In silico evaluation of the auto-agraggation of 33-mer Gliadin peptide

MARÍA J. AMUNDARAIN; FERNANDO ZAMARREÑO; JUAN FRANCISCO VISO; M. GEORGINA HERRERA; VERÓNICA DODERO; MARCELO D. COSTABEL

Villa Carlos Paz

Congreso; XLII Reunión Anual de la Sociedad Argentina de Biofísica; 2013

Sociedad Argentina de Biofísica

Molecular modelling methods represent essential tools to undertake the study of biological systems, providing a better understanding of both their structure and functionality. In this work we apply molecular dynamics simulations and electrostatic calculations to analyse the initial steps of auto-aggregation of 33-mer peptide. The fragment 33-mer is the result of the partial degradation of the protein α-gliadin. This protein, along with others of the same family, is found in gluten of grains which are toxic to people who suffer from coeliac disease. This peptide has been proposed to initiate the inflammation process that leads to the damage of epithelial cells of the small intestine. However, the molecular bases of this process are not well known yet. We are particularly interested in studying its ability of auto-aggregation into more complex structures, since different superstructures have been observed in vitro. Therefore, we have analysed three possible assemblies in water using GROMACS for the MD simulations and APBS to evaluate electrostatic interactions.