Molecular Chaperones as Therapeutic Targets for Parkinson's Disease

Molecular chaperone proteins are used by cells to promote correct protein folding, or to target misfolded proteins for degradation. The lab has previously shown that molecular chaperone proteins colocalize with alpha-synuclein in Lewy bodies and that alpha-synuclein aggregation and toxicity can be prevented by co-expressing molecular chaperones. These studies utilize cell-based models of alpha-synuclein aggregation and toxicity as well as whole-animal models.

Current projects focus on the role of chaperone proteins in alpha-synuclein induced toxicity, aggregation and clearance. This includes studies in collaboration with Pfizer to investigate the effect of novel inhibitors that alter levels of molecular chaperones in the brain for their ability to stop alpha-synuclein toxicity and aggregation — thus, preventing neurons from dying in the brain.