The First Affiliated Hospital of Zhengzhou University, Zhengzhou 450052, China.
Spectrochim Acta A Mol Biomol Spectrosc. 2013 Nov;115:1-11. doi: 10.1016/j.saa.2013.06.025. Epub 2013 Jun 19.
The interactions between Trypsin and bifendate (DDB) or analogs (I, II and III) were investigated by fluorescence, UV-visible absorption, resonance light scattering, synchronous fluorescence and 3D spectroscopy under mimic physiological conditions. The results revealed that DDB and analogs caused the fluorescence quenching of Trypsin by the formation of DDB/I/II/III-Trypsin complex. The quenching and energy transfer mechanisms were discussed. The binding constants and thermodynamic parameters at three different temperatures were obtained. The hydrophobic interaction was the predominant intermolecular forces to stabilize the complex. Results showed that DDB was the stronger quencher and bound to Trypsin with higher affinity than other three analogs.
在模拟生理条件下，通过荧光、紫外-可见吸收、共振光散射、同步荧光和三维光谱研究了胰蛋白酶与双飞粉（DDB）或类似物（I、II 和 III）之间的相互作用。结果表明，DDB 和类似物通过形成 DDB/I/II/III-胰蛋白酶复合物导致胰蛋白酶的荧光猝灭。讨论了猝灭和能量转移机制。在三个不同温度下获得了结合常数和热力学参数。疏水相互作用是稳定配合物的主要分子间力。结果表明，DDB 是更强的猝灭剂，与胰蛋白酶的结合亲和力高于其他三种类似物。
