In Parkinson’s disease (PD), alpha-Synuclein aggregates to Lewy bodies, which are connected to neuronal dysfunction and death, similar to Abeta and tau in Alzheimer’s (AD), prion protein in Creutzfeldt Jacob and IAPP in Type II diabetes mellitus (T2DM). Using structural biology derived predictions (1), alpha-Synuclein is shown to form non-toxic intrinsically disordered monomers and non-toxic fibrils, while immediate toxicity is exerted by oligomers (2). Prevention of formation of these toxic oligomers by small molecules, specifically anle138b, observed in vitro and in vivo (3) using ultracentrifugation or superresolution imaging (4), specifically anle138b, leads to neuroprotection and restoration of functionality of the neurons in all mentioned diseases, specifically in PD (3,4), MSA (5), AD based on tau (6) or Abeta<sub>42</sub> overexpression (7) and T2DM (8). Biophysical characterization of anle138b with target proteins will be discussed (6,9) in solution and in membranes with NMR spectroscopy.

Modulation of aggregating proteins studied by NMR and beyond in neuro- and cellular degeneration

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.