Yue Yuanyuan, Liu Jianming, Liu Ren, Dong Qiao, Fan Jing
School of Environment, Henan Normal University, Xinxiang, Henan 453007, PR China; School of Chemistry and Chemical Engineering, Henan Normal University, Xinxiang, Henan 453007, PR China.
School of Chemistry and Chemical Engineering, Henan Normal University, Xinxiang, Henan 453007, PR China.
Spectrochim Acta A Mol Biomol Spectrosc. 2014 Apr 24;124:46-51. doi: 10.1016/j.saa.2013.12.108. Epub 2014 Jan 8.
The interaction between human serum albumin and helicid was studied by steady-state fluorescence, ultraviolet-visible, circular dichroism, Fourier transform infrared techniques and molecular modeling. The binding site numbers, association constants, and corresponding thermodynamic parameters were used to investigate the quenching mechanism. The alternations of protein secondary structure in the presence of helicid were demonstrated using synchronous fluorescence, Fourier transform infrared, circular dichroism and three-dimensional fluorescence spectra. The molecular modeling results revealed that helicid could bind to hydrophobic pocket of HSA with hydrophobic and hydrogen bond force. The binding site of helicid in HSA was ascertained. Moreover, an apparent distance of 3.33 nm between the Trp214 and helicid was obtained via fluorescence resonance energy transfer method.
采用稳态荧光、紫外可见光谱、圆二色光谱、傅里叶变换红外光谱技术及分子模拟研究了人血清白蛋白与蛇床子素的相互作用。利用结合位点数、结合常数及相应的热力学参数研究猝灭机制。通过同步荧光光谱、傅里叶变换红外光谱、圆二色光谱和三维荧光光谱证明了蛇床子素存在下蛋白质二级结构的变化。分子模拟结果表明，蛇床子素可通过疏水作用和氢键作用与人血清白蛋白的疏水口袋结合，确定了蛇床子素与人血清白蛋白的结合位点。此外，通过荧光共振能量转移法测得色氨酸214与蛇床子素之间的表观距离为3.33 nm。
