Indefinite self-association of proteins and peptides results in formation of oligomeric assemblies of varied size, morphology, and function. Of particular interest, because of their connection to degenerative disease, is the self-assembly of amyloidogenic proteins into fibrillar aggregates. There is growing evidence that heterotypic interactions between different amyloidogenic proteins sometimes occur, and that such interactions can drastically change the outcome of homotypic interactions.Elucidation of the molecular basis for amyloidogenic interactions remains a challenging problem, which can best be addressed through careful selection of protein systems, and the use of multiple complementary biophysical and biochemical techniques. In this talk I will focus primarily on our use of fluorescence and light scattering methods to explore interactions between amyloid proteins, including recent work using single particle tracking. Two systems will be described: homotypic interactions of repeat-containing polypeptides, and heterotypic association of transthyretin (and transthyretin-derived peptides) with beta-amyloid.

Self- and non-self interactions of amyloidogenic proteins and peptides

247th National Meeting (2014)

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