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The 13mer \u03b1\u2010gliadin peptide, p31\u201043, induces proinflammatory responses, observed by <jats:italic>in\u00a0vitro <\/jats:italic>assays and animal models, that may contribute to innate immune mechanisms of CeD pathogenesis. Since a cellular receptor for p31\u201043 has not been identified, this raises the question of whether this peptide could mediate different biological effects. In this work, we aimed to characterize the p31\u201043 secondary structure by different biophysical and <jats:italic>in\u00a0silico<\/jats:italic> techniques. By dynamic light scattering and using an oligomer\/fibril\u2010sensitive fluorescent probe, we showed the presence of oligomers of this peptide in solution. Furthermore, atomic force microscopy analysis showed p31\u201043 oligomers with different height distribution. Also, peptide concentration had a very strong influence on peptide self\u2010organization process. Oligomers gradually increased their size at lower concentration. Whereas, at higher ones, oligomers increased their complexity, forming branched structures. By CD, we observed that p31\u201043 self\u2010organized in a polyproline II conformation in equilibrium with \u03b2\u2010sheets\u2010like structures, whose pH remained stable in the range of 3\u20138. In addition, these findings were supported by molecular dynamics simulation. The formation of p31\u201043 nanostructures with increased \u03b2\u2010sheet structure may help to explain the molecular etiopathogenesis in the induction of proinflammatory effects and subsequent damage at the intestinal mucosa in CeD.<\/jats:p>","DOI":"10.1111\/febs.15109","type":"journal-article","created":{"date-parts":[[2019,10,29]],"date-time":"2019-10-29T05:55:10Z","timestamp":1572328510000},"page":"2134-2149","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":29,"title":["Structural conformation and self\u2010assembly process of p31\u201043 gliadin peptide in aqueous solution. 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