Jiangsu Provincial Key Laboratory of Coastal Wetland Bioresources and Environmental Protection, Yancheng City, Jiangsu Province, People's Republic of China.
Spectrochim Acta A Mol Biomol Spectrosc. 2010 Mar;75(3):1130-7. doi: 10.1016/j.saa.2009.12.071. Epub 2010 Jan 6.
The interaction between bisphenol A (BPA) and lysozyme (or trypsin) was investigated by UV-vis absorption, fluorescence, synchronous fluorescence, and three-dimensional fluorescence spectra techniques under physiological pH 7.40. BPA effectively quenched the intrinsic fluorescence of lysozyme and trypsin via static quenching. H-bonds and van der Waals interactions played a major role in stabilizing the BPA-proteinase complex. The distance r between donor and acceptor was obtained to be 1.65 and 2.26 nm for BPA-lysozyme and BPA-trypsin complexes, respectively. The effect of BPA on the conformation of lysozyme and trypsin was analyzed using synchronous fluorescence and three-dimensional fluorescence spectra.
在生理 pH 值 7.40 下，通过紫外可见吸收光谱、荧光光谱、同步荧光光谱和三维荧光光谱技术研究了双酚 A（BPA）与溶菌酶（或胰蛋白酶）之间的相互作用。BPA 通过静态猝灭有效地猝灭了溶菌酶和胰蛋白酶的固有荧光。氢键和范德华相互作用在稳定 BPA-蛋白酶复合物中起主要作用。对于 BPA-溶菌酶和 BPA-胰蛋白酶复合物，供体和受体之间的距离 r 分别为 1.65nm 和 2.26nm。通过同步荧光光谱和三维荧光光谱分析了 BPA 对溶菌酶和胰蛋白酶构象的影响。
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