| 杨露露,杨雾,伍智蔚,易忠胜.化学通报,2017,80(2):185-190,207. |
| 计算模拟与光谱法研究4-羟基-2, 2＇, 3, 4＇-四溴二苯醚与人血清白蛋白的相互作用 |
| Study on the interaction of 4-hydroxyl-2,2'',3,4''-tetrabromodiphenyl ether with human serum albumin by computer-aided molecular modeling and spectroscopy |
| 投稿时间：2016-06-20 修订日期：2016-08-01 |
| DOI： |
| 中文关键词: 羟基化多溴联苯醚 人血清白蛋白 光谱法 计算模拟 相互作用 |
| 英文关键词:hydroxylated polybrominated diphenyl ethers human serum albumin spectroscopy computational simulations interaction |
| 基金项目:国家自然科学基金项目(No.21267008) ，广西自然科学基金项目(No.2013GXNSFAA019034)和广西高等学校高水平创新团队及卓越学者计划项目(桂教人〔2014〕49号) |
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| 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发生结合作用显著猝灭了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 > 106 L?mol-1表明两者的结合作用较强，结合距离r为3.66 nm。根据热力学参数分析，ΔH﹥0，ΔS﹥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 ultraviolet-visible (UV–vis) absorption spectroscopy. The results of three-dimensional (3D) fluorescence have shown that the fluorescence intensity of HSA was decreased in the presence of 4-OH-BDE-42, and the microenvironment and conformation in HSA was also changed. In addition, the characterizations of fluorescence and ultraviolet-visible spectroscopy showed that the intrinsic fluorescence of HSA with binding to 4-OH-BDE-42 was definitely quenched via static quenching and non-radiative energy transfer. The higher than 106 L?mol-1 value of Ka indicates there is a strong binding force between 4-OH-BDE-42 and HSA, and the binding distance r was 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 ΔH>0, ΔS>0. That was 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. |
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