PUB - Publikationen an der Universität Bielefeld

Gluten-related disorders are a group of diseases that involve the activation of the immune system triggered by the ingestion of gluten. These disorders have a high prevalence in Western societies, around 5% worldwide because gluten is present in wheat, rye, barley, and some varieties of oats. Gliadin is a protein present in wheat, and it is the most studied protein in gluten-related disorders. It is accepted that the incomplete proteolysis of the gluten proteins is responsible for disease in susceptible individuals. From the chemical perspective, up to now, the research efforts focused on the identification, quantification, and separation of the components of gluten and connecting them with their pathological role in vitro and in vivo. Interestingly, while the primary structure of the molecules involved in the disease is known, there is a lack of information about their intrinsic behavior –such as their folding and molecular organization- under physiologically relevant conditions and physiological roles in human nutrition. Gliadin and its 33-mer fragment have a central pathogenic role in gluten-related disorders, and we discovered that it forms oligomers and large aggregates. Additionally, other gliadin peptides form amyloid-like structures and influence the expression of pro-inflammatory and apoptotic genes in cellular models. Our research focuses on understanding the role of such gluten-peptide aggregates as triggers of the disease.