Evaluation of 33-mer gliadin peptide oligomerization: A fluorescence and microscopy study.

HERRERA, M.G; CELEJ, M. S; SCHILARDI. P.L; DODERO.V.I

Sierra de la Ventana

Congreso; XLIII Reunión Anual de la Sociedad Argentina de Biofísica; 2014

33-mer peptide, LQLQPF(PQPQLPY)3PQPQPF, is a proteolytic resistance fragment of gliadin protein present in wheat, rye and barley (1, 2). It is known that 33-mer is able to cross the gut mucosa and trigger an immune response in sensible individuals; however the mechanism involved in these processes remains unclear (2,3). Previously, we reported that 33-mer is able to oligomerize depending on peptide concentration (4). Here, we took advantage of the presence of three tyrosines (Y) in the 33-mer peptide sequence to perform fluorescence experiments to obtain information about the mechanism involved in solution. In particularly anisotropy and time-resolved studies are presented. The different oligomerization stages are detected by AFM.References: (1)Shan, L., et. al. Science, 2002, 2275.(2) Shan, L., et. al. J. Proteome. Res., 2005, 1732.(3)Hadjivassiliou, M., et. al. Trends Immunol., 2004, 578.(4) Herrera, M.et.; al. Biopolymers, 2013, 96.