Amyloidogenic proteins such as prion protein (PrP) are linked to human diseases like morbus Alzheimer, Parkinson's disease, new variant Creutzfeldt Jacob disease (nvCJD), and bovine spongiform encephalopathy (BSE; mad cow disease).
The focus of our work is the study of conformational properties and stability of PrP. PrP is highly conserved in many animal species and is found in a soluble, cellular form (PrPC) and in an infectious, pathogenic form (PrPSc). PrPC and PrPSc are of identical sequence but differ in spatial structure. Our primary goal is to rationally design molecules that interfere with the conformational transition from PrPC into PrPSc or that dissolve amyloidogenic prion plaques. To this end, we need to understand the mechanism of the pathogenic conformational change. Further, we are working on the characterization of structure and stability of PrP bound to other molecules, either potential anti-prion drugs or PrP binding proteins.
A special safety level S2-laboratory allows preparation and handling of recombinant PrP.