Protein misfolding in Alzheimer's disease: a neuroscientist takes lessons in biophysics

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• Dr Leila Luheshi, University of Cambridge
• Wednesday 03 February 2010, 10:30-11:30
• Unilever Lecture Theatre, Unilever Centre, Department of Chemistry.

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Canceled

Protein misfolding is a problem that lies at the heart of the pathogenesis of many neurodegenerative disorders, of which Alzheimer’s Disease (AD) is the most common. The misfolding of the Amyloid Beta peptide, which aggregates and deposits in the brains of AD patients, has been extensively characterised in vitro. However, it has proved more difficult to understand the extent to which the mechanisms of amyloid beta aggregation are conserved in vivo and how they relate to its role in the pathogenesis of AD. Our approach to addressing this problem has been to take inspiration from the work of biophysicists who have systematically and quantitatively measured the effects of intrinsic and extrinsic perturbations of the amyloid beta aggregation process in the test tube and apply the to a model of amyloid beta aggregation in the brain of Drosophila. We have made a large number of manipulations of the aggregation of amyloid beta in the Drosophila nervous system either by rational mutagenesis or through the co-expression of conformation specific binding proteins and quantified their effects on the aggregation and neurotoxicity of the peptide. By combining this information with more detailed biophysical observations made of the effects of the same perturbations on amyloid beta aggregation in vitro we are beginning to understand which features of this process are responsible for neurodegeneration in AD.

This talk is part of the Biophysics Colloquia - (Chemistry) series.

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