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

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

Congreso; XLII Reunion Anual de la Sociedad Argentiina de Biofísica; 2013

Gliadin, a protein present in wheat, rye and barley undergoes incomplete enzymatic degradation during digestion, 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 NFkB, 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 intolerance disorders. Acknowledgements:Supported by UNS, CONICET, DAAD, and ME-SPU (17-16-296) grants. References: (1)Sapone, A. et al. BMC Medicine. 2012, 10:13. (2)Herrera, M. G., Zamarreño, F., Costabel, M., Ritacco, H., Hütten, A., Sewald, N., Dodero, V. I. Biopolymers. 2013, in press.