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

VEUTHEY . T; HERRERA, M.G; COSTABEL. M.M.; DODERO.V.I

Sierra de la Ventana

Congreso; XLIII Reunión Anual de la Sociedad Argentina de Biofísica; 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 gluten 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 this process (3); we propose to evaluate the Supramolecular characteristics of gliadin at both conditions. We have performed UV-Vis and Fluorescence Spectroscopies, Electron Microscopies and Dynamic Light Sccatering to study gliadin at these physiological pHs. We hypothesize that gliadin could self-assembly to a compact structure that do not allow enzymes action on it, generating its proteolytic resistance. References: (1)Rubio-Tapia, A. et. al. Curr opin gastroenterol. 2010, 116.(2)Sapone, A. et al. BMC Med.2012, 13. (3)Kararli, T. T. et. al. Biopharm Drug Dispos 351.