Department of Biological Sciences

Research Overview

An increasing number of diseases are associated with misfolding of proteins, which can lead to the acummulation in vital organs of amorphous protein aggregates or ordered amyloid fibrils. These diseases include conditions such as Alzheimer's, Huntington's, Parkinson's and transmissible spongiform encephalopathies (TSEs). TSEs, such as mad cow disease in cattle, scrapie in sheep, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler-Scheinker disease (GSS) and fatal familial insomnia (FFI) in humans, are associated with the conversion of a cellular plasma membrane glycoprotein, the prion protein, to an altered form that is suggested to be both the infectious agent and the cause of rapid neurodegeneration. Structural studies have established that prion conversion from the cellular healthy conformation to the disease-associated form involves a major refolding of the prion protein that results in amorphous aggregates or ordered amyloid fibrils.

In my research group we are interested in understanding the molecular mechanism of prion conversion, studying the folding and structure of prions both in solution and in association with lipid membranes, the aggregation and fibrillization of prions, and the mechanisms of neurodegeneration and neuronal death.

Research interest groups:
Biophysics; Membranes and Transport; Neurosciences; Structural Biology;