Wang Yan-Qing, Zhang Hong-Mei, Cao Jian, Tang Bo-Ping
Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection, Yancheng City, Jiangsu Province 224002, People's Republic of China; Institute of Applied Chemistry and Environmental Engineering, Yancheng Teachers University, Yancheng City, Jiangsu Province 224002, People's Republic of China.
Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection, Yancheng City, Jiangsu Province 224002, People's Republic of China; Institute of Applied Chemistry and Environmental Engineering, Yancheng Teachers University, Yancheng City, Jiangsu Province 224002, People's Republic of China.
J Photochem Photobiol B. 2014 Sep 5;138:182-90. doi: 10.1016/j.jphotobiol.2014.06.002. Epub 2014 Jun 11.
Interactions of bisphenol S, a new bisphenol analogue with bovine serum albumin and calf thymus DNA were investigated using different spectroscopic methods and molecular modeling calculation. According to the analysis of experimental and theoretical data, we concluded that hydrophobic interactions and hydrogen bonding primarily mediated the binding processes of bisphenol S with bovine serum albumin and DNA. In addition, the electrostatic force should not be excluded. Molecular modeling studies indicated that the binding site of bisphenol S to bovine serum albumin located in the subdomain IB, while bisphenol S was a groove binder of DNA. In addition, BPS did not obviously induce second structural changes of bovine serum albumin, but it induced a conformational change of calf thymus DNA.
采用不同的光谱方法和分子模拟计算，研究了新型双酚类似物双酚S与牛血清白蛋白和小牛胸腺DNA的相互作用。根据实验和理论数据的分析，我们得出结论，疏水相互作用和氢键主要介导了双酚S与牛血清白蛋白和DNA的结合过程。此外，静电力也不应被排除。分子模拟研究表明，双酚S与牛血清白蛋白的结合位点位于亚结构域IB，而双酚S是DNA的沟槽结合剂。此外，双酚S没有明显诱导牛血清白蛋白的二级结构变化，但它诱导了小牛胸腺DNA的构象变化。
