We apply tools of structural biology, biophysics, biochemistry, molecular biology and bio-computing to an understanding of the mechanisms of BSE, TSE and other diseases of protein misfolding.
Misfolded prions cause a variety of fatal neurodegenerative diseases in both animals and humans.
Dr. David Wishart
Athabasca Hall 3-41
Welcome to the Prion Structure, Function & Dynamics Project
The Prion Structure, Function & Dynamics Project is a collaboration between researchers from the University of Alberta, the University of Toronto and the University of British Columbia. Our goal is study the structure, function and dynamics of the Prion protein.
Prions are the causative agents of a number of incurable neurodegenerative diseases including "mad cow" disease (for cattle), scrapie (for sheep), chronic wasting disease (for deer) and Creutzfeld Jacob disease (for humans). Prions are not viruses or bacteria, but are actually naturally occurring proteins that are found in just about every animal on earth, including humans. Occasionally these normal prion proteins (called PrPc) spontaneously unfold or misfold. If they do, they start propagating or passing on their unfolded state to other "normal" prions, leading to a molecular avalanche of normal prions being rapidly converted to misfolded prions. These misfolded prions (called PrPsc) form large, insoluble aggregates (like curds in curdled milk). The presence of large amounts of PrPsc, especially in brain cells leads to cell death, rapid neural degeneration and classic manifestations of prion disease.
Research into the behaviour of prion diseases will eventually lead to earlier diagnosis and treatment in all mammals afflicted by their associated diseases. To make progress towards this greater goal, the Prion Project brings together top researchers from three universities and from a variety of disciplines to study the structure, function & dynamics of the Prion protein.