Binding of peanut allergen Ara h 2 with Vaccinium fruit polyphenols. (30th June 2019)

• Record Type: Journal Article
• Authors: Plundrich, Nathalie J.; Cook, Bethany T.; Maleki, Soheila J.; Fourches, Denis; Lila, Mary Ann
• Is Part Of: Food chemistry. Volume 284(2019)
• Page Start: 287
• Page End: 295
• Publication Date: 2019-06-30
• Subjects: Ara h 2 -- Molecular docking -- Polyphenol -- IgE binding -- Circular dichroism (CD) -- Food allergy; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2019.01.081
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: Polyphenol binding induced Ara h 2 secondary structural changes. Polyphenol interaction with Ara h 2 significantly decreased IgE binding capacity. Procyanidin C1, chlorogenic acid, and benzoic acid appeared to bind to Ara h 2. Abstract: The potential for 42 different polyphenols found in Vaccinium fruits to bind to peanut allergen Ara h 2 and inhibit IgE binding epitopes was investigated using cheminformatics techniques. Out of 12 predicted binders, delphinidin-3-glucoside, cyanidin-3-glucoside, procyanidin C1, and chlorogenic acid were further evaluated in vitro . Circular dichroism, UV–Vis spectroscopy, and immunoblotting determined their capacity to (i) bind to Ara h 2, (ii) induce protein secondary structural changes, and (iii) inhibit IgE binding epitopes. UV–Vis spectroscopy clearly indicated that procyanidin C1 and chlorogenic acid interacted with Ara h 2, and circular dichroism results suggested that interactions with these polyphenols resulted in changes to Ara h 2 secondary structures. Immunoblotting showed that procyanidin C1 and chlorogenic acid bound to Ara h 2 significantly decreased the IgE binding capacity by 37% and 50%, respectively. These results suggest that certain polyphenols can inhibit IgE recognition of Ara h 2 by obstructing linear IgE epitopes.