He Wu, Dou Huanjing, Zhang Lu, Wang Lvjing, Wang Ruiyong, Chang Junbiao
College of Chemistry and Molecular Engineering, Zhengzhou University, 100 Science Avenue, Zhengzhou 450001, China.
Spectrochim Acta A Mol Biomol Spectrosc. 2014 Jan 24;118:510-9. doi: 10.1016/j.saa.2013.09.027. Epub 2013 Sep 12.
The interactions between Trypsin and Bicyclol or analogs (Bifendate, I, II and III) were investigated by spectrophotometric methods. It was found that Bicyclol or analogs had strong ability to quench the intrinsic fluorescence of Trypsin by a static quenching procedure. The binding constants were obtained at three temperatures. The thermodynamics parameters reveal that the hydrophobic and electrostatic interactions play an important role in the interaction. Results showed that the microenvironments of tryptophan residue of Trypsin were disturbed by the analogs. Results indicated that Bifendate was the strongest quencher among five compounds.
采用分光光度法研究了胰蛋白酶与双环醇及其类似物（联苯双酯、I、II和III）之间的相互作用。结果发现，双环醇及其类似物能够通过静态猝灭过程强烈猝灭胰蛋白酶的内源荧光。在三个温度下获得了结合常数。热力学参数表明，疏水作用和静电作用在该相互作用中起重要作用。结果表明，胰蛋白酶色氨酸残基的微环境受到类似物的干扰。结果表明，联苯双酯是五种化合物中最强的猝灭剂。
