Shandong Key Laboratory of Water Pollution Control and Resource Reuse, School of Environmental Science and Engineering, Shandong University, Shandong Province, Jinan, PR China.
Spectrochim Acta A Mol Biomol Spectrosc. 2011 Dec;83(1):130-5. doi: 10.1016/j.saa.2011.07.092. Epub 2011 Aug 10.
The toxicity of sodium benzoate to trypsin was investigated by fluorescence spectroscopy, synchronous fluorescence spectroscopy, UV-visible absorption spectroscopy and circular dichroism (CD) spectroscopy under mimic physiological conditions. Sodium benzoate could unfold trypsin by decreasing the β-sheet structure, which leads to more exposure of internal amino acid groups and the obvious intrinsic fluorescence quenching with the rising concentration of sodium benzoate. The results of spectroscopic measurements indicated that sodium benzoate changed the internal microenvironment of trypsin and induced the alteration of the whole molecule, which were performed toxic effects on the organism. Trypsin and sodium benzoate interacted with each other to produce a substance by van der Waals forces and hydrogen bond, the model of which was shown by AutoDock software.
在模拟生理条件下，采用荧光光谱法、同步荧光光谱法、紫外-可见吸收光谱法和圆二色性（CD）光谱法研究了苯甲酸钠对胰蛋白酶的毒性。苯甲酸钠通过降低β-折叠结构使胰蛋白酶变性，导致内部氨基酸基团更多地暴露，随着苯甲酸钠浓度的升高，固有荧光明显猝灭。光谱测量结果表明，苯甲酸钠改变了胰蛋白酶的内部微环境，诱导整个分子发生变化，从而对生物体产生毒性作用。胰蛋白酶和苯甲酸钠通过范德华力和氢键相互作用生成一种物质，该模型由 AutoDock 软件显示。
