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SUMMARY:Protein misfolding in Alzheimer's disease: a neuroscientist takes 
 lessons in biophysics - Dr Leila Luheshi\, University of Cambridge
DTSTART:20100203T103000Z
DTEND:20100203T113000Z
UID:TALK23009@talks.cam.ac.uk
CONTACT:8272
DESCRIPTION:Protein misfolding is a problem that lies at the heart of the 
 pathogenesis\nof many neurodegenerative disorders\, of which Alzheimer's D
 isease (AD) is\nthe most common. The misfolding of the Amyloid Beta peptid
 e\, which\naggregates and deposits in the brains of AD patients\, has been
  extensively\ncharacterised in vitro.  However\, it has proved more diffic
 ult to understand\nthe extent to which the mechanisms of amyloid beta aggr
 egation are conserved\nin vivo and how they relate to its role in the path
 ogenesis of AD.  Our\napproach to addressing this problem has been to take
  inspiration from the\nwork of biophysicists who have systematically and q
 uantitatively measured\nthe effects of intrinsic and extrinsic perturbatio
 ns of the amyloid beta\naggregation process in the test tube and apply the
  to a model of amyloid\nbeta aggregation in the brain of Drosophila.  We h
 ave made a large number of\nmanipulations of the aggregation of amyloid be
 ta in the Drosophila nervous\nsystem either by rational mutagenesis or thr
 ough the co-expression of\nconformation specific binding proteins and quan
 tified their effects on the\naggregation and neurotoxicity of the peptide.
   By combining this information\nwith more detailed biophysical observatio
 ns made of the effects of the same\nperturbations on amyloid beta aggregat
 ion in vitro we are beginning to\nunderstand which features of this proces
 s are responsible for\nneurodegeneration in AD.
LOCATION:Unilever Lecture Theatre\, Unilever Centre\, Department of Chemis
 try
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