@article{plundrich_cook_maleki_fourches_lila_2019, title={Binding of peanut allergen Ara h 2 with Vaccinium fruit polyphenols}, volume={284}, ISSN={["1873-7072"]}, DOI={10.1016/j.foodchem.2019.01.081}, abstractNote={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.}, journal={FOOD CHEMISTRY}, author={Plundrich, Nathalie J. and Cook, Bethany T. and Maleki, Soheila J. and Fourches, Denis and Lila, Mary Ann}, year={2019}, month={Jun}, pages={287–295} }
 @article{bansode_randolph_plundrich_lila_williams_2019, title={Peanut protein-polyphenol aggregate complexation suppresses allergic sensitization to peanut by reducing peanut-specific IgE in C3H/HeJ mice}, volume={299}, ISSN={["1873-7072"]}, DOI={10.1016/j.foodchem.2019.125025}, abstractNote={Peanut allergy is usually lifelong and accidental exposure impose formidable risk. The aim of this study was to assess the capacity of peanut proteins complexed to polyphenol extracts to reduce allergic response in C3H/HeJ mice. Mice were sensitized to peanut flour followed by exposure to amino acid diets fortified with peanut protein-polyphenol aggregates of either with low (15%; w/w) or high (40%; w/w) complexation ratios of blueberry (BB-Low and BB-High) and cranberry (CB-Low and CB-High) extracts. Treatment groups on diets with high complexation ratios of blueberry and cranberry aggregates showed significant reduction in peanut specific plasma Immunoglobulin E (IgE). Western blot analysis of spleen lysates showed CD63 protein expression was reduced in a dose-dependent manner in blueberry and cranberry complexed peanut protein supplemented diet groups. Our results demonstrate for the first time that complexation of polyphenols to peanut flour can potentially lower plasma IgE of peanut-sensitized C3H/HeJ mice.}, journal={FOOD CHEMISTRY}, author={Bansode, Rishipal R. and Randolph, Priscilla D. and Plundrich, Nathalie J. and Lila, Mary Ann and Williams, Leonard L.}, year={2019}, month={Nov} }
 @article{plundrich_bansode_williams_lila_2017, title={In vitro Hypoallergenicity of Peanut Protein-Blueberry Polyphenol Aggregate Particles}, volume={139}, ISSN={["1097-6825"]}, DOI={10.1016/j.jaci.2016.12.455}, abstractNote={The effector phase of the peanut (PN) allergic reaction involves crosslinking of PN allergen epitopes with PN-specific IgE located on mast cell and basophil surfaces causing them to degranulate and to release inflammatory compounds. Plant-derived polyphenolic compounds are able to bind to proteins. In this study, stable aggregate particles comprised of PN proteins and blueberry pomace polyphenols were investigated for their allergen response potential by binding to IgE in vitro. Peanut protein-blueberry pomace polyphenol aggregate particles were created by complexing lowbush blueberry (Vaccinium angustifolium) pomace 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 markers of degranulation (β-hexosaminidase and histamine). IgE binding capacity to PN proteins in aggregate particles was significantly decreased (p<0.05) in the 15, 30 and 40% polyphenol samples by 21, 30 and 31% compared to uncomplexed PN proteins, respectively. 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. Aggregate particles with lower %polyphenol concentrations appeared to mitigate Ionomycin induced-degranulation. Results suggest the modification of PN proteins with blueberry pomace polyphenols led to the formation of aggregate particles with reduced allergenic potential. Future trials are warranted to investigate the immunomodulatory mechanisms of the aggregate particles.}, number={2}, journal={JOURNAL OF ALLERGY AND CLINICAL IMMUNOLOGY}, author={Plundrich, Nathalie and Bansode, Rishipal and Williams, Leonard and Lila, Mary Ann}, year={2017}, month={Feb}, pages={AB139–AB139} }
 @article{plundrich_bansode_williams_lila_2017, title={In vitro hypoallergenic potential of peanut protein-polyphenol aggregate particles}, volume={31}, journal={FASEB Journal}, author={Plundrich, N. J. and Bansode, R. R. and Williams, L. L. and Lila, M. A.}, year={2017} }
 @article{plundrich_bansode_foegeding_williams_lila_2017, title={Protein-bound Vaccinium fruit polyphenols decrease IgE binding to peanut allergens and RBL-2H3 mast cell degranulation in vitro}, volume={8}, ISSN={["2042-650X"]}, DOI={10.1039/c7fo00249a}, abstractNote={Peanut allergy is a worldwide health concern.}, number={4}, journal={FOOD & FUNCTION}, author={Plundrich, Nathalie J. and Bansode, Rishipal R. and Foegeding, E. Allen and Williams, Leonard L. and Lila, Mary Ann}, year={2017}, month={Apr}, pages={1611–1621} }
 @article{foegeding_plundrich_schneider_campbell_lila_2017, title={Protein-polyphenol particles for delivering structural and health functionality}, volume={72}, ISSN={["1873-7137"]}, DOI={10.1016/j.foodhyd.2017.05.024}, abstractNote={Dietary proteins and polyphenols contribute both nutritive and extra-nutritional (disease-preventing and metabolism-enhancing) benefits, and can participate in food structure formation and stabilization. There is a desire to increase consumption of proteins and polyphenols based on health considerations, and one approach is to form protein-polyphenol particles that combine both health and structural functionality in food products. The roles of proteins and polyphenols individually, or when bound together, are discussed in terms of health benefits (nutrition, disease prevention, satiety, allergy alleviation) and impact on food structure. The overall goal should be a rational design of protein-polyphenol particles to ensure a positive contribution to food quality, protein nutrition, and delivery of a health-relevant dose of polyphenols to the gastrointestinal tract.}, journal={FOOD HYDROCOLLOIDS}, author={Foegeding, E. Allen and Plundrich, Nathalie and Schneider, Margaret and Campbell, Caroline and Lila, Mary Ann}, year={2017}, month={Nov}, pages={163–173} }
 @article{graf_cheng_esposito_shertel_poulev_plundrich_itenberg_dayan_lila_raskin_2015, title={Compounds leached from quinoa seeds inhibit matrix metalloproteinase activity and intracellular reactive oxygen species}, volume={37}, ISSN={["1468-2494"]}, DOI={10.1111/ics.12185}, abstractNote={Synopsis}, number={2}, journal={INTERNATIONAL JOURNAL OF COSMETIC SCIENCE}, author={Graf, B. L. and Cheng, D. M. and Esposito, D. and Shertel, T. and Poulev, A. and Plundrich, N. and Itenberg, D. and Dayan, N. and Lila, M. A. and Raskin, I.}, year={2015}, month={Apr}, pages={212–221} }
 @article{plundrich_white_dean_davis_foegeding_lila_2015, title={Stability and immunogenicity of hypoallergenic peanut protein-polyphenol complexes during in vitro pepsin digestion}, volume={6}, ISSN={["2042-650X"]}, DOI={10.1039/c5fo00162e}, abstractNote={Allergenic peanut proteins are relatively resistant to digestion, and if digested, metabolized peptides tend to remain large and immunoreactive, triggering allergic reactions in sensitive individuals.}, number={7}, journal={FOOD & FUNCTION}, author={Plundrich, Nathalie J. and White, Brittany L. and Dean, Lisa L. and Davis, Jack P. and Foegeding, E. Allen and Lila, Mary Ann}, year={2015}, pages={2145–2154} }
 @article{plundrich_kulis_white_grace_guo_burks_davis_lila_2014, title={Novel Strategy To Create Hypoallergenic Peanut Protein-Polyphenol Edible Matrices for Oral Immunotherapy}, volume={62}, ISSN={["1520-5118"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-84905588654&partnerID=MN8TOARS}, DOI={10.1021/jf405773b}, abstractNote={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.}, number={29}, journal={JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY}, author={Plundrich, Nathalie J. and Kulis, Mike and White, Brittany L. and Grace, Mary H. and Guo, Rishu and Burks, A. Wesley and Davis, Jack P. and Lila, Mary Ann}, year={2014}, month={Jul}, pages={7010–7021} }
 @article{plundrich_grace_raskin_lila_2013, title={Bioactive polyphenols from muscadine grape and blackcurrant stably concentrated onto protein-rich matrices for topical applications}, volume={35}, ISSN={["1468-2494"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-84880133164&partnerID=MN8TOARS}, DOI={10.1111/ics.12057}, abstractNote={Synopsis}, number={4}, journal={INTERNATIONAL JOURNAL OF COSMETIC SCIENCE}, author={Plundrich, N. and Grace, M. H. and Raskin, I. and Lila, M. Ann}, year={2013}, month={Aug}, pages={394–401} }
 @article{roopchand_grace_kuhn_cheng_plundrich_poulev_howell_fridlender_lila_raskin_et al._2012, title={Efficient sorption of polyphenols to soybean flour enables natural fortification of foods}, volume={131}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-81855221898&partnerID=MN8TOARS}, DOI={10.1016/j.foodchem.2011.09.103}, abstractNote={The present study demonstrated that defatted soybean flour (DSF) can sorb polyphenols from blueberry and cranberry juices while separating them from sugars. Depending on DSF concentration and juice dilution, the concentration of blueberry anthocyanins and total polyphenols sorbed to DSF ranged from 2–22 mg/g and 10–95 mg/g, respectively while the concentration of anthocyanins and proanthocyanidins in cranberry polyphenol-enriched DSF ranged from 2.5–17 mg/g and 21–101 mg/g, respectively. Blueberry polyphenols present in one serving of fresh blueberries (73 g) were delivered in just 1.4 g of blueberry polyphenol-enriched DSF. Similarly, one gram of cranberry polyphenol-enriched DSF delivered the amount of proanthocyanidins available in three 240 ml servings of cranberry juice cocktail. The concentration of blueberry anthocyanins and total polyphenols eluted from DSF remained constant after 22 weeks of incubation at 37 °C, demonstrating the high stability of the polyphenol–DSF matrix. LC–MS analysis of eluates confirmed that DSF retained major cranberry and blueberry polyphenols intact. Blueberry polyphenol-enriched DSF exhibited significant hypoglycaemic activities in C57bl/6J mice, and cranberry polyphenol-enriched DSF showed antimicrobial and anti-UTI activities in vitro, confirming its efficacy. The described sorption process provides a means to create protein-rich food ingredients containing concentrated plant bioactives without excess sugars, fats and water that can be incorporated in a variety of scientifically validated functional foods and dietary supplements.}, number={4}, journal={Food Chemistry}, author={Roopchand, D.E. and Grace, M.H. and Kuhn, P. and Cheng, D.M. and Plundrich, N. and Poulev, A. and Howell, A. and Fridlender, B. and Lila, M.A. and Raskin, I. and et al.}, year={2012}, pages={1193–1200} }