@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}, 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={Abstract 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={Quinoa (Chenopodium quinoa Willd.) is a seed crop rich in bioactive compounds including phytoecdysones (especially 20-hydroxyecdysone, 20HE), polyphenols, proteins and essential fatty acids. We previously reported a method to leach and concentrate quinoa bioactives into a complex phytochemical mixture termed quinoa leachate (QL). Here, we aimed to determine the effect of QL and its chemically distinct fractions on five biochemical endpoints relevant to skin care applications: (i) cell viability, (ii) matrix metalloproteinase (MMP) mRNA expression, (iii) MMP enzymatic activity, (iv) tyrosinase enzymatic activity and (v) intracellular reactive oxygen species (ROS) production. Quinoa leachate was fractionated and chemically characterized using column chromatography and liquid chromatography–mass spectrometry (LC-MS). Cell viability was determined using a MTT assay in four mammalian cell lines. MMP-1 mRNA expression was assessed in human dermal fibroblasts (HDF) via qRT-PCR. The enzymatic activity of MMP-9 and tyrosinase was measured using fluorometric and colorimetric in vitro assays, respectively. Lipopolysaccharide (LPS)-induced ROS production was determined in human dermal fibroblasts by fluorescence intensity of an oxidant-sensitive probe. Quinoa leachate was separated into three fractions: (i) carbohydrate-rich fraction (QL-C; 71.3% w/w of QL); (ii) phytoecdysone, polyphenol and protein-rich fraction (QL-P, 13.3% w/w of QL); (iii) oil-rich fraction (QL-O, 10.8% w/w of QL). QL did not reduce cell viability in any of the four cell lines tested. QL, QL-P and QL-O each significantly inhibited MMP-1 mRNA expression in HDF at a concentration of 5 μg mL−1. QL and QL-P also significantly inhibited MMP-9 enzymatic activity, whereas QL-P demonstrated significant tyrosinase enzymatic inhibition. Furthermore, QL, QL-P, QL-O and 20HE significantly inhibited intracellular ROS production. This study is the first to demonstrate the MMP, tyrosinase and ROS inhibiting properties of multiple different phytochemical components derived from quinoa seeds. Our work indicates that quinoa phytochemicals may play a role in the treatment and prevention of skin ageing through a multiplicity of effects. Le Quinoa (Chenopodium quinoa Willd) est une culture de semences riches en composés bioactifs, y compris les phytoecdysones (en particulier 20 hydroxecdysone, 20HE), des polyphénols, des protéines et des acides gras essentiels. Nous avons précédemment rapporté une méthode d'extraction et de concentration des composés bioactifs de quinoa dans un mélange complexe phytochimique appelé lixiviat de quinoa (QL). Ici, nous avons cherché à déterminer l'effet de QL et de ses fractions chimiquement distinctes sur cinq paramètres biochimiques pertinents pour des applications de soins de la peau: (i) la viabilité cellulaire, (ii) l'expression de l’ARNm des matrix matalloproteinases (MMP), (iii) l'activité enzymatique MMP, (iv) L'activité enzymatique de la tyrosinase, et (v) les espèces réactives de l'oxygène intracellulaire (ROS). QL a été fractionné et caractérisé chimiquement en utilisant une Chromatographie sur colonne et de spectrométrie de masse liquide (LC-MS). La viabilité cellulaire a été déterminée en utilisant un test MTT dans les quatre lignées cellulaires de mammifères. L'expression de l’ARNm MMP-1 a été évaluée dans des fibroblastes dermiques humains (HDF) par qRT-PCR. Les activités enzymatiques de la MMP-9 et de la tyrosinase ont été mesurées en utilisant des dosages colorimétriques et fluorimétriques in vitro, respectivement. La production de ROS induite par le lipopolysaccharide (LPS) a été déterminée dans les fibroblastes dermiques humains par l'intensité de fluorescence d'une sonde oxydosensible. QL a été séparé en trois fractions: (i) la fraction riche en glucides (QL-C, 71,3% p/p de QL); (ii) phytoecdysone, polyphénol, la fraction riche en protéines (QL-P, 13,3% p/p de QL); (iii) fraction riche en huile (QL-O, 10,8% p/p de QL). QL ne réduit pas la viabilité des cellules dans aucune des quatre lignées cellulaires testées. QL, QL-P et QL-O inhibent l'expression de l’ARNm de MMP-1 de manière significative dans HDF à une concentration de 5 pg mL−1. QL et QL-P inhibent également de manière significative l'activité enzymatique de la MMP-9 d'une manière dépendante de la dose, tandis que QL-P a montré une inhibition significative de la tyrosinase. En outre, QL, QL-P, QL-O, et 20HE ont inhibé significativement la production de ROS intracellulaire. Cette étude est la première à démontrer les propriétés de plusieurs différentes composantes phytochimiques provenant de graines de quinoa sur MMP, la tyrosinase, et les ROS inhibiteurs. Nos travaux indiquent que les composés phytochimiques de quinoa peuvent jouer un rôle dans le traitement et la prévention du vieillissement cutané grâce à une multiplicité d'effets. Figure S1. LC-MS chromatogram of fatty acids present in the oil-rich fraction of quinoa leachate (QL-O). Figure S2. Phytochemical constituents of quinoa leachate (QL) are stable over 8 week at 25 and 37°C. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.}, 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={Natural botanical agents that are antimicrobial, or that modulate skin hyperpigmentation via tyrosinase inhibition, are increasingly sought in the cosmetic industry.In this study, an efficient tactic is demonstrated for concentrating and stabilizing skin-beneficial bioactive compounds from muscadine grape and blackcurrant juice or muscadine pomace, into hemp flour (HF), hemp protein isolate (HPI) and soy protein isolate (SPI) matrices suitable for cosmetic applications.Anthocyanins were most efficiently captured from blackcurrant juice into HF (8.39 mg g(-1) ). HPI most effectively captured total phenolics from muscadine pomace (72.32 and 77.32 mg g(-1) from Noble and Carlos, respectively), while the three matrices incorporated highest levels of ellagic acid, gallic acid, and PAC B1 from Noble muscadine grape juice. The enriched matrices demonstrated effective in vitro inhibition of tyrosinase (up to 57.29% for blackcurrant juice-HPI matrix), and in general, juice sources provided greater inhibition on L-dopamine oxidation by tyrosinase than pomace sources. The polyphenol-enriched matrices effectively inhibited microbial proliferation in a screening assay against Staphylococcus aureus bacteria, whereas untreated HF, HPI or SPI did not inhibit bacterial growth.The technology of combining and stably concentrating phytoactive polyphenols with proteins has potential use for cosmetic topical applications.}, 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} }