Liu Rong, Cheng Zhengjun, Jiang Xiaohui
Chemical Synthesis and Pollution Control Key Laboratory of Sichuan Province, China West Normal University, Nanchong, 637002, China.
Luminescence. 2014 Dec;29(8):1033-46. doi: 10.1002/bio.2655. Epub 2014 May 8.
The interactions of dihydroartemisinin (DHA) and artemisinin (ART) with bovine serum albumin (BSA) have been investigated using fluorescence, UV/vis absorption and Fourier transform infrared (FTIR) spectra under simulated physiological conditions. The binding characteristics of DHA/ART and BSA were determined by fluorescence emission and resonance light scattering (RLS) spectra. The quenching mechanism between BSA and DHA/ART is static. The binding constants and binding sites of DHA/ART-BSA systems were calculated at different temperatures (293, 298, 304 and 310 K). According to Förster non-radiative energy transfer theory, the binding distance of BSA to DHA/ART was calculated to be 1.54/1.65 nm. The effect of DHA/ART on the secondary structure of BSA was analyzed using UV/vis absorption, FTIR, synchronous fluorescence and 3D fluorescence spectra. In addition, the effects of common ions on the binding constants of BSA-DHA and BSA-ART systems were also discussed.
在模拟生理条件下，利用荧光、紫外/可见吸收光谱和傅里叶变换红外（FTIR）光谱研究了双氢青蒿素（DHA）和青蒿素（ART）与牛血清白蛋白（BSA）的相互作用。通过荧光发射光谱和共振光散射（RLS）光谱确定了DHA/ART与BSA的结合特性。BSA与DHA/ART之间的猝灭机制为静态猝灭。计算了不同温度（293、298、304和310 K）下DHA/ART-BSA体系的结合常数和结合位点。根据Förster非辐射能量转移理论，计算出BSA与DHA/ART的结合距离为1.54/1.65 nm。利用紫外/可见吸收光谱、FTIR光谱、同步荧光光谱和三维荧光光谱分析了DHA/ART对BSA二级结构的影响。此外，还讨论了常见离子对BSA-DHA和BSA-ART体系结合常数的影响。
