Conception and study of periodic polymers modelled on the repetitive domain of wheat gliadins

Gliadins and glutenins contain a repetitive domain which might be involved in the macroscopic mechanical properties of gluten. In order to analyse the specific contribution of these domains we built synthetic genes encoding r epetitive amino acid blocks mimicking one of the consensus repeats found in gliadins tie Pro-Gln-Gln-Pro-Tyr (PQQPY)). Using a combination of cohesive and non cohesive ends, a convenient strateg y was deviced in order to design a gene family encoding (PQQPY)(8), (PQQPY) (16) and (PQQPY)(32). We optimized conditions for high level expression and purification of such peptides in Escherichia coli. After their obtention, the repetitive polypeptides were identified and further characterized by sp ectroscopic technics (UV and IR spectroscopy, circular dichroism).