Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white
| Autor: | Miloš Milčić, Marina Atanaskovic-Markovic, Danijela Apostolovic, Miljan Simonović, Ivan Stambolic, Jana Ognjenovic, Jelena Vesic, Tanja Cirkovic Velickovic, Marija Stojadinovic |
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| Rok vydání: | 2014 |
| Předmět: |
Protein Conformation
Ovalbumin Antigen-Presenting Cells Fluorophore quenching Immunoglobulin E medicine.disease_cause Catechin Monocytes Analytical Chemistry chemistry.chemical_compound Allergen Egg White Food allergy medicine Humans IgE binding Tea biology Chemistry Circular Dichroism Degranulation Polyphenols food and beverages General Medicine Allergens respiratory system medicine.disease Basophils Spectrometry Fluorescence Biochemistry Molecular docking biology.protein Electrophoresis Polyacrylamide Gel Epigallo-catechin 3-gallate sense organs Food Hypersensitivity Ex vivo Protein Binding Food Science Egg white |
| Zdroj: | Food Chemistry |
| ISSN: | 0308-8146 |
| DOI: | 10.1016/j.foodchem.2014.05.005 |
| Popis: | Polyphenols, the potent plant secondary metabolites, have beneficial effects on human health, but the mechanism(s) by which these effects are exerted is not well understood. Here, we present the detailed analysis of the interactions between the major green tea catechin, epigallo-catechin 3-gallate (EGCG), and the major dietary protein and allergen, ovalbumin (OVA). We show that EGCG binds to the pocket that partly overlaps with the previously identified IgE-binding region in OVA, and that this interaction induces structural changes in the allergen. Moreover, our ex vivo studies reveal that OVA binds IgE and stimulates degranulation of basophils, and that its uptake by monocytes proceeds at a slower rate in the presence of EGCG. This study provides further evidence in support of the proposed mechanism by which EGCG interactions with the food allergens contribute to its diverse biological activities and may impair antigen uptake by antigen-presenting cells. (C) 2014 Elsevier Ltd. All rights reserved. |
| Databáze: | OpenAIRE |
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