Regensburg 2010 – scientific programme

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SYMR: Symposium Nuclear Magnetic Resonance: from Applications in Condensed-Matter Physics to New Frontiers

SYMR 4: SYMR Nuclear Magnetic Resonance: From Applications in Condensed Matter Physics to New Frontiers

SYMR 4.6: Invited Talk

Tuesday, March 23, 2010, 12:15–12:45, H1

Life on the Edge: The Origins and Proliferation of Protein Misfolding Diseases — •Chistopher M. Dobson — University of Cambridge, Department of Chemistry, Lensfield Road, Cambridge CB2 1EW, UK

The failure of proteins to fold, or to remain correctly folded, can give rise to serious cellular malfunctions that frequently lead to disease. One particularly important group of such diseases is associated with the aggregation of misfolded proteins into thread-like structures known as amyloid fibrils, and includes disorders ranging from Alzheimer's disease to late-onset diabetes. The manner in which the normal soluble forms of peptides and proteins can convert into these pathogenic amyloid structures is being uncovered by a wide variety of in vitro experimental studies along with theoretical simulations and bioinformatics studies [Dobson and Chiti, Annu. Rev. Biochem. 75, 333-366 (2006)]. As with folding, these studies are increasingly being linked to events occurring in vivo using a variety of strategies. Of particular interest are experiments designed to link the principles of misfolding and aggregation to the effects of such processes in model organisms such as Drosophila (the fruit fly). This talk will try to draw together some of the ideas that are emerging from recent in our laboratory based on NMR spectroscopy, including evidence for the extremely narrow boundary between normal and aberrant behaviour [Tartaglia et al., Trends Biochem. Soc. 32, 204-206 (2007)], and how this concept sheds light on the origin, current proliferation and potential means of prevention of the associated diseases.