UnderSTANDING THE molecular BASIS OF AMYLOID-ASSOCIATED NEURODEGENERATIVE DISEASES

Misfolding and aggregation of proteins into the amyloid state is associated with more than 50 human disorders, including neurodegenerative diseases such as Alzheimer’s and Parkinson’s, as well as type II diabetes and prion diseases. Currently, there is no cure for these amyloid-associated diseases and only limited treatment options are available. Furthermore, numerous anti-amyloid drugs have failed in clinical trials, demonstrating our lack of understanding of underlying disease mechanisms

Using structural biology and single molecule biophysical tools, I aim to elucidate the structures of amyloid aggregates could help identify key structural features such as specific folds, mutations or modifications that underlie the neurotoxicity of the aggregates and small oligomeric species and develop small molecule modulators of disease-associated amyloid aggregation.