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.