In vitro, amyloid fibrils form through nucleation and growth, which requires a high concentration of the peptide or protein in the solution. Such conditions are missing in physiological conditions. An alternative route to the fibril growth is through surface-mediated self-assembly and growth, where under the right conditions a surface can help orient and unravel a protein and facilitate rapid diffusion, allowing the fibrils to grow.<br/><br/>In this presentation, I will demonstrate how under the right conditions, a flat surface can provide the template for rapid self-assembly through diffusion-limited aggregation, resulting in fibril growth within a few minutes. These studies show that on the surface, the alignment on the surface can reduce the barrier for nucleation and the enhanced diffusion, even for elongated fibrils contribute to the rapid self-assembly. I will discuss the role of this enhanced assembly in potential artifacts during imaging as well as their potential role in nucleating large fibrils in bulk.

Surface-mediated self-assembly as a route to nucleate amyloid fibril growth

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.