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SUMMARY:α-Synuclein: amyloid inclusions and supra-fibrillar structures - 
  Prof. Mireille Claessens (University of Twente\, The Netherlands)
DTSTART:20160504T093000Z
DTEND:20160504T103000Z
UID:TALK66117@talks.cam.ac.uk
CONTACT:Jerome Charmet
DESCRIPTION:Alpha-synuclein (aS) is a disordered membrane binding protein 
 that plays a key role in the development of Parkinson's disease (PD). In P
 D aS self-assembles into filamentous structures called amyloid fibrils. Th
 ese fibrils are chemically and mechanically very stable. Once formed they 
 cluster into characteristic cellular inclusions such as Lewy bodies. The f
 orces driving inclusion body formation and their role in the disease patho
 logy remain elusive. Lewy body formation has been associated with both neu
 roprotection and toxicity. In this talk\, I will summarize our recent work
  on the accumulation aS in functionally different inclusions in cells and 
 on the forces driving self-assembly of aS fibrils in supra-fibrillar struc
 tures in vitro. I will discuss how we used a broad repertoire of biophysic
 al techniques to characterize aS amyloid micro- and nano-structures and ob
 tain insight into possible disease mechanisms.
LOCATION:Department of Chemistry\, Cambridge\, Unilever lecture theatre
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