Atomic Force Microscopy and Electron Microscopy Studies of 33-mer Gliadin Peptide on silicon surface

HERRERA M.G.; PATRICIA SCHILARDI; ROBERTO SALVAREZZA; NADINE MILL; KARSTEN ROT; HUTTEN ANDREAS; NORBERT SEWALD; DODERO V. I

Congreso; XLI Reunión Anual de la Sociedad Argentina de Biofísica; 2012

The 33-mer fragment of gliadin protein, LQLQPF(PQPQLPY)3PQPQPF is one of the proline-rich peptides which elicit an immune response in susceptible individuals and it is associated with gluten sensitivity (1) and celiac disease (2). Celiac disease results from innate and adaptive immune system dysregulation. Activation of the adaptive immune system implies that gliadin peptides cross the intestinal epithelium probably by a paracellular as well as transcellular mechanisms (3). It has been hypothesized that increased intestinal permeability is an early event in celiac disease pathogenesis (4) but it is completely unknown what endows gliadin and especially the 33-mer fragment such special features to act as stress triggers to the epithelium. In order to mimic the interfacial interaction of 33-mer and the intestinal epithelium, we have performed a study to evaluate 33-mer self-assembly on silicon and silicon oxide surfaces by AFM, TEM, STEM and SEM.