Dresden 2017 – wissenschaftliches Programm

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BP: Fachverband Biologische Physik

BP 56: Protein Structure and Dynamics

BP 56.1: Hauptvortrag

Donnerstag, 23. März 2017, 15:00–15:30, SCH A251

Biophysical Studies of Amyloid Formation and Its Inhibition — •Sheena Radford — The University of Leeds

Amyloid formation involves the polymerisation of proteins and peptides into polymers with a cross-beta fold. How amyloid formation causes disease, and identifying the culprit species involved, remain a significant challenge. This results from the complexity of the aggregation process and the fact that amyloid assembly is initiated by non-native states of proteins that are partially folded or intrinsically disordered. Structure determination is thus difficult, and identifying the interacting surfaces in these transiently formed and dynamic ensembles is challenging. In this lecture I will describe our recent attempts to discover new insights into how proteins aggregate into amyloid and how to prevent cellular dysfunction caused by amyloid assembly/disassembly mechanisms using a number of different strategies. Specifically, I will show how we have used different biophysical and biochemical approaches to map the nature of the earliest protein-protein interactions in amyloid assembly and to re-assess the potential role(s) of fibrils in disease. Finally, using a novel screen developed with E.coli, we have been able to discover new highly potent inhibitors of aggregation for some of the most highly aggregating protein sequences known.