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The 33\u2010mer deamidated gliadin peptide (DGP) is a metabolically modified wheat\u2010gluten superantigen for CeD. Here, we demonstrate that the 33\u2010mer DGP spontaneously assembles into oligomers with a diameter of approximately 24\u2005nm. The 33\u2010mer DGP oligomers present two main secondary structural motifs\u2013a major polyproline II helix and a minor \u03b2\u2010sheet structure. Importantly, in the presence of 33\u2010mer DGP oligomers, there is a statistically significant increase in the permeability in the gut epithelial cell model Caco\u20102, accompanied by the redistribution of zonula occludens\u20101, a master tight junction protein. These findings provide novel molecular and supramolecular insights into the impact of 33\u2010mer DGP in CeD and highlight the relevance of gliadin peptide oligomerization.<\/jats:p>","DOI":"10.1002\/anie.202317552","type":"journal-article","created":{"date-parts":[[2024,3,18]],"date-time":"2024-03-18T10:58:58Z","timestamp":1710759538000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":10,"title":["The Celiac\u2010Disease Superantigen Oligomerizes and Increases Permeability in an Enterocyte Cell Model"],"prefix":"10.1002","volume":"63","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8874-7410","authenticated-orcid":false,"given":"Maria G.","family":"Herrera","sequence":"first","affiliation":[{"name":"Department of Chemistry Bielefeld University  Universit\u00e4tsstr. 25 33615 Bielefeld Germany"},{"name":"Department of Physiology and Molecular and Cellular Biology Institute of Biosciences Biotechnology and Translational 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