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Insights into the binding of ferulic acid to the thermally treated xanthine oxidase
Author(s) -
Dumitrascu Loredana,
Stănciuc Nicoleta,
Bahrim Gabriela Elena,
Aprodu Iuliana
Publication year - 2016
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.3099
Subject(s) - chemistry , hydrogen bond , van der waals force , ferulic acid , autodock , quenching (fluorescence) , xanthine oxidase , binding constant , binding site , molecule , docking (animal) , fluorescence spectroscopy , fluorescence , binding energy , hydrophobic effect , enthalpy , active site , stereochemistry , in silico , organic chemistry , biochemistry , enzyme , thermodynamics , medicine , physics , nursing , quantum mechanics , nuclear physics , gene
Ferulic acid (FA) is a biologically active compound used as an additive in the food industry, and possesses a wide range of therapeutic effects for treating different health problems. The interaction between FA and bovine xanthine oxidase (XOD) has been investigated by means of fluorescence spectroscopy methods. The numbers of binding sites and the binding constants were estimated at various temperatures and the results indicated the existence of one specific FA binding site of XOD. Detailed information on the interaction between molecules gathered after performing in silico molecular docking indicated the accommodation of the FA molecule in a XOD binding pocket, in close vicinity to the active site residues. The formation of the XOD–FA complex causes the quenching of protein fluorescence. The process followed a static mechanism at lower temperatures, and a dynamic mechanism at higher temperatures. The thermodynamic parameters calculated on the basis of different temperatures revealed that the association between FA and XOD is a spontaneous process driven by enthalpy and dominated by hydrogen bonding and van der Waals interaction. The results of synchronous fluorescence and 3D fluorescence spectra showed that the conformation of protein was altered in the presence of FA. Copyright © 2016 John Wiley & Sons, Ltd.