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Study on the binding of chlorogenic acid to pepsin by spectral and molecular docking
Author(s) -
Zeng Huajin,
Liang Huili,
You Jing,
Qu Lingbo
Publication year - 2014
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.2610
Subject(s) - chemistry , pepsin , binding constant , quenching (fluorescence) , fluorescence , van der waals force , hydrogen bond , fluorescence spectroscopy , chlorogenic acid , docking (animal) , binding site , chromatography , molecule , enzyme , biochemistry , organic chemistry , medicine , physics , nursing , quantum mechanics
The interaction of pepsin with chlorogenic acid (CHA) was investigated using fluorescence, UV/vis spectroscopy and molecular modeling methods. Stern–Volmer analysis indicated that the fluorescence quenching of pepsin by CHA resulted from a static mechanism, and the binding constant was 1.1846 × 10 5 and 1.1587 × 10 5 L/mol at 288 and 310 K, respectively. The distance between donor (pepsin) and acceptor (CHA) was calculated to be 2.39 nm and the number of binding sites for CHA binding on pepsin was ~ 1. The results of synchronous fluorescence and three‐dimensional fluorescence showed that binding of CHA to pepsin could induce conformational changes in pepsin. Molecular docking experiments found that CHA bonded with pepsin in the area of the hydrophobic cavity with Van der Waals' forces or hydrogen bonding interaction, which were consistent with the results obtained from the thermodynamic parameter analysis. Furthermore, the binding of CHA can inhibit pepsin activity in vitro. Copyright © 2013 John Wiley & Sons, Ltd.