{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,14]],"date-time":"2026-09-14T22:23:05Z","timestamp":1789424585811,"version":"build-2803163510"},"reference-count":185,"publisher":"MDPI AG","issue":"2","license":[{"start":{"date-parts":[[2021,1,8]],"date-time":"2021-01-08T00:00:00Z","timestamp":1610064000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Celiac disease is an autoimmune disorder characterized by a heightened immune response to gluten proteins in the diet, leading to gastrointestinal symptoms and mucosal damage localized to the small intestine. Despite its prevalence, the only treatment currently available for celiac disease is complete avoidance of gluten proteins in the diet. Ongoing clinical trials have focused on targeting the immune response or gluten proteins through methods such as immunosuppression, enhanced protein degradation and protein sequestration. Recent studies suggest that polyphenols may elicit protective effects within the celiac disease milieu by disrupting the enzymatic hydrolysis of gluten proteins, sequestering gluten proteins from recognition by critical receptors in pathogenesis and exerting anti-inflammatory effects on the system as a whole. This review highlights mechanisms by which polyphenols can protect against celiac disease, takes a critical look at recent works and outlines future applications for this potential treatment method.<\/jats:p>","DOI":"10.3390\/ijms22020595","type":"journal-article","created":{"date-parts":[[2021,1,10]],"date-time":"2021-01-10T19:55:56Z","timestamp":1610308556000},"page":"595","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":25,"title":["Gliadin Sequestration as a Novel Therapy for Celiac Disease: A Prospective Application for Polyphenols"],"prefix":"10.3390","volume":"22","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9613-9100","authenticated-orcid":false,"given":"Charlene B.","family":"Van Buiten","sequence":"first","affiliation":[{"name":"Department of Food Science and Human Nutrition, College of Health and Human Sciences, Colorado State University, Fort Collins, CO 80524, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8416-8772","authenticated-orcid":false,"given":"Ryan J.","family":"Elias","sequence":"additional","affiliation":[{"name":"Department of Food Science, College of Agricultural Sciences, Pennsylvania State University, University Park, PA 16802, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,1,8]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1084\/jem.191.4.603","article-title":"The intestinal T cell response to alpha-gliadin in adult celiac disease is focused on a single deamidated glutamine targeted by tissue transglutaminase","volume":"191","author":"Molberg","year":"2000","journal-title":"J. Exp. Med."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1538","DOI":"10.1038\/ajg.2012.219","article-title":"The Prevalence of Celiac Disease in the United States","volume":"107","author":"Ludvigsson","year":"2012","journal-title":"Am. J. Gastroenterol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1001\/archinte.163.3.286","article-title":"Prevalence of Celiac Disease in At-Risk and Not-At-Risk Groups in the United States","volume":"163","author":"Fasano","year":"2003","journal-title":"Arch. Intern. Med."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"282","DOI":"10.3390\/diseases3040282","article-title":"The Role of Environmental Factors in the Development of Celiac Disease: What Is New?","volume":"3","author":"Lionetti","year":"2015","journal-title":"Diseases"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1111\/j.1365-277X.2007.00763.x","article-title":"Economic burden of a gluten-free diet","volume":"20","author":"Lee","year":"2007","journal-title":"J. Hum. Nutr. Diet."},{"key":"ref_6","first-page":"12","article-title":"Non-dietary methods in the treatment of celiac disease","volume":"10","year":"2015","journal-title":"Prz. Gastroenterol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"604","DOI":"10.1111\/j.1365-2796.2011.02376.x","article-title":"Novel Therapies for Coeliac Disease","volume":"269","author":"Sollid","year":"2012","journal-title":"J. Intern. Med."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1732","DOI":"10.1021\/pr050173t","article-title":"Identification and Analysis of Multivalent Proteolytically Resistant Peptides from Gluten: Implications for Celiac Sprue","volume":"4","author":"Shan","year":"2006","journal-title":"J. Proteome Res."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1053\/j.gastro.2008.09.016","article-title":"Polymeric binders suppress gliadin-induced toxicity in the intestinal epithelium","volume":"136","author":"Pinier","year":"2009","journal-title":"Gastroenterology"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"316","DOI":"10.1053\/j.gastro.2011.10.038","article-title":"The copolymer P(HEMA-co-SS) binds gluten and reduces immune response in gluten-sensitized mice and human tissues","volume":"142","author":"Pinier","year":"2012","journal-title":"Gastroenterology"},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Van Buiten, C.B. (2017). Physicochemical Modification of Gliadin by Dietary Polyphenols and the Potential Implications for Celiac Disease. [Ph.D. Thesis, Pennsylvania State University].","DOI":"10.1096\/fasebj.31.1_supplement.974.23"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"e1700879","DOI":"10.1002\/mnfr.201700879","article-title":"Green Tea Polyphenols Mitigate Gliadin-Mediated Inflammation and Permeability in Vitro","volume":"62","author":"Lambert","year":"2018","journal-title":"Mol. Nutr. Food Res."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"2997","DOI":"10.1039\/C9FO00553F","article-title":"Physicochemical interactions with (-)-epigallocatechin-3-gallate drive structural modification of celiac-associated peptide \u03b12-gliadin (57-89) at physiological conditions","volume":"10","author":"Yennawar","year":"2019","journal-title":"Food Funct."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1080\/10408398209527350","article-title":"Chemical, biochemical and biological significance of polyphenols in cereals and legumes","volume":"17","author":"Salunkhe","year":"1983","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1080\/10408699891274273","article-title":"Tannins and Human Health: A Review","volume":"38","author":"Chung","year":"1998","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"942","DOI":"10.1111\/j.1365-2222.2010.03460.x","article-title":"Polyphenol-enriched apple extract attenuates food allergy in mice","volume":"40","author":"Zuercher","year":"2010","journal-title":"Clin. Exp. Allergy"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"7010","DOI":"10.1021\/jf405773b","article-title":"Novel strategy to create hypoallergenic peanut protein-polyphenol edible matrices for oral immunotherapy","volume":"62","author":"Plundrich","year":"2014","journal-title":"J. Agric. Food Chem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1016\/j.foodchem.2015.04.001","article-title":"Complexes of green tea polyphenol, epigalocatechin-3-gallate, and 2S albumins of peanut","volume":"185","author":"Vesic","year":"2015","journal-title":"Food Chem."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1345","DOI":"10.1016\/j.foodchem.2009.01.052","article-title":"Reducing the allergenic capacity of peanut extracts and liquid peanut butter by phenolic compounds","volume":"115","author":"Chung","year":"2009","journal-title":"Food Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"45572","DOI":"10.1074\/jbc.M207606200","article-title":"Circular dichroism and nuclear magnetic resonance spectroscopic analysis of immunogenic gluten peptides and their analogs","volume":"277","author":"Parrot","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"2275","DOI":"10.1126\/science.1074129","article-title":"Structural basis for gluten intolerance in celiac sprue","volume":"297","author":"Shan","year":"2002","journal-title":"Science"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1093\/jexbot\/53.370.947","article-title":"Cereal seed storage proteins: Structures, properties and role in grain utilization","volume":"53","author":"Shewry","year":"2002","journal-title":"J. Exp. Bot."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1098\/rstb.2001.1024","article-title":"The structure and properties of gluten: An elastic protein from wheat grain","volume":"357","author":"Shewry","year":"2002","journal-title":"Philos. Trans. R. Soc. Lond."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/bj2670001","article-title":"The prolamin storage proteins of cereal seeds: Structure and evolution","volume":"267","author":"Shewry","year":"1990","journal-title":"Biochem. J."},{"key":"ref_25","unstructured":"Fox, P., and Condon, J.J. (1982). Food Proteins, Elsevier Applied Science."},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Ortolan, F., and Steel, C.J. (2017). Protein Characteristics that Affect the Quality of Vital Wheat Gluten to be Used in Baking: A Review. Compr. Rev. Food Sci. Food Saf.","DOI":"10.1111\/1541-4337.12259"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1097\/01.meg.0000221847.09792.34","article-title":"Gliadin, glutenin or both? The search for the Holy Grail in coeliac disease","volume":"18","author":"Howdle","year":"2006","journal-title":"Eur. J. Gastroenterol. Hepatol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1111\/j.1651-2227.1996.tb14239.x","article-title":"Relation between gliadin structure and coeliac toxicity","volume":"412","author":"Wieser","year":"1996","journal-title":"Acta Paediatr. Suppl."},{"key":"ref_29","unstructured":"Berg, J.M., and Tymoczko, J.L. (2002). Section 23.1, Proteins Are Degraded to Amino Acids. Biochemistry, W. H. Freeman."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"G996","DOI":"10.1152\/ajpgi.00136.2002","article-title":"Intestinal digestive resistance of immunodominant gliadin peptides","volume":"283","author":"Hausch","year":"2002","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1088","DOI":"10.1021\/jf3045523","article-title":"Structural analysis and Caco-2 cell permeability of the celiac-toxic A-gliadin peptide 31-55","volume":"61","author":"Iacomino","year":"2013","journal-title":"J. Agric. Food Chem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1053\/j.gastro.2008.03.023","article-title":"Gliadin Induces an Increase in Intestinal Permeability and Zonulin Release by Binding to the Chemokine Receptor CXCR3","volume":"135","author":"Lammers","year":"2008","journal-title":"Gastroenterology"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1038\/mi.2008.75","article-title":"Celiac disease: From oral tolerance to intestinal inflammation, autoimmunity and lymphomagenesis","volume":"2","author":"Meresse","year":"2009","journal-title":"Mucosal Immunol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1152\/physrev.00003.2008","article-title":"Zonulin and Its Regulation of Intestinal Barrier Function: The Biological Door to Inflammation, Autoimmunity, and Cancer","volume":"91","author":"Fasano","year":"2011","journal-title":"Physiol. Rev."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1084\/jem.20071204","article-title":"Secretory IgA mediates retrotranscytosis of intact gliadin peptides via the transferrin receptor in celiac disease","volume":"205","author":"Moura","year":"2008","journal-title":"J. Exp. Med."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1136\/gut.2007.136366","article-title":"Mechanisms of epithelial translocation of the \u03b12-gliadin-33mer in celiac sprue","volume":"57","author":"Schumann","year":"2008","journal-title":"Gut"},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Fasano, A. (2012). Novel therapeutic\/integrative approaches for celiac disease and dermatitis herpetiformis. Clin. Dev. Immunol.","DOI":"10.1155\/2012\/959061"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1186\/ar1202","article-title":"Targeting the interleukin-15\/interleukin-15 receptor system in inflammatory autoimmune diseases","volume":"6","author":"Waldmann","year":"2004","journal-title":"Arthritis Res. Ther."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1111\/imr.12191","article-title":"IL-15: A central regulator of celiac disease immunopathology","volume":"260","author":"Abadie","year":"2014","journal-title":"Immunol. Rev."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"408","DOI":"10.1111\/j.1365-2249.2005.02783.x","article-title":"The immune recognition of gluten in coeliac disease","volume":"140","author":"Ciccocioppo","year":"2005","journal-title":"Clin. Exp. Immunol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"994","DOI":"10.1053\/j.gastro.2006.12.025","article-title":"Inhibition of TGF-beta Signaling by IL-15: A New Role for IL-15 in the Loss of Immune Homeostasis in Celiac Disease","volume":"132","author":"Benahmed","year":"2007","journal-title":"Gastroenterology"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"2512","DOI":"10.4049\/jimmunol.176.4.2512","article-title":"Gliadin Stimulation of Murine Macrophage Inflammatory Gene Expression and Intestinal Permeability Are MyD88-Dependent: Role of the Innate Immune Response in Celiac Disease","volume":"176","author":"Thomas","year":"2006","journal-title":"J. Immunol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1111\/j.1749-6632.2009.04037.x","article-title":"Tight Junctions, Intestinal Permeability and Autoimmunity Celiac Disease and Type 1 Diabetes Paradigms","volume":"1165","author":"Visser","year":"2010","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1038\/nrgastro.2012.221","article-title":"The digestive neuronal-glial-epithelial unit: A new actor in gut health and disease","volume":"10","author":"Neunlist","year":"2013","journal-title":"Nat. Rev. Gastroenterol. Hepatol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"4851","DOI":"10.1016\/j.febslet.2005.07.066","article-title":"Rapid disruption of intestinal barrier function by gliadin involves altered expression of apical junctional proteins","volume":"579","author":"Sander","year":"2005","journal-title":"FEBS Lett."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1136\/gut.52.2.218","article-title":"Early effects of gliadin on enterocyte intracellular signalling involved in intestinal barrier function","volume":"52","author":"Clemente","year":"2003","journal-title":"Gut"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1042\/cs0680573","article-title":"Human jejunal transglutaminase: Demonstration of activity, enzyme kinetics and substrate specificity with special relation to gliadin and coeliac disease","volume":"68","author":"Bruce","year":"1985","journal-title":"Clin. Sci."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"2917","DOI":"10.1007\/s10620-008-0450-4","article-title":"Deamidation of gliadin peptides in lamina propria: Implications for celiac disease","volume":"53","author":"Skovbjerg","year":"2008","journal-title":"Dig. Dis. Sci."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"788","DOI":"10.1053\/j.gastro.2020.04.018","article-title":"Evidence That Pathogenic Transglutaminase 2 in Celiac Disease Derives From Enterocytes","volume":"159","author":"Iversen","year":"2020","journal-title":"Gastroenterology"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"e20190860","DOI":"10.1084\/jem.20190860","article-title":"B cell tolerance and antibody production to the celiac disease autoantigen transglutaminase 2","volume":"217","author":"Blazevski","year":"2020","journal-title":"J. Exp. Med."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"746","DOI":"10.1016\/j.autrev.2012.01.007","article-title":"The function of tissue transglutaminase in celiac disease","volume":"11","author":"Vanoli","year":"2012","journal-title":"Autoimmun. Rev."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"1757","DOI":"10.4049\/jimmunol.173.3.1757","article-title":"Antigen presentation to celiac lesion-derived T cells of a 33-mer gliadin peptide naturally formed by gastrointestinal digestion","volume":"173","author":"Qiao","year":"2004","journal-title":"J. Immunol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1038\/364033a0","article-title":"Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1","volume":"364","author":"Brown","year":"1993","journal-title":"Nature"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1038\/368215a0","article-title":"Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide","volume":"368","author":"Stern","year":"1994","journal-title":"Nature"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/j.coi.2009.03.004","article-title":"Antigen presentation in celiac disease","volume":"21","author":"Qiao","year":"2009","journal-title":"Curr. Opin. Immunol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"7349","DOI":"10.3748\/wjg.v21.i24.7349","article-title":"Effector and suppressor T cells in celiac disease","volume":"21","author":"Mazzarella","year":"2015","journal-title":"World J. Gastroenterol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/j.imlet.2005.02.017","article-title":"Adaptive and innate immune responses in celiac disease","volume":"99","author":"Gianfrani","year":"2005","journal-title":"Immunol. Lett."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1912","DOI":"10.1053\/j.gastro.2009.09.008","article-title":"Celiac disease: From pathogenesis to novel therapies","volume":"137","author":"Schuppan","year":"2009","journal-title":"Gastroenterology"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1016\/j.bpg.2015.04.001","article-title":"T-cell and B-cell immunity in celiac disease","volume":"29","author":"Sollid","year":"2015","journal-title":"Best Pract. Res. Clin. Gastroenterol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1093\/ajcn\/85.1.160","article-title":"A prospective, double-blind, placebo-controlled trial to establish a safe gluten threshold for patients with celiac disease","volume":"85","author":"Catassi","year":"2007","journal-title":"Am. J. Clin. Nutr."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1016\/j.yapd.2008.07.001","article-title":"Celiac Disease: Pathophysiology, Clinical Manifestations and Associated Autoimmune Conditions","volume":"55","author":"Barker","year":"2008","journal-title":"Adv. Pediatr."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1053\/gast.2001.22123","article-title":"Current Approaches to Diagnosis and Treatment of Celiac Disease: An Evolving Spectrum","volume":"120","author":"Fasano","year":"2001","journal-title":"Gastroenterology"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"2419","DOI":"10.1056\/NEJMcp1113994","article-title":"Celiac Disease","volume":"367","author":"Fasano","year":"2007","journal-title":"N. Engl. J. Med."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1008","DOI":"10.1136\/jcp.2005.035345","article-title":"Coeliac disease: An update for pathologists","volume":"59","author":"Dickson","year":"2006","journal-title":"J. Clin. Pathol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/j.cell.2013.07.004","article-title":"The Intestinal Crypt, A Prototype Stem Cell Compartment","volume":"154","author":"Clevers","year":"2013","journal-title":"Cell"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"1216","DOI":"10.5858\/arpa.2013-0261-RA","article-title":"The Clinical Significance of Duodenal Lymphocytosis With Normal Villus Architecture","volume":"137","author":"Hammer","year":"2013","journal-title":"Arch. Pathol. Lab. Med."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1111\/j.1651-2227.1953.tb05563.x","article-title":"Coeliac Disease: II. The Presence in Wheat of a Factor Having a Deleterious Effect in Cases of Coeliac Disease","volume":"42","author":"Dicke","year":"1953","journal-title":"Acta Paediatr."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"836","DOI":"10.1016\/S0140-6736(52)90795-2","article-title":"Coeliac Disease: Gastrointestinal Studies and the Effect of Dietary","volume":"259","author":"Anderson","year":"1952","journal-title":"Lancet"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1111\/j.1651-2227.1953.tb05586.x","article-title":"Coeliac Disease: IV. An Investigation into the Injurious Constituents of Wheat in Connection with their Action on Patients with Celiac Disease","volume":"42","author":"Weijers","year":"1953","journal-title":"Acta Paediatr."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1093\/ajcn\/79.4.669","article-title":"Effect of a gluten-free diet on gastrointestinal symptoms in celiac disease","volume":"79","author":"Murray","year":"2004","journal-title":"Am. J. Clin. Nutr."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1111\/apt.12893","article-title":"Histological recovery and gluten-free diet adherence: A prospective 1-year follow-up study of adult patients with coeliac disease","volume":"40","author":"Galli","year":"2014","journal-title":"Aliment. Pharmacol. Ther."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"16","DOI":"10.3390\/nu2010016","article-title":"The Gluten-Free Diet: Safety and Nutritional Quality","volume":"2","author":"Saturni","year":"2010","journal-title":"Nutrients"},{"key":"ref_73","first-page":"156","article-title":"Coeliac Disease\u2014New Pathophysiological Findings and their Implications for Therapy","volume":"30","author":"Stein","year":"2014","journal-title":"Viszeralmedizin"},{"key":"ref_74","first-page":"S304","article-title":"Nexvax2(R), a Peptide-Based Antigen-Specific Immunotherapy, Administered Intra-Dermally Three-Times Over 15-Days attenuates Responsiveness to Immuno-Dominant Gluten Peptides in HLA-DQ2.5+ People with Celiac Disease (CeD)","volume":"150","author":"Goel","year":"2016","journal-title":"Gastroenterol. Abstr."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1111\/apt.15435","article-title":"Randomised clinical trial: A placebo-controlled study of subcutaneous or intradermal NEXVAX2, an investigational immunomodulatory peptide therapy for coeliac disease","volume":"50","author":"Truitt","year":"2019","journal-title":"Aliment. Pharmacol. Ther."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1002\/ygh2.380","article-title":"Baseline quantitative histology in therapeutics trials reveals villus atrophy in most patients with coeliac disease who appear well controlled on gluten-free diet","volume":"2","author":"Daveson","year":"2020","journal-title":"GastroHep"},{"key":"ref_77","unstructured":"(2020, November 27). ImmusanT Discontinues Phase 2 Clinical Trials for Nexvax2(R). Available online: https:\/\/www.coeliac.org.au\/news-stories\/immusant-discontinues-phase-2-clinical-trials-for-nexvax2\/."},{"key":"ref_78","doi-asserted-by":"crossref","unstructured":"Lapara, J.M., Olivares, M., Gallina, O., and Sanz, Y. (2012). Bifidobacterium longum CECT 7347 Modulates Immune Responses in a Gliadin-Induced Enteropathy Animal Model. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0030744"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"953","DOI":"10.3109\/09637486.2014.940283","article-title":"Lactobacillus paracasei CBA L74 interferes with gliadin peptides entrance in Caco-2 cells","volume":"65","author":"Sarno","year":"2014","journal-title":"Int. J. Food Sci. Nutr."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1111\/j.1365-2249.2008.03635.x","article-title":"Live probiotic Bifidobacterium lactis bacteria inhibit the toxic effects induced by wheat gliadin in epithelial cell culture","volume":"152","author":"Lindfors","year":"2008","journal-title":"Clin. Exp. Immunol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1177\/1756283X15616576","article-title":"The potential utility of tight junction regulation in celiac disease: Focus on larazotide acetate","volume":"9","author":"Khaleghi","year":"2016","journal-title":"Therap. Adv. Gastroenterol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.ijpharm.2008.08.047","article-title":"Mechanism of action of ZOT-derived peptide AT-1002, a tight junction regulator and absorption enhancer","volume":"365","author":"Gopalakrishnan","year":"2009","journal-title":"Int. J. Pharm."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"1311","DOI":"10.1053\/j.gastro.2015.02.008","article-title":"Larazotide acetate for persistent symptoms of celiac disease despite a gluten-free diet: A randomized controlled trial","volume":"148","author":"Leffler","year":"2015","journal-title":"Gastroenterology"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"1554","DOI":"10.1038\/ajg.2012.211","article-title":"A randomized, double-blind study of larazotide acetate to prevent the activation of celiac disease during gluten challenge","volume":"107","author":"Leffler","year":"2012","journal-title":"Am. J. Gastroenterol."},{"key":"ref_85","first-page":"765","article-title":"Pivotal Advance: Bifidobacteria and Gram-negative bacteria differentially influence immune responses in the proinflammatory milieu of celiac disease","volume":"87","author":"Cinova","year":"2010","journal-title":"J. Leukoc. Biol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1128\/CMR.00106-13","article-title":"Intestinal Microbiota and Probiotics in Celiac Disease","volume":"27","author":"Grzeskowiak","year":"2014","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1097\/MCG.0b013e31827759ac","article-title":"Exploratory, randomized, double-blind, placebo-controlled study on the effects of Bifidobacterium infantis natren life start strain super strain in active celiac disease","volume":"47","author":"Smecuol","year":"2013","journal-title":"J. Clin. Gastroenterol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"508","DOI":"10.1016\/j.jaci.2014.07.022","article-title":"Experimental hookworm infection and gluten microchallenge promote tolerance in celiac disease","volume":"135","author":"Croese","year":"2014","journal-title":"J. Allergy Clin. Immunol."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"15849","DOI":"10.1073\/pnas.0908834106","article-title":"Antibody-mediated blockade of IL-15 reverses the autoimmune intestinal damage in transgenic mice that overexpress IL-15 in enterocytes","volume":"106","author":"Yokoyama","year":"2009","journal-title":"PNAS"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"1201","DOI":"10.4155\/cli.12.119","article-title":"The emerging role of vedolizumab in the treatment of ulcerative colitis","volume":"2","author":"Mosli","year":"2012","journal-title":"Clin. Investig."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"864","DOI":"10.1124\/jpet.109.153973","article-title":"The Binding Specificity and Selective Antagonism of Vedolizumab, an Anti-alpha4beta7 Integrin Therapeutic Antibody in Development for Inflammatory Bowel Diseases","volume":"330","author":"Soler","year":"2009","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1124\/jpet.110.169714","article-title":"Characterization of CCX282-B, an Orally Bioavailable Antagonist of the CCR9 Chemokine Receptor, for Treatment of Inflammatory Bowel Disease","volume":"335","author":"Walters","year":"2010","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_93","doi-asserted-by":"crossref","unstructured":"Keshav, S., Vanasek, T., Niv, Y., Petryka, R., Howaldt, S., Bafutto, M., Racz, I., Hetzel, D., Nielsen, O., and Severine, V. (2013). A Randomized Controlled Trial of the Efficacy and Safety of CCX282-B, an Orally-Administered Blocker of Chemokine Receptor CCR9, for Patients with Crohn\u2019s Disease. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0060094"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"10150","DOI":"10.1021\/jf902268z","article-title":"Blocking Peptides Decrease Tissue Transglutaminase Processing of Gliadin in Vitro","volume":"57","author":"Hoffmann","year":"2009","journal-title":"J. Agric. Food Chem."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"2053","DOI":"10.1016\/j.bmc.2007.10.091","article-title":"Design of azidoproline containing gluten peptides to suppress CD4 + T-cell responses associated with Celiac disease","volume":"16","author":"Kapoerchan","year":"2008","journal-title":"Bioorg. Med. Chem."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"1091","DOI":"10.1016\/j.molimm.2009.10.036","article-title":"Design, synthesis and evaluation of high-affinity binders for the celiac disease associated HLA-DQ2 molecule","volume":"47","author":"Kapoerchan","year":"2010","journal-title":"Mol. Immunol."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"1859","DOI":"10.1021\/ja056423o","article-title":"Inhibition of HLA-DQ2-Mediated Antigen Presentation by Analogues of a High Affinity 33-Residue Peptide from alpha2-Gliadin","volume":"128","author":"Xia","year":"2006","journal-title":"J. Am. Chem. Soc."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"1400","DOI":"10.1053\/j.gastro.2005.07.054","article-title":"Unexpected Role of Surface Transglutaminase Type II in Celiac Disease","volume":"129","author":"Maiuri","year":"2005","journal-title":"Gastroenterology"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"S490","DOI":"10.1016\/S0016-5085(18)31861-4","article-title":"The Oral Transglutaminase 2 (TG2) Inhibitor Zed1227 Blocks TG2 Activity in a Mouse Model of Intestinal Inflammation","volume":"154","author":"Ventura","year":"2018","journal-title":"Gastroenterology"},{"key":"ref_100","unstructured":"(2020, November 30). Reversibly Acting Transglutaminase 2 Inhibitors: Drug Candidates for the Treatment of Fibrosis. Available online: https:\/\/zedira.com\/News\/Reversibly-acting-transglutaminase-2-inhibitors-drug-candidates-for-the-treatment-of-fibrosis_127."},{"key":"ref_101","unstructured":"(2020, November 30). Press Release: Dr. Falk Pharma and Zedira Announce Completion of Phase 1b Clinical Trial of ZED1227 for the Treatment of Celiac Disease and Move on to Proof of Concept Study. Available online: https:\/\/zedira.com\/News\/Press-release-Dr-Falk-Pharma-and-Zedira-announce-completion-of-phase-1b-clinical-trial-of-ZED1227-for-the-treatment-of-celiac-disease-and-move-on-to-proof-of-concept-study_97."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"4499","DOI":"10.1128\/AEM.00260-07","article-title":"Highly Efficient Gluten Degradation by Lactobacilli and Fungal Proteases During Food Processing: New Perspectives for Celiac Disease","volume":"73","author":"Rizzello","year":"2007","journal-title":"Appl. Environ. Microbiol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"2134","DOI":"10.3390\/nu7042134","article-title":"Sourdough Fermentation of Wheat Flour does not Prevent the Interaction of Transglutaminase 2 with \u03b12-Gliadin or Gluten","volume":"7","author":"Sandberg","year":"2015","journal-title":"Nutrients"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"5837","DOI":"10.3748\/wjg.v19.i35.5837","article-title":"Consumption of gluten with gluten-degrading enzyme by celiac patients: A pilot-study","volume":"19","author":"Tack","year":"2013","journal-title":"World J. Gastroenterol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1007\/s10620-011-1906-5","article-title":"Safety, Tolerability, and Activity of ALV003: Results from Two Phase 1 Single, Escalating-Dose Clinical Trials","volume":"57","author":"Siegel","year":"2012","journal-title":"Dig. Dis. Sci."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"1277","DOI":"10.1007\/s10620-016-4426-5","article-title":"AGY, a Novel Egg Yolk-Derived Anti-gliadin Antibody, Is Safe for Patients with Celiac Disease","volume":"62","author":"Sample","year":"2017","journal-title":"Dig. Dis. Sci."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"3166","DOI":"10.1021\/jf205319s","article-title":"In-vitro and in-vivo binding activity of chicken egg yolk immunoglobulin y (IgY) against gliadin in food matrix","volume":"60","author":"Gujral","year":"2012","journal-title":"J. Agric. Food Chem."},{"key":"ref_108","doi-asserted-by":"crossref","unstructured":"McCarville, J.L., Nisemblat, Y., Galipeau, H.J., Jury, J., Tabakman, R., Cohen, A., Naftali, E., Neiman, B., Halbfinger, E., and Murray, J.A. (2014). BL-7010 Demonstrates Specific Binding to Gliadin and Reduces Gluten-Associated Pathology in a Chronic Mouse Model of Gliadin Sensitivity. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0109972"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"418","DOI":"10.1002\/bip.21352","article-title":"Interaction of alpha-gliadin with polyanions: Design considerations for sequestrants used in supportive treatment of celiac disease","volume":"93","author":"Liang","year":"2010","journal-title":"Biopolymers"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1002\/bip.21109","article-title":"Interaction of alpha-gliadin with poly(HEMA-co-SS): Structural characterization and biological implication","volume":"91","author":"Liang","year":"2009","journal-title":"Biopolymers"},{"key":"ref_111","unstructured":"Imperato, F. (2006). Role of phenolics in the resistance mechanisms of plants against fungal pathogens and insects. Phytochemistry: Advances in Research, Research Signpost."},{"key":"ref_112","unstructured":"Postmyr, L. (2008). Biopolymer Chemistry, Tapir Academic Press."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.3390\/nu2121231","article-title":"Chemistry and Biochemistry of Dietary Polyphenols","volume":"2","author":"Tsao","year":"2010","journal-title":"Nutrients"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"1152","DOI":"10.1002\/mnfr.200700086","article-title":"Common tea formulations modulate in vitro digestive recovery of green tea catechins","volume":"51","author":"Green","year":"2007","journal-title":"Mol. Nutr. Food Res."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.freeradbiomed.2016.05.019","article-title":"Quinone-induced protein modifications: Kinetic preference for reaction of 1,2-benzoquinones with thiol groups in proteins","volume":"97","author":"Li","year":"2016","journal-title":"Free Radic. Biol. Med."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1039\/C3FO60263J","article-title":"Nature and consequences of non-covalent interactions between flavonoids and macronutrients in foods","volume":"5","author":"Bordenave","year":"2014","journal-title":"Food Funct."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"4494","DOI":"10.1016\/S0021-9258(19)69462-7","article-title":"The specificity of proanthocyanidin-protein interactions","volume":"256","author":"Hagerman","year":"1981","journal-title":"J. Biol. Chem."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"942","DOI":"10.1021\/bm0345110","article-title":"Molecular model for astringency produced by polyphenol\/protein interactions","volume":"5","author":"Fairclough","year":"2004","journal-title":"Biomacromolecules"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"1593","DOI":"10.1021\/jf010897z","article-title":"Polyphenol\/peptide binding and precipitation","volume":"50","author":"Charlton","year":"2002","journal-title":"J. Agric. Food Chem."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"1035","DOI":"10.1021\/np9904509","article-title":"Flavonoids as Antioxidants","volume":"63","author":"Pietta","year":"2000","journal-title":"J. Nat. Prod."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"8915","DOI":"10.1021\/jf201491k","article-title":"Investigating the hydrogen peroxide quenching capacity of proteins in polyphenol-rich foods","volume":"59","author":"Zhou","year":"2011","journal-title":"J. Agric. Food Chem."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"1621","DOI":"10.1271\/bbb.63.1621","article-title":"Radical Scavenging Activity of Tea Catechins and Their Related Compounds","volume":"63","author":"Nanjo","year":"1999","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1080\/10408399709527797","article-title":"The Chemistry of Tea Flavonoids","volume":"37","author":"Balentine","year":"1997","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1080\/10408690390826464","article-title":"Tea catechins and polyphenols: Health effects, metabolism, and antioxidant functions","volume":"43","author":"Higdon","year":"2003","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/S0027-5107(01)00183-X","article-title":"Molecular mechanisms underlying chemopreventive activities of anti-inflammatory phytochemicals: Down-regulation of COX-2 and iNOS through suppression of NF-kB activation","volume":"480","author":"Surh","year":"2001","journal-title":"Fundam. Mol. Mech. Mutagen."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"1281","DOI":"10.1016\/S0006-2952(97)00504-2","article-title":"Inhibition of Inducible Nitric Oxide Synthase Gene Expression and Enzyme Activity by Epigallocatechin Gallate, a Natural Product from Green Tea","volume":"54","author":"Chan","year":"1997","journal-title":"Biochem. Pharmacol."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1124\/mol.52.3.465","article-title":"(-)-Epigallocatechin-3-gallate Blocks the Induction of Nitric Oxide Synthase by Down-Regulating Lipopolysaccharide- Induced Activity of Transcription Factor Nuclear Factor-kB","volume":"52","author":"Lin","year":"1997","journal-title":"Mol. Pharmacol."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"1175","DOI":"10.1016\/S0006-2952(01)00767-5","article-title":"Effects of purified green and black tea polyphenols on cyclooxygenase- and lipoxygenase-dependent metabolism of arachidonic acid in human colon mucosa and colon tumor tissues","volume":"62","author":"Hong","year":"2001","journal-title":"Biochem. Pharmacol."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"1528","DOI":"10.1016\/j.metabol.2010.01.018","article-title":"Epigallocatechin gallate\u2013mediated protection against tumor necrosis factor-\u03b1\u2013induced monocyte chemoattractant protein\u20131 expression is heme oxygenase\u20131 dependent","volume":"59","author":"Zheng","year":"2010","journal-title":"Metabolism"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"690","DOI":"10.1186\/2193-1801-2-690","article-title":"(-)-Epigallocatechin-3-gallate suppresses hepatic preneoplastic lesions developed in a novel rat model of non-alcoholic steatohepatitis","volume":"2","author":"Sumi","year":"2013","journal-title":"Springerplus"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"1771","DOI":"10.1017\/S000711451000005X","article-title":"Effects of epigallocatechin gallate on regulatory T cell number and function in obese v. lean volunteers","volume":"103","author":"Yun","year":"2010","journal-title":"Br. J. Nutr."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1079\/BJN19880100","article-title":"Effect of tannin-rich leaves of oak (Quercus incana) on various microbial enzyme activities of the bovine rumen","volume":"60","author":"Makkar","year":"1988","journal-title":"Br. J. Nutr."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1079\/BJN19880099","article-title":"Effects of condensed tannins prepared from leaves of fodder plants on digestive enzymes in vitro and in the intestine of rats","volume":"60","author":"Horigome","year":"1988","journal-title":"Br. J. Nutr."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/j.jnutbio.2006.12.005","article-title":"Green Tea as Inhibitor of the Intestinal Absorption of Lipids: Potential Mechanism for its Lipid-Lowering Effect","volume":"18","author":"Koo","year":"2007","journal-title":"J. Nutr. Biochem."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"2791","DOI":"10.1093\/jn\/136.11.2791","article-title":"Epigallocatechin gallate and caffeine differentially inhibit the intestinal absorption of cholesterol and fat in ovariectomized rats","volume":"136","author":"Wang","year":"2006","journal-title":"J. Nutr."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"8829","DOI":"10.1021\/jf401779z","article-title":"Characterization of binding interactions of (-)-epigallocatechin-3-gallate from green tea and lipase","volume":"61","author":"Wu","year":"2013","journal-title":"J. Agric. Food Chem."},{"key":"ref_137","first-page":"67","article-title":"Nitrogen balance studies among boys fed combinations of faba beans and wheat differing in polyphenolic contents","volume":"31","author":"Hussein","year":"1985","journal-title":"Nutr. Rep. Int."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"2734","DOI":"10.1021\/jf103072z","article-title":"Epigallocatechin-3-gallate inhibits lactase but is alleviated by salivary proline-rich proteins","volume":"59","author":"Naz","year":"2011","journal-title":"J. Agric. Food Chem."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"1178","DOI":"10.1016\/j.foodchem.2006.03.020","article-title":"Food Chemistry Effects of tea polyphenols on the activities of alpha-amylase, pepsin, trypsin and lipase","volume":"101","author":"He","year":"2006","journal-title":"Food Chem."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1016\/j.jff.2012.04.006","article-title":"Green tea catechins of food supplements facilitate pepsin digestion of major food allergens, but hampers their digestion if oxidized by phenol oxidase","volume":"4","author":"Tantoush","year":"2012","journal-title":"J. Funct. Foods"},{"key":"ref_141","doi-asserted-by":"crossref","unstructured":"Martinez-Gonzalez, A., Diaz-Sanchez, A., de la Rosa, L., Vargas-Requena, C., Bustos-Jaimes, I., and Alvarez-Parrilla, E. (2017). Polyphenolic Compounds and Digestive Enzymes: In Vitro Non-Covalent Interactions. Molecules, 22.","DOI":"10.3390\/molecules22040669"},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"91","DOI":"10.3748\/wjg.v20.i1.91","article-title":"Inflammatory bowel disease: Pathogenesis","volume":"20","author":"Zhang","year":"2014","journal-title":"World Gastroenterol."},{"key":"ref_143","doi-asserted-by":"crossref","unstructured":"Vezza, T., Rodr\u00edguez-Nogales, A., Algieri, F., Utrilla, M.P., Rodriguez-Cabezas, M.E., and Galvez, J. (2016). Flavonoids in Inflammatory Bowel Disease: A Review. Nutrients, 8.","DOI":"10.3390\/nu8040211"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1038\/ajg.2014.357","article-title":"Treatment of IBD: Where We Are and Where We Are Going","volume":"110","author":"Bernstein","year":"2015","journal-title":"Am. J. Gastroenterol."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1016\/j.crohns.2011.08.012","article-title":"Green tea polyphenol epigallocatechin-3-gallate shows therapeutic antioxidative effects in a murine model of colitis","volume":"6","author":"Westphal","year":"2012","journal-title":"J. Crohn\u2019s Colitis"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"132","DOI":"10.3389\/fimmu.2013.00132","article-title":"Green tea polyphenols and sulfasalazine have parallel anti-inflammatory properties in colitis models","volume":"4","author":"Oz","year":"2013","journal-title":"Front. Immunol."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"2334","DOI":"10.1093\/jn\/128.12.2334","article-title":"Green Tea Polyphenols Block Endotoxin-Induced Tumor Necrosis Factor- Production and Lethality in a Murine Model","volume":"128","author":"Yang","year":"1998","journal-title":"J. Nutr."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1016\/j.cbi.2010.08.007","article-title":"Anti-inflammatory effects of dietary phenolic compounds in an in vitro model of inflamed human intestinal epithelium","volume":"188","author":"Sergent","year":"2010","journal-title":"Chem. Biol. Interact."},{"key":"ref_149","doi-asserted-by":"crossref","unstructured":"Al-Sadi, R., Ye, D., Boivin, M., Guo, S., Hashimi, M., Ereifej, L., and Ma, T.Y. (2014). Interleukin-6 Modulation of Intestinal Epithelial Tight Junction Permeability Is Mediated by JNK Pathway Activation of Claudin-2 Gene. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0085345"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1203\/01.PDR.0000050141.73528.AD","article-title":"Modulation of Human Intestinal Epithelial Cell IL-8 Secretion by Human Milk Factors","volume":"53","author":"Claud","year":"2003","journal-title":"Pediatr. Res."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"2072","DOI":"10.1097\/MIB.0000000000001108","article-title":"Dietary Polyphenols in the Aetiology of Crohn\u2019s Disease and Ulcerative Colitis-A Multicenter European Prospective Cohort Study (EPIC)","volume":"23","author":"Lu","year":"2017","journal-title":"Inflamm. Bowel Dis."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/j.nutres.2020.01.002","article-title":"Mango (Mangifera indica L.) polyphenols reduce IL-8, GRO, and GM-SCF plasma levels and increase Lactobacillus species in a pilot study in patients with inflammatory bowel disease","volume":"75","author":"Kim","year":"2020","journal-title":"Nutr. Res."},{"key":"ref_153","doi-asserted-by":"crossref","unstructured":"Roth, S., Spalinger, M.R., Gottier, C., Biedermann, L., Zeitz, J., Lang, S., Weber, A., Rogler, G., and Scharl, M. (2016). Bilberry-derived anthocyanins modulate cytokine expression in the intestine of patients with ulcerative colitis. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0154817"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1016\/j.foodchem.2012.10.076","article-title":"Apple polyphenols suppress antigen presentation of ovalbumin by THP-1-derived dendritic cells","volume":"138","author":"Katayama","year":"2013","journal-title":"Food Chem."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"1468","DOI":"10.1016\/j.foodchem.2012.03.057","article-title":"Removing peanut allergens by tannic acid","volume":"134","author":"Chung","year":"2012","journal-title":"Food Chem."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"2145","DOI":"10.1039\/C5FO00162E","article-title":"Stability and immunogenicity of hypoallergenic peanut protein\u2013polyphenol complexes during in vitro pepsin digestion","volume":"6","author":"Plundrich","year":"2015","journal-title":"Food Funct."},{"key":"ref_157","first-page":"57","article-title":"Evaluation of Residual Immunoreactivity in Red and White Wines Clarified with Gluten or Gluten Derivatives","volume":"25","author":"Cattaneo","year":"2003","journal-title":"Int. J. Tissue React."},{"key":"ref_158","first-page":"45","article-title":"Evaluation by SDS-PAGE and Immunoblotting of Residual Antigenicity in Gluten-Treated Wine: A Preliminary Study","volume":"24","author":"Restani","year":"2002","journal-title":"Int. J. Tissue React."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"3586","DOI":"10.1016\/j.foodchem.2013.05.136","article-title":"Study on the interaction between gliadins and a coumarin as molecular model system of the gliadins\u2013anthocyanidins complexes","volume":"141","author":"Tozzi","year":"2013","journal-title":"Food Chem."},{"key":"ref_160","doi-asserted-by":"crossref","unstructured":"Taddei, P., Zanna, N., and Tozzi, S. (2013). Raman characterization of the interactions between gliadins and anthocyanins. J. Raman Spectrosc., 44.","DOI":"10.1002\/jrs.4288"},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"1100","DOI":"10.1016\/j.foodchem.2011.05.084","article-title":"Interaction between gliadins and anthocyan derivatives","volume":"129","author":"Mazzaracchio","year":"2011","journal-title":"Food Chem."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"390","DOI":"10.1111\/j.1365-2621.2011.02852.x","article-title":"Adsorption behaviour of some anthocyanins by wheat gluten and its fractions in acidic conditions","volume":"47","author":"Mazzaracchio","year":"2012","journal-title":"Int. J. Food Sci. Technol."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"32151","DOI":"10.1039\/C5RA02968F","article-title":"De The interaction between tannins and gliadin derived peptides in a celiac disease perspective","volume":"5","author":"Dias","year":"2015","journal-title":"RSC Adv."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"1154","DOI":"10.1016\/j.foodchem.2017.11.054","article-title":"Interaction mechanisms of condensed tannins (proanthocyanidins) with wheat gluten proteins","volume":"245","author":"Girard","year":"2018","journal-title":"Food Chem."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"6442","DOI":"10.1021\/acs.jafc.6b05371","article-title":"Polyphenol Interactions Mitigate the Immunogenicity and Allergenicity of Gliadins","volume":"65","author":"Lupi","year":"2017","journal-title":"J. Agric. Food Chem."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/j.foodchem.2019.01.081","article-title":"Binding of peanut allergen Ara h 2 with Vaccinium fruit polyphenols","volume":"284","author":"Plundrich","year":"2019","journal-title":"Food Chem."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.foodchem.2014.05.005","article-title":"Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white","volume":"164","author":"Velickovic","year":"2014","journal-title":"Food Chem."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"125051","DOI":"10.1016\/j.foodchem.2019.125051","article-title":"A multi-spectroscopic study on the interaction of food polyphenols with a bioactive gluten peptide: From chemistry to biological implications","volume":"299","author":"Dias","year":"2019","journal-title":"Food Chem."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"1029","DOI":"10.1016\/j.ijbiomac.2018.02.055","article-title":"Molecular insights on the interaction and preventive potential of epigallocatechin-3-gallate in Celiac Disease","volume":"112","author":"Dias","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1007\/BF02602553","article-title":"Peptide binding characteristics of the coeliac disease-associated DQ(aII*0501, 1*0201) molecule","volume":"44","author":"Kooy","year":"1996","journal-title":"Immunogenetics"},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1084\/jem.20012028","article-title":"Specificity of tissue transglutaminase explains cereal toxicity in celiac disease","volume":"195","author":"Vader","year":"2002","journal-title":"J. Exp. Med."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/s10565-005-0085-6","article-title":"The Caco-2 cell line as a model of the intestinal barrier: Influence of cell and culture-related factors on Caco-2 cell functional characteristics","volume":"21","author":"Sambuy","year":"2005","journal-title":"Cell Biol. Toxicol."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/S0300-483X(99)00223-1","article-title":"Induction of apoptosis in Caco-2 cells by wheat gliadin peptides","volume":"145","author":"Giovannini","year":"2000","journal-title":"Toxicology"},{"key":"ref_174","doi-asserted-by":"crossref","unstructured":"Capozzi, A., Vincentini, O., Gizzi, P., Porzia, A., Longo, A., Felli, C., Mattei, V., Mainiero, F., Silano, M., and Sorice, M. (2013). Modulatory Effect of Gliadin Peptide 10-mer on Epithelial Intestinal CACO-2 Cell Inflammatory Response. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0066561"},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/j.jff.2019.03.039","article-title":"Procyanidin B2 rich cocoa extracts inhibit inflammation in Caco-2 cell model of in vitro celiac disease by down-regulating interferon-gamma- or gliadin peptide 31-43-induced transglutaminase-2 and interleukin-15","volume":"57","author":"Kramer","year":"2019","journal-title":"J. Funct. Foods"},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"2267","DOI":"10.1002\/mnfr.201501042","article-title":"(-)-Epigallocatechin-3-gallate decreases colonic inflammation and permeability in a mouse model of colitis, but reduces macronutrient digestion and exacerbates weight loss","volume":"60","author":"Bitzer","year":"2016","journal-title":"Mol. Nutr. Food Res."},{"key":"ref_177","doi-asserted-by":"crossref","unstructured":"Gonz\u00e1lez-Quilen, C., Grau-Bov\u00e9, C., Jorba-Mart\u00edn, R., Caro-Tarrag\u00f3, A., Pinent, M., Ard\u00e9vol, A., Beltr\u00e1n-Deb\u00f3n, R., Terra, X., and Blay, M.T. (2020). Protective properties of grape-seed proanthocyanidins in human ex vivo acute colonic dysfunction induced by dextran sodium sulfate. Eur. J. Nutr.","DOI":"10.1007\/s00394-020-02222-3"},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1136\/gut.44.1.17","article-title":"Increased expression of mRNA for matrix metalloproteinases-1 and -3 and tissue inhibitor of metalloproteinases-1 in intestinal biopsy specimens from patients with coeliac disease","volume":"44","author":"Daum","year":"1999","journal-title":"Gut"},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.humimm.2009.09.351","article-title":"Serum cytokine elevations in celiac disease: Association with disease presentation","volume":"71","author":"Manavalan","year":"2010","journal-title":"Hum. Immunol."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1007\/s10875-006-9061-z","article-title":"Gliadin Peptides Activate Blood Monocytes from Patients with Celiac Disease","volume":"27","author":"Cinova","year":"2007","journal-title":"J. Clin. Immunol."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"1298","DOI":"10.1093\/hmg\/ddt520","article-title":"Coregulation and modulation of NF\u03baB-related genes in celiac disease: Uncovered aspects of gut mucosal inflammation","volume":"23","author":"Irastorza","year":"2014","journal-title":"Hum. Mol. Genet."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1007\/s10238-014-0325-2","article-title":"Gliadin-dependent cytokine production in a bidimensional cellular model of celiac intestinal mucosa","volume":"15","author":"Vincentini","year":"2015","journal-title":"Clin. Exp. Med."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1111\/j.1365-2567.2010.03378.x","article-title":"Identification of a novel immunomodulatory gliadin peptide that causes interleukin-8 release in a chemokine receptor CXCR3-dependent manner only in patients with coeliac disease","volume":"132","author":"Lammers","year":"2011","journal-title":"Immunology"},{"key":"ref_184","first-page":"232","article-title":"Role of Tissue Transglutaminase in Celiac Disease","volume":"30","author":"Molberg","year":"2000","journal-title":"J. Pediatr. Gastroenterol. Nutr."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1172\/JCI30253","article-title":"Celiac disease: Pathogenesis of a model immunogenetic disease","volume":"117","author":"Kagnoff","year":"2007","journal-title":"J. Clin. Investig."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/22\/2\/595\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T05:08:54Z","timestamp":1760159334000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/22\/2\/595"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,1,8]]},"references-count":185,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2021,1]]}},"alternative-id":["ijms22020595"],"URL":"https:\/\/doi.org\/10.3390\/ijms22020595","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,1,8]]}}}