Our laboratory works on the cutting edge to understand Prion diseases from many different angles. Below are brief descriptions of the project areas of the lab:
Several classes of amyloid-directed compounds have been shown to inhibit a-synuclein (a-syn) aggregation and been investigated as potential new drugs, despite this, not a single molecule has reached the market.
The underlying conversion mechanism of PrPC into PrPSc is poorly understood and it is further complicated by the existence of several different strains characterized by distinct tertiary and quaternary structures as well as different clinical patterns.
A prerequisite for understanding Prion Diseases is unraveling the molecular mechanism leading to the detrimental conversion process wherein the α-helical motifs of the cellular prion protein (PrPC) are replaced by β-sheets in the disease-causing form (PrPSc).
The cellular prion protein (PrPC) has been extensively investigated since its conformational isoform, the prion, was identified as the causative agent of prion disorders.
