Journal
FOOD CHEMISTRY
Volume 135, Issue 4, Pages 2418-2424Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2012.06.114
Keywords
Phenolic acids; Flavones; Catechines; Molecular docking; Fluorescence emission spectrometry; Bovine serum albumin
Funding
- Slovenian Research Agency [P4-0121]
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Polyphenols are responsible for the major organoleptic characteristics of plant-derived foods and beverages. Here, we investigated the binding of several polyphenols to bovine serum albumin (BSA) at pH 7.5 and 25 degrees C: catechins [(-)-epigallocatechin-3-gallate, (-)-epigallocatechin, (-)-epicatechin-3-gallate], flavones (kaempferol, kaempferol-3-glucoside, quercetin, naringenin) and hydroxycinnamic acids (rosmarinic acid, caffeic acid, p-coumaric acid). Fluorescence emission spectrometry and molecular docking were applied to compare experimentally determined binding parameters with molecular modelling. Among these polyphenols, (-)-epicatechin-3-gallate showed the highest Stern-Volmer modified quenching constant, followed by (-)-epigallocatechin-3-gallate. Similarly, (-)-epicatechin-3-gallate had the highest effect on the Circular Dichroic spectrum of BSA, while the changes induced by other polyphenols were negligible. Molecular docking predicted high binding energies for (-)-epicatechin-3-gallate and (-)-epigallocatechin-3-gallate for the binding site on BSA near Trp213. Our data reveal that the polyphenol structures significantly affect the binding process: the binding affinity generally decreases with glycosylation and reduced numbers of hydroxyl groups on the second aromatic ring. (C) 2012 Elsevier Ltd. All rights reserved.
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