Several degenerative diseases are associated to the deposition of protein aggregates. Examples include the amyloid aggregates of amyloid-beta peptide, alpha-synuclein, prion protein, and islet amyloid polypeptide (IAPP), which are associated to Alzheimer, Parkinson, prion diseases, and type 2 diabetes, respectively. In most cases, essential metal ion homeostasis is impaired, while direct metal-protein interactions clearly impact the amyloid aggregation of the implicated proteins in vitro. Our research group studies the interaction of copper ions with these amyloidogenic proteins, using spectroscopic tools to understand the impact of the metal ion in protein folding and aggregation. This presentation will provide an overview of the lessons learned from studying the interaction of Cu ions with alpha-synuclein, the amyloid-beta peptide, prion protein fragments, and IAPP. These proteins/peptides are intrinsically disordered and have the flexibility to accommodate the preferred coordination and geometric preferences of the metal ion. However, the location of the copper binding sites in relation to the hydrophobic residues that drive aggregation plays a key role in the mechanism of amyloid formation and how it is impacted by the metal ion.  Overall, these stories provide important structural insights into the bioinorganic chemistry of these degenerative diseases.

Metal ion binding to proteins and its impact in amyloid aggregation

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.