Gliadin is able to self-assembly under physiological pHs. Insights of gliadin intorelance disorders

VEUTHEY TANIA V; HERRERA GEORGINA; COSTABEL MARCELO; DODERO VERONICA I

Sierra de la Ventana

Congreso; XLIII Reunión Anual de Biofisica; 2014

Gliadin and glutenin are the major component of gluten, a protein complex present in wheat .It is known that its mean ingestion in a healthy individual is around 50g per day. Gluten but especially gliadin is the responsible of a wide range of autoimmune disorders as celiac disease and gliadin intolerance. Actual statistics have determined that the first one affects 1% and the second 7% of the total world population (1, 2). These disorders are caused by the incomplete proteolysis of gliadin during digestion, however the reasons of this resistance remains unclear. Taking into account that change of pH from ≈ 2-3 to 7 is an important step during digestion (3); we evaluated the supramolecular characteristics of gliadin at both conditions by combination of UV-Vis and Fluorescence Spectroscopy, Electron Microscopy and Dynamic Light Scattering. Based on our results, we hypothesized that the morphology and nature of gliadin aggregates could led to proteolytic resistance in vivo.