INVESTIGADORES
SCHILARDI Patricia Laura
congresos y reuniones científicas
Título:
Atomic Force Microscopy and Electron Microscopy Studies of 33-mer Gliadin Peptide on silicon surface
Autor/es:
GEORGINA HERRERA; PATRICIA L. SCHILARDI; ROBERTO C. SALVAREZZA.; NADINE MILL; K. ROTT; ANDREAS HUTTEN; NORBERT SEWALD; VERÓNICA I. DODERO
Lugar:
Tucumán
Reunión:
Congreso; XLI Reunión Anual de la Sociedad Argentina de Biofísica; 2012
Resumen:
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.
References
1. Hadjivassiliou, M., Williamson, C. A. & Woodroofe, N. Trends Immunol. 25, 578-582
(2004).
2. Rubio-Tapia, A. & Murray, J. A. Curr. Opin. Gastroenterol. 26, 116-122 (2010).
3. A. Fasano, T. Shea-Donohue. Nature Clinical Practice Gastroenterology & Hepatology.2,
416-422 (2005).
4. M. Schumann, et. al., Gut.57, 747?54 (2008).
Acknowledgments
Supported by ANPCyT, DAAD, CONICET and UNS grants.