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ARS Home » Southeast Area » New Orleans, Louisiana » Southern Regional Research Center » Food Processing and Sensory Quality Research » Research » Publications at this Location » Publication #364457
Research Project: Reducing Peanut and Tree Nut Allergy

Location: Food Processing and Sensory Quality Research

Title: Binding of peanut allergen Ara h 2 with Vaccinium fruit polyphenols

Author
item PLUNDRICH, NATHALIE - North Carolina State University
item COOK, BETHANY - North Carolina State University
item Maleki, Soheila
item FOURCHES, DENIS - North Carolina State University
item LILA, MARY - North Carolina State University

Submitted to: Journal of Food Chemistry
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 1/8/2019
Publication Date: 1/18/2019
Citation: Plundrich, N.J., Cook, B.T., Maleki, S.J., Fourches, D., Lila, M.A. 2019. Binding of peanut allergen Ara h 2 with Vaccinium fruit polyphenols. Journal of Food Chemistry. 284:287-295.

Interpretive Summary: 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. Structure and IgE binding were assessed with the chemicals tested for binding to determined their capacity to (i) bind to Ara h 2, (ii) induce structural changes, and (iii) inhibit IgE binding sites. Spectroscopy clearly indicated that procyanidin C1 and chlorogenic acid interacted with Ara h 2, and Structural analysis 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 binding.

Technical 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.