The Parkinson's disease (PD) associated protein α-synuclein (aSyn) can form macroscopic intracellular inclusions of protein aggregates in vivo. In vitro monomeric aSyn aggregates into fibrillar protein amyloids called pre-formed fibrils (PFF). PFF possess autocatalytic activity and function as templates for monomeric aSyn to aggregate into PFF. Several distinct PFF polymorphs that differ in morphology, stability and structure were described in detail. Recently two structural cryo-electron microscopy models of the fibrillar core of a high salt in vitro aSyn polymorph were published providing structural insights at atomic resolution. The in vitro seeding activity as well as the fibril morphology might be linked to the in vivo prion-like spreading and propagation of Parkinson's disease (PD) in the central nervous system (CNS) and therefore biologically highly relevant. Here we show detailed biochemical and structural characterization of an in vitro aSyn polymorph seeded by PFF under controlled aggregation conditions using fluorescent dye binding as well as HD exchange coupled to NMR spectroscopy.

Analysis of α-synuclein fibril structure by fluorescent dyes and NMR spectroscopy

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.