Amyloid protein deposits are strongly associated with the pathology observed in Alzheimer’s disease, senile systemic amyloidosis, Parkinson’s disease, and other degenerative disorders. Although the proteins in each disease differ in sequence and native fold, and all have different normal biological functions, all can be triggered to misfold and self-associate into insoluble aggregates of cross-beta structure and fibrillar morphology. Because these different proteins, upon misfolding, adopt similar conformations, we wondered whether they could interact heterotypically as well as homotypically. In this talk I will describe two examples.
Regina Murphy from University of Wisconsin