中文摘要：

利用分子模拟、荧光光谱、紫外吸收光谱等方法，研究了4-羟基-2，2’，3，4’-四溴二苯醚（4-OH—BDE-42）与人血清白蛋白（HSA）的相互作用。三维荧光分析表明，4-OH—BDE-42的存在降低了HSA的荧光强度，且使HSA的微环境和构象发生变化。荧光光谱和紫外吸收光谱显示，4-OH—BDE-42与HSA结合后显著猝灭了HSA的内源性荧光，猝灭机制为静态猝灭与非辐射能量转移。结合常数Ka〉10^6L·mol^-1，表明两者的结合作用较强，结合距离r为3．66nm。根据热力学参数分析，△H〉0，AS〉0，即4-OH—BDE-42与HSA之间结合的主要作用力为疏水作用，这与分子对接、结合自由能分析结论一致。结合自由能贡献分析表明，LYS199、GLU292、ARG257、ARG218、ALA291、HIS242为4-OH—BDE-42与HSA结合的关键氨基酸残基。

英文摘要：

The binding of 4-hydroxyl-2,2＇ ,3,4＇ -tetrabromodiphenyl ether （4-OH-BDE-42） with human serum albumin （HSA） was investigated by molecular modeling, fluorescence spectroscopy and UV-Vis absorption spectroscopy. The results of three-dimensional （3D） fluorescence showed that the fluorescence intensity of HSA decreases in the presence of 4-OH-BDE-42, and the microenvironment and conformation in HSA are also changed. In addition, the characterizations of fluorescence and UV-Vis spectroscopy showed that the intrinsic fluorescence of HSA with binding to 4-OH-BDE-42 is definitely quenched via static quenching and non-radiative energy transfer. Kl is higher than 106 L＇mol-I , indicating there is a strong binding force between 4-OH-BDE-42 and HSA, and the binding distance r is obtained to be 3.66 nm. According to the analysis of thermodynamic parameters, the hydrophobic interaction was identified as the major driving force for the binding with △H 〉 0, AS 〉 0, which is consistent with the results of molecular docking and the analysis of binding free energy. The residues, LYS199, GLU292, ARG257, ARG218, ALA291, and HIS242, were identified as the key residues in binding site of HSA.