Abstract
Prion diseases such as Creutzfeldt-Jakob or mad cow diseases originate from the misfolding and aggregation of proteins, with invariably lethal outcome. In this study we generate prion fibrils and investigate their structural properties by atomic force microscopy. Fibril shapes are analyzed statistically using worm-like chain models that describe the bending of semi-flexible polymers under thermal fluctuations. This way we quantify the mechanical properties of wild-type and mutant prion fibrils exhibiting highly diverse morphologies characterized by distinct bending rigidities and breakability. Acquiring such structural insights on prion misfolded forms will provide the appropriate tools to test experimentally the hypothesis of a link between the conformational stability of prion protein fibrils and their propensity to be toxic and infectious.View Large Image | View Hi-Res Image | Download PowerPoint Slide
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