Evaluation of 33-mer gliadin assemblies. Towards understanding its immunomodulator role in gliadin related diseases

M. G. HERRERA; LONEZ, C.; CELEJ. S; H. RITACCO; RUYSSCHAERT, J.; V. I. DODERO

Carlo Paz, Cordoba

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

Universidd Nacional de Cordoba

Gliadin, a protein present in wheat, rye and barley undergoes incomplete enzymatic degradation duringdigestion, producing several peptides. One of them is a 33-mer peptide, LQLQPF(PQPQLPY)3PQPQPF,a proline rich fragment which elicits an immune response in susceptible individuals and it is associated with gluten sensitivity and celiac disease[1]. Recently, our group has demonstrated that the 33-mer gliadin peptide is able to self-assemble into nanospheres which align into fractal linear arrays above a certain concentration under physiological conditions [2]. Herein, the evaluation of 33-mer self-assembly system by fluorescence spectroscopy techniques, ATR-FT-IR and DLS is presented. Interestingly, 33-mer assemblies are able to induce a transcription factor related to inflammatory reactions, in a dose dependent manner. Our results demonstrate a relation between 33-mer assemblies and inflammation, which can be relevant in the early steps of gliadin intoler ance disorders.