LAUSR

Amylin is a 37 residue intrinsically disordered protein whose aggregation is associated with Type II diabetes. For most amyloid aggregates, the intermediate aggregations states (“oligomers”) are supposed to be more toxic than the mature fibrillar state, and interaction with the cell membrane is an important component of the toxicity. It is likely that the origin of amylin toxicity is linked to the conformational changes which occur as the peptide undergoes the aggregation process. Here we probe the membrane affinity and the conformation of the peptide as a function of its aggregation state.