prof.dr. Mireille Claessens: Alpha-synuclein self-assembly at multiple length scales
|Wanneer:||vr 23-01-2015 11:00 - 12:00|
Alpha-synuclein (aS) is a disordered protein that can self-assemble into filamentous structures called amyloid fibrils. aS fibrils are chemically and mechanically very stable, once formed they tend to cluster and form intracellular inclusions. The formation of such inclusions is a hallmark of Parkinson’s disease but their role in the disease process and the forces driving clustering remain elusive. Currently the discussion on the toxicity of aS aggregation focusses on soluble oligomeric aS aggregates instead of fibrils. Although aS oligomers are hypothesized to be toxic, the molecular architecture of these aggregates and the mechanisms by which they cause cell damage remain a mystery.In this presentation, I will summarize our recent work on the self-assembly of aS at multiple length scales and discuss how we used a broad repertoire of quantitative single molecule and ensemble biophysical techniques, to characterize aS amyloid micro- and nano-structures and their interactions with lipid membranes to obtain insight into possible disease mechanisms.