PUB - Publikationen an der Universität Bielefeld

Celiac disease (CeD) is an autoimmune disorder triggered by gluten proteins, affecting approximately 1% of the global population. The 33-mer deamidated gliadin peptide (DGP) is a metabolically modified wheat-gluten superantigen for CeD. Here, we demonstrate that the 33-mer DGP spontaneously assembles into oligomers with a diameter of approximately 24 nm. The 33-mer DGP oligomers present two main secondary structural motifs-a major polyproline II helix and a minor beta-sheet structure. Importantly, in the presence of 33-mer DGP oligomers, there isa statistically significant increase in the permeability in the gut epithelial cell model Caco-2, accompanied by the redistribution of zonula occludens-1, a master tight junction protein. These findings provide novel molecular and supramolecular insights into the impact of 33-mer DGP in CeD and highlight the relevance of gliadin peptide oligomerization. © 2024 Wiley-VCH GmbH.