Fluorescence spectroscopic analysis on interaction of fleroxacin with pepsin
Fluorescence spectroscopic analysis on interaction of fleroxacin with pepsin
复制标题
氟罗沙星与胃蛋白酶相互作用的荧光光谱分析。
DOI：
10.1002/bio.2469
复制
发表时间：
2013-11-01
期刊：
影响因子：
2.9
通讯作者：
Yang, Dongzhi
中科院分区：
文献类型：
--
作者：
Lian, Shuqin;Wang, Guirong;Yang, Dongzhi
用荧光光谱法研究了氟罗沙星（FLX）与胃蛋白酶的相互作用。基于荧光猝灭和同步荧光光谱结合三维荧光光谱研究FLX对胃蛋白酶的影响，结果表明FLX改变了胃蛋白酶色氨酸残基的微环境和分子构象。结果表明，FLX对胃蛋白酶的荧光猝灭与形成新的复合物和非辐射能量转移有关。计算了不同温度下的猝灭常数KSV、结合常数K和结合位点数n。根据Forster非辐射能量转移机理计算了胃蛋白酶与FLX的分子间相互作用距离（r = 6.71）和能量转移效率（E = 0.216）。疏水和静电相互作用在FLX-胃蛋白酶缔合中起主要作用。此外，通过分子模拟研究，进一步测试了疏水相互作用和结合自由能。
The interaction between fleroxacin (FLX) and pepsin was investigated by spectrofluorimetry. The effects of FLX on pepsin showed that the microenvironment of tryptophan residues and molecular conformation of pepsin were changed based on fluorescence quenching and synchronous fluorescence spectroscopy in combination with three-dimensional fluorescence spectroscopy. Static quenching was suggested and it was proved that the fluorescence quenching of pepsin by FLX was related to the formation of a new complex and a non-radiation energy transfer. The quenching constants KSV , binding constants K and binding sites n were calculated at different temperatures. The molecular interaction distance (r = 6.71) and energy transfer efficiency (E = 0.216) between pepsin and FLX were obtained according to the Forster mechanism of non-radiation energy transfer. Hydrophobic and electrostatic interaction played a major role in FLX-pepsin association. In addition, the hydrophobic interaction and binding free energy were further tested by molecular modeling study.