The 33-mer gliadin peptide and its deamidated derivative, known as 33-mer DGP, are proteolytically resistant peptides central to the pathomechanism of celiac disease (CeD), the autoimmune presentation of gluten-related disorders (GRD). Both peptides can form spontaneous oligomers in the nanomolar concentration, leading to the formation of nanostructures. In other protein-related diseases, oligomers and aggregates are central in their pathomechanism
therefore, it was hypothesized that the oligomerization of proteolytical-resistant 33-mer gliadin peptides could be an underrecognized disease trigger. This review focuses on the current understanding of 33-mer peptides and their oligomers in vitro and cellular experiments. We intend to give the necessary details that incentivize the chemistry community to get involved in the effort to understand the self-assembly of gliadin peptides and the role of their supramolecular structures in CeD and the other GRD. More research is needed to design effective and safe chemical and/or nutritional interventions beyond the gluten-free diet.