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

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

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 remain unclear (2, 3). Previously, we reported that 33-mer oligomerizes depending on peptide concentration (4). Here, we took advantage of the presence of three tyrosines (Y) in the 33-mer peptide sequence to perform anisotropy and time-resolved fluorescence studies in order to obtain information about the mechanism of peptide self-assembly in solution.. The different oligomerization stages were also appraised by complementary atomic force microscopy experiments. Acknowledgements: We thank Dr. G. Montich for allowing us to use the TCSPC lifetime equipment. 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