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三丁基锡(TBT)化合物与牛血清白蛋白(BSA)的相互作用

Interaction of Tributyltin (TBT) Compound and Bovine Serum Albumin (BSA)

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【作者】 张朝红; 董殿波; 赵哲; 臧树良; 陈中林; 王杰; 张华春;

【Author】 ZHANG Zhao-hong1, DONG Dian-bo1, ZHAO Zhe1, ZANG Shu-liang1, 2, CHEN Zhong-lin1, WANG Jie1, ZHANG Hua-chun11. Department of Environmental Science, Liaoning University, Shenyang 110036, China2. Department of Chemistry, Liaoning University, Shenyang 110036, China

【机构】 辽宁大学环境科学系; 辽宁大学化学院 辽宁沈阳110036; 辽宁沈阳110036;

【摘要】 通过紫外、荧光和圆二色(CD)光谱,研究了船体防污漆的防污成分三丁基锡(TBT)化合物与牛血清白蛋白(BSA)的相互作用,考察了浓度、酸度和有机溶剂等因素的影响。结果表明,TBT与BSA的相互作用是双重的,既有TBT中丁基基团的疏水作用,又有锡离子与BSA的配位作用,使BSA内部的色氨酸和酪氨酸等芳香氨基酸残基裸露,导致BSA二级结构破坏,α-螺旋含量减少和构象改变。

【Abstract】 Tributyltin (TBT) compound is one of the main components of antifouling paint for boats and ships. The interaction of TBT compound and bovine serum albumin (BSA) was investigated by ultraviolet, fluorescence and circular dichroism (CD) spectra. The influences of concentration, acidity and organic solvent were also studied. The results showed that the interaction of TBT and BSA was dual, showing not only the hydrophobic actions of butyl groups but also the coordination action of tin cation with BSA molecule, which resulted in the exposures of aromatic amino acids residues of tryptophane and tyrosine in BSA molecule, the destruction of BSA secondary structure, the decrease in α-helix content, and the transformation of the conformation.

【基金】 国家自然科学基金项目(20271024);辽宁省教育厅自然科学基金项目(05L154)资助
  • 【文献出处】 光谱学与光谱分析 ,Spectroscopy and Spectral Analysis , 编辑部邮箱 ,2007年02期
  • 【分类号】Q355
  • 【被引频次】7
  • 【下载频次】288
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