The Supramolecular structure of gliadin protein is modulated by pH: toward understanding the molecular triggers of gliadin related pathologies

HERRERA GEORGINA; VEUTHEY TANIA V; DODERO VERONICA I

Villa Carlos Paz

Congreso; XLII Reunion anual de la Sociedad Argentina de Biofisica; 2013

Gliadin has been described as the most toxic protein fraction of gluten related with different human diseases, such as celiac disease, durhing disease, ataxia and gliadin sensibility and allergy, among others [1, 2]. It has been hypothesized that gliadin can reach the intestinal lumen inducing an increase in intestinal permeability that seem to be a critical and early event in the pathogenesis of these diseases [3]. Although it is known the ability of gliadin to form high molecular weight aggregates [4], it has not been performed a complete characterization of those aggregates. Considering the relevance of pH in the digestion process, we decided to carry out a supramolecular evaluation of gliadin at different pHs by a physicochemical approach. The aim will be directed to shed light on the molecular self-organization depending on environmental stimulus. Herein, the evaluation of gliadin aggregates by a combination of UV-Vis, steady state fluorescence, dynamic light scattering, optical and electron microscopy is presented