infrared (FTIR), circular dichroism (CD) and UV-vis spectroscopic techniques and molecular docking under simulative physiological conditions. The results obtained from fluorescence quenching data revealed that the drug-BSA interaction altered the conformational structure of BSA. Meanwhile, the 3D fluorescence, CD, FTIR and UV-vis data demonstrated that the conformation of BSA was slightly altered in the presence of teicoplanin and vancomycin, with different reduced α-helical contents. The binding distances for the drug-BSA system were provided by the efficiency of fluorescence resonance energy transfer (FRET). Furthermore, the thermodynamic analysis implied that hydrogen bond and van der Waals' forces were the main interaction for the drug-BSA systems, which agreed well with the results from the molecular modeling study. The results obtained herein will be of biological significance in future toxicological and pharmacological investigation.
本文在模拟生理条件下，采用荧光猝灭、同步荧光、傅里叶变换红外光谱（FTIR）、圆二色光谱（CD）、紫外可见光谱技术及分子对接方法，研究了替考拉宁和万古霉素与牛血清白蛋白（BSA）的结合特性。荧光猝灭数据结果表明，药物与BSA的相互作用改变了BSA的构象结构。同时，三维荧光、CD、FTIR和紫外可见光谱数据表明，在替考拉宁和万古霉素存在的情况下，BSA的构象略有改变，α-螺旋含量降低程度不同。荧光共振能量转移（FRET）效率给出了药物-BSA体系的结合距离。此外，热力学分析表明，氢键和范德华力是药物-BSA体系的主要相互作用，这与分子模拟研究结果吻合良好。本文所得结果在未来的毒理学和药理学研究中将具有生物学意义。
