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
收藏
页码：236 / 243
页数：7
相关论文
共 29 条
  • [1] Wang W., Zhu X.M., Wang C.M., Et al., Pharmacokinetics and pharmacodynamics of oral and intravenous cefetamet in dog, Eur. J. Drug Metab. Pharmacok., 40, 4, pp. 401-407, (2015)
  • [2] Noh K., Kim E., Kang W., Quantitative determination of cefetamet in human plasma by liquid chromatography-mass spectrometry, Biomed. Chromatog., 25, 7, pp. 779-782, (2011)
  • [3] Aszmann O.C., The life and work of theodore schwann, J. Reconstrut. Microsurg., 16, 4, pp. 291-295, (2000)
  • [4] Gole A., Dash C., Rao M., Et al., Encapsulation and biocatalytic activity of the enzyme pepsin in fatty lipid films by selective electrostatic interactions, Chem. Commun., 16, 4, pp. 297-298, (2000)
  • [5] Wang Y.R., Fang Q., Guo C.H., Et al., Probing the binding of torasemide to pepsin and trypsin by spectroscopic and molecular docking methods, Spectrosc. Spect. Anal., 36, 10, pp. 3414-3421, (2016)
  • [6] Lian S.Q., Yang D.Z., Zheng X.X., Et al., Study on interaction of gatifloxacin with pepsin by fluorospectrophotometry, PTCA (Part B: Chem. Anal.), 49, 3, pp. 253-255, (2013)
  • [7] Wang Q., He J.W., Yan J., Et al., Spectroscopy and docking simulations of the interaction between lochnericine and bovine serum albumin, Luminescence, 30, 2, pp. 240-246, (2015)
  • [8] Wang G.K., Yan C.L., Lu X.M., Et al., Study on the interaction of ciprofloxacin hydrochloride with trypsin by spectroscopic and molecular modeling methods, Acta Chim. Sinica, 67, 17, pp. 1967-1972, (2009)
  • [9] Zhu S.Z., Liu Y., Spectroscopic analyses on interaction of naphazoline hydrochloride with bovine serum albumin, Spectrochim. Acta A, 98, pp. 142-147, (2012)
  • [10] Liu Y.Y., Zhang G.W., Liao Y.J., Et al., Binding characteristics of psoralen with trypsin: Insights from spectroscopic and molecular modeling studies, Spectrochim. Acta A, 151, pp. 498-505, (2015)
123