Binding of triclosan to human serum albumin: insight into the molecular toxicity of emerging contaminant
Binding of triclosan to human serum albumin: insight into the molecular toxicity of emerging contaminant
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三氯生与人血清白蛋白的结合：深入了解新兴污染物的分子毒性
DOI：
10.1007/s11356-012-0901-5
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发表时间：
2012-07
影响因子：
5.8
通讯作者：
Lin, Shuangshuang
中科院分区：
文献类型：
--
作者：
Chen, Jiabin;Zhou, Xuefei;Zhang, Yalei;Zi, Yanqin;Qian, Yajie;Gao, Haiping;Lin, Shuangshuang
目的研究三氯生（TCS）与人血清白蛋白（HSA）的结合机理、结合常数、结合力类型、给受体结合距离以及TCS对HSA构象变化的影响。荧光猝灭光谱和同步光谱的记录与激发和发射狭缝的带的通道设置在10和20 nm。在加入TCS之前和之后记录HSA的三维荧光光谱。结果TCS对人血清白蛋白的荧光猝灭为静态猝灭，猝灭常数Ka分别为1.14 × 105，8.75 × 104，6.67 × 104，在293、298、303和309 K时，其平均温度分别为5.00 × 104和5.00 × 104。热力学参数，焓变（ΔH）和熵变（ΔS）计算为−37.9 kJ mol− 1和32.6 J mol− 1 K −1。根据Fürster非放射性能量转移理论，求得TCS与人血清白蛋白色氨酸残基的结合距离为1.81nm。紫外-可见吸收光谱、同步荧光光谱、三维荧光光谱和圆二色性光谱显示TCS对HSA二级结构的影响。结论TCS与HSA结合形成TCS-HSA复合物，结合距离为1.81nm。疏水相互作用和氢键在结合中占主导地位。TCS可改变HSA的二级构象。这项工作提供了一个新的污染物和蛋白质之间的非共价相互作用的见解，有助于阐明这些污染物的毒性机制。
PurposeThe interaction between triclosan (TCS) and human serum albumin (HSA) was investigated in order to obtain the binding mechanism, binding constant, the type of binding force, the binding distance between the donor and acceptor, and the effect of TCS on the conformation change of HSA.MethodsA HSA solution was added to the quartz cell and then titrated by successive addition of TCS. The fluorescence quenching spectra and synchronous spectra were recorded with the excitation and emission slits of the passage of band set at 10 and 20 nm. Three-dimensional fluorescence spectra of HSA were recorded before and after the addition of TCS. The capillary electrophoresis was conducted with the pressure injection mode at 0.5 psi for 5 s, separation under 25 kV, and detection at 214 nm.ResultsFluorescence data indicated the fluorescence quenching of HSA by TCS was static quenching, and the quenching constants (Ka) were 1.14 × 105, 8.75 × 104, 6.67 × 104, and 5.00 × 104at 293, 298, 303, and 309 K, respectively. The thermodynamic parameters, enthalpy change (ΔH) and entropy change (ΔS) for the interaction were calculated to be −37.9 kJ mol−1and 32.6 J mol−1K−1. The binding distance between TCS and tryptophan residues of HSA was obtained to be 1.81 nm according to Fǒrster nonradioactive energy transfer theory. The UV-Vis absorption spectroscopy, the synchronous fluorescence spectroscopy, three-dimensional fluorescence spectroscopy, and circular dichroism spectroscopy revealed the alterations of HSA secondary structure in the presence of TCS. Finally, the interaction between TCS and HSA was further confirmed by capillary electrophoresis.ConclusionsTCS was bound to HSA to form the TCS-HSA complex, with the binding distance of 1.81 nm. Hydrophobic interaction and hydrogen bond were dominated in the binding. TCS could change the secondary conformation of HSA. This work provides an insight into noncovalent interaction between emerging pollutants and protein, helping to elucidate the toxic mechanism of such pollutants.
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DOI：
10.1016/j.scitotenv.2009.10.049
发表时间：
2010
期刊：
The Science of the total environment
影响因子：
--
作者：
Y. Yoon;J. Ryu;Jeill Oh;B. Choi;S. Snyder
通讯作者：
Y. Yoon;J. Ryu;Jeill Oh;B. Choi;S. Snyder
影响因子：
2
作者：
M. Servos;Martha D. Smith;R. Mcinnis;B. Burnison;Bill-H. Lee;P. Seto;S. Backus
通讯作者：
M. Servos;Martha D. Smith;R. Mcinnis;B. Burnison;Bill-H. Lee;P. Seto;S. Backus
影响因子：
2.9
作者：
Jesper Østergaard;N. Heegaard
通讯作者：
Jesper Østergaard;N. Heegaard
影响因子：
2.9
作者：
LEHRER, SS
通讯作者：
LEHRER, SS
影响因子：
11.4
作者：
Herbert T. Buxton;D. Kolpin
通讯作者：
Herbert T. Buxton;D. Kolpin