Binding of peanut allergen Ara h 2 with Vaccinium fruit polyphenols

Nathalie J. Plundrich, Bethany T. Cook, Soheila J. Maleki, Denis Fourches, Mary Ann Lila

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)287-295
Number of pages9
JournalFood chemistry
Volume284
DOIs
StatePublished - Jun 30 2019

Keywords

  • Ara h 2
  • Circular dichroism (CD)
  • Food allergy
  • IgE binding
  • Molecular docking
  • Polyphenol

ASJC Scopus subject areas

  • Analytical Chemistry
  • Food Science

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