Towards the understanding of the early stages of gliadin intolerance disorders using a supramolecular perspective.

HERRERA. M.G; BENEDINI, L.A.; VEUTHEY . T; LONEZ, C; HELLWEG, T.; RUYSSCHAERT , J-M; DODERO.V.I

Capital Federal

Congreso; Ubiquitin and ubiquitin like proteins: at the crossroads from chromatin to protein; 2014

Gliadin, a protein present in wheat, rye and barley undergoes incomplete enzymatic degradationduring digestion, producing several peptides. One of them is a 33-mer peptide,LQLQPF(PQPQLPY)3PQPQPF, a proline-rich fragment which is associated with gluten sensitivityand celiac disease (CD) (1). The initial pathogenic mechanism is still unknown, however, it is clearthat the immune system is involved. In this regard, CD is associated with the presence of one copyof the HLA-DQ2 heterodimer and less frequently in 6% of the patients with the HLA-DQ8molecule. The up regulation of Ubiquitin D (UBD) is associated with intestinal mucosa of activeCD (2). Recently, our group demonstrated that the 33-mer gliadin peptide is able to self- assembleinto spherical and linear oligomers under physiological conditions. A conformational transition fromPPII to beta-sheet was observed during the self-assembly process (3). Our recent results show aconnection between 33-mer supramolecular assemblies and inflammation, which can be relevant inthe early steps of gliadin intolerance disorders. A supramolecular perspective is presented. Acknowledgements: Supported by UNS, CONICET, DAAD, and SPU grants.References:(1) Sapone, A. et al. BMC Medicine. 2012, 10:13.(2) Liu, J. et.al. Am. J. Hum. Genet. 2002, 70(1):51.(3) M. G. Herrera, et.al. Biopolymers. 2014, 101(1):96.