Journal Articles

In vitro Hypoallergenic Potential of Peanut Protein-Polyphenol Aggregate Particles

May 11, 2017

Nathalie J. Plundrich 1, Rishipal R. Bansode 2, Leonard L. Williams 2 and Mary Ann Lila 1 (2017). In vitro Hypoallergenic Potential of Peanut Protein-Polyphenol Aggregate Particles. The FASEB Journal 31(1).

Author Affiliations

1 Plants for Human Health Institute, Department of Food, Bioprocessing and Nutrition Sciences, North Carolina State University, North Carolina Research Campus, Kannapolis, NC
2 North Carolina Agricultural and Technical State University, Center for Excellence in Post-Harvest Technologies, North Carolina Research Campus, Kannapolis, NC


The single most effective management of peanut (PN) allergy is the strict avoidance of the allergenic food. However, PN proteins are found in a variety of food products. A lot of effort has focused on mediating PN allergy either through attempted modulation of the human immune system (e.g. oral immunotherapy) or the allergenic food proteins (by processing techniques or genetic modification). In this study, we took advantage of the natural binding properties of plant-derived compounds (i.e. polyphenols) to proteins. We created stable aggregate particles comprised of PN proteins and cranberry pomace or PN skin polyphenols which were investigated for their IgE binding potential. Their capacity to modulate mast cell degranulation and cell signaling involving phosphorylation of MAPK and p-38 was investigated in vitro using RBL-2H3 cells.

PN protein-cranberry pomace and PN protein-PN skin polyphenol aggregate particles were created by complexing cranberry (Vaccinium macrocarpon Ait.) pomace or PN skin polyphenols with roasted PN flour. Particles containing 5 to 40% polyphenols were created. For the detection of PN-specific IgE binding by PN proteins, immunoblotting was performed with pooled plasma from seven PN-allergic individuals. RBL-2H3 mast cells were exposed to aggregate particles or PN flour and evaluated for their inhibitory activity on ionomycin-induced degranulation (β-hexosaminidase and histamine).

Results showed that PN protein-bound polyphenols were able to decrease the IgE binding capacity to PN proteins in aggregate particles and the highest reduction was observed in the 40% polyphenol samples, a 22% and a 38% decrease in the PN protein-PN skin and cranberry pomace polyphenol aggregate particles, respectively. This was significant when compared to IgE binding capacity of unmodified PN proteins (p<0.05; n=4 or 5). Anti-DNP IgE-sensitized RBL-2H3 cells challenged with DNP-BSA and ionomycin in the presence of aggregate particles were evaluated for their release of β-hexosaminidase and histamine. PN protein-PN skin and cranberry pomace polyphenol aggregate particles appeared to reduce ionomycin-induced β-hexosaminidase release (60 and 61%, respectively) and histamine release (64 and 66%, respectively). PN protein-PN skin and cranberry pomace polyphenol aggregate particles when exposed to ionomycin-induced RBL-2H3 cells, inhibited phosphorylation of MAPK and induced the phosphorylation of p-38 in a dose dependent manner.

Results suggest the modification of PN proteins with cranberry pomace and PN skin polyphenols led to the formation of PN protein-polyphenol aggregate particles with reduced allergenic potential. Future trials are warranted to investigate the immunomodulatory mechanisms of these aggregate particles.

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