Alzheimer’s Disease (AD) is currently the sixth leading cause of death in the United States. This is an irreversible neurodegenerative disease that leads to the loss of memory, thinking abilities, and simple task capabilities. The onset of Alzheimer’s Disease is initiated by the amyloid precursor protein (APP) after cleaving to form amyloid beta peptides (Aβ-42) that aggregate as hydrophobic beta sheets during post-translational modification as a result of oxidative stress in the brain. AD patients have been found to have high concentrations of heavy metals in the brain, including Cu2+, which can bind to the primary structure of Aβ-42 and create plaques in the brain. The work presented here focuses on quantifying the in vitro formation of amyloid monomers, trimers, tetramers, oligomers, and plaques in the presence of differing copper chelating compounds using native PAGE, hydroxyl radical trapping, and cyclic voltammetry. In vivo paralysis assays were carried out in Caenorhabditis elegans (C. elegans) expressing Aβ-42 and a control strain to further study the formation of amyloid plaques and the impact of copper chelating ligands.

Investigating the effects of copper and copper chelates on amyloid beta peptide aggregation and neurotoxicity in vitro and in vivo using C. elegans

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.