Study of Interaction Between Cefetamet Pivoxil and Pepsin by Spectroscopic and Molecular Docking

被引：0

作者：

Liu B.-S. ^{[1
]}

Wang J.-J. ^{[1
]}

Chen L. ^{[1
]}

Li Z.-Y. ^{[1
]}

Ma L.-H. ^{[1
]}

Wang C.-D. ^{[1
]}

机构：

[1] National Chemistry Experimental Teaching Demonstration Center, College of Chemistry & Environmental Science, Hebei University, Baoding

来源：

Faguang Xuebao/Chinese Journal of Luminescence | 2018年 / 39卷 / 02期

基金：

中国国家自然科学基金;

关键词：

Cefetamet pivoxil; Interaction; Molecular docking; Pepsin; Spectroscopy;

D O I：

10.3788/fgxb20183902.0236

中图分类号：

学科分类号：

摘要：

The interaction of cefetamet pivoxil (CFP) and pepsin (PEP) has been investigated by fluorescence spectra, synchronous fluorescence spectra, UV-Vis absorption spectra, circular dichroism (CD) spectra and molecular docking method at 298, 303 and 310 K. The results indicate that CFP mainly uses the static quenching method of nonradiative energy transfer to cause the fluorescence quenching of PEP, which is mainly combined by static electricity forces. The binding rate is 74.73%-92.13% at 310 K. The effect of CFP on PEP structure was studied by synchronous and circular dichroism (CD). The results show that the binding of CFP and PEP induces the conformational change of PEP, and quenches the endogenous fluorescence in PEP. The results of molecular docking reveal that CFP locates in the catalytic active site of PEP, and the results of docking are consistent with that of experimental calculation. It is confirmed that the addition of CFP leads to the gradual quenching of PEP fluorescence. The fluorescence quenching reaction of CFP to PEP can be used to determine the content of CFP in the medicine. © 2018, Science Press. All right reserved.

引用

页码：236 / 243

页数：7

共 29 条

[21] Zeng H.J., Liang H.L., You J., Et al., Study on the binding of chlorogenic acid to pepsin by spectral and molecular docking, Luminescence, 29, 7, pp. 715-721, (2014)
[22] Kaboudin B., Moradi K., Faghihi M.R., Et al., The fluorescence spectroscopic studies on the interaction of novel aminophosphinic acids with bovine serum albumin, J. Lumin., 139, 7, pp. 104-112, (2013)
[23] Zhao X.C., Liu R.T., Teng Y., Et al., The interaction between Ag<sup>+</sup> and bovine serum albumin: a spectroscopic investigation, Sci. Total Environ., 409, 5, pp. 892-897, (2011)
[24] Li Z., Li Z.G., Yang L.L., Et al., investigation of the binding between pepsin and nucleoside analogs by spectroscopy and molecular simulation, J. Fluoresc., 25, 2, pp. 451-463, (2015)
[25] Shen L.L., Xu H., Huang F.W., Et al., Investigation on interaction between ligupurpuroside A and pepsin by spectroscopic and docking methods, Spectrochim. Acta A, 135, 7, pp. 256-263, (2015)
[26] Matsui H., Okuda T., Penetration of cefpiramide and cefazolin into peritoneal capsular fluid in rabbits, Antimicrob. Agents. Chemother., 32, 1, pp. 33-36, (1988)
[27] Jia Y., Yang H.Q., Guo L.Q., Et al., Investigation of interaction between cefixime and pepsin by spectroscopic methods, Chem. Res. App., 28, 5, pp. 673-680, (2016)
[28] Zeng H.J., Li M.T., Li Q., Et al., Mechanism of interaction between levofloxacin and pepsin by spectroscopic and molecular docking methods, Chin. J. Lumin., 37, 4, pp. 481-486, (2016)
[29] Zhang H.M., Cao J., Fei Z.H., Et al., Investigation on the interaction behavior between bisphenol A and pepsin by spectral and docking studies, J. Mol. Struct., 1021, 4, pp. 34-39, (2012)

← 1 2 3 →