Considerable progress has been made, using experiments and computations, to decipher the general principles governing the mechanism of formation of oligomers and fibrils of amyloid proteins implicated in diseases, including the amyloid-β protein (Aβ) associated with Alzheimer's disease (AD). However, the identification of the link between protein aggregation and the systems of disease at the molecular level has proved elusive. The biogenesis of Aβ starts with interaction of the Amyloid Precursor Protein (APP) with secretases in the presence of membrane. Subsequently, a variety of intermolecular interactions influence the route to oligomer formation and the extent of cytotoxicity. I will discuss ongoing work to systematically investigate the biogenesis of Aβ, its propensity toward aggregation, and putative mechanisms of cytotoxicity in order to highlight critical areas for future research.

Probing the principles governing protein assembly and amyloid aggregation

ACS Spring Meeting 2021

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