4.7 Article

Novel Strategy To Create Hypoallergenic Peanut Protein-Polyphenol Edible Matrices for Oral Immunotherapy

Journal

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 62, Issue 29, Pages 7010-7021

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/jf405773b

Keywords

basophil; cranberry; mouse model; peanut allergy; polyphenols

Funding

  1. Everett W. Byrd Endowment
  2. NC State appropriations for North Carolina State University at Kannapolis

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Peanut allergy is an IgE-mediated hypersensitivity. Upon peanut consumption by an allergic individual, epitopes on peanut proteins bind and cross-link peanut-specific IgE on mast cell and basophil surfaces triggering the cells to release inflammatory mediators responsible for allergic reactions. Polyphenolic phytochemicals have high affinity to bind proteins and form soluble and insoluble complexes with unique functionality. This study investigated the allergenicity of polyphenol-fortified peanut matrices prepared by complexing various polyphenol-rich plant juices and extracts with peanut flour. Polyphenol-fortified peanut matrices reduced IgE binding to one or more peanut allergens (Ara h 1, Ara h 2, Ara h 3, and Ara h 6). Attenuated total reflectance-Fourier transform infrared spectroscopy (ATR-FTIR) suggested changes in secondary protein structure. Peanut protein-cranberry polyphenol fortified matrices triggered significantly less basophil degranulation than unmodified flour in an ex vivo assay using human blood and less mast cell degranulation when used to orally challenge peanut-allergic mice. Polyphenol fortification of peanut flour resulted in a hypoallergenic matrix with reduced IgE binding and degranulation capacity, likely due to changes in protein secondary structure or masking of epitopes, suggesting potential applications for oral immunotherapy.

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