Tuomas P. J. Knowles
University of Cambridge, Department of Chemistry, UK
Filamentous protein aggregation underlies a number of functional and pathological processes in nature. This talk focuses on the formation of amyloid fibrils, a class of beta-sheet rich protein filament. Such structures were initially discovered in the context of disease states where their uncontrolled formation impedes normal cellular function, but are now known to also possess numerous beneficial roles in organisms ranging from bacteria to humans. The formation of these structures commonly occurs through supra-molecular polymerisation following an initial primary nucleation step. In recent years it has become apparent that in addition to primary nucleation, secondary nucleation events which are catalysed in the presence of existing aggregates can play a significant role in the dynamics of such systems. This talk describes our efforts to understand the nature of the nucleation processes in protein aggregation as well as the dynamics of such systems and how these features connect to the biological roles that these structures can have in both health and disease.