Our laboratory develops new methods to study the misfolding of amyloidogenic proteins, including α-synuclein, which has been implicated in the pathogenesis of Parkinson’s Disease.  We utilize unnatural amino acid mutagenesis, bioorthogonal labeling techniques, and protein ligation to produce homogenous α-synuclein labeled with fluorescent probes and photocrosslinkers.  Fluorescence and crosslinking measurements are used in combination with solid state NMR and cryo-EM data to generate models of misfolded forms of α-synuclein.  These models allow us to identify small molecules that bind to α-synuclein to prevent the formation of amyloid fibrils or to be used as imaging agents for the early identification of Parkinson’s Disease pathology.  We have also used fluorescently labeled α-synuclein to understand the mechanism of amyloid spread between neurons, which has the potential to identify new drug targets.  Taken together, our studies provide insight into the mechanism of α-synuclein toxicity in Parkinson’s Disease as well as the development of potential treatments.

Visualizing alpha-synuclein in Parkinson's disease: From all-atom models to <i>in vivo</i> imaging

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.

Visualizing alpha-synuclein in Parkinson's disease: From all-atom models to in vivo imaging