Amyloid formation: interface influence

Hamley, I. W. ORCID: https://orcid.org/0000-0002-4549-0926 (2010) Amyloid formation: interface influence. Nature Chemistry, 2. pp. 707-708. ISSN 1755-4330 doi: 10.1038/nchem.816

Abstract/Summary

The causes of pathological conditions such as Alzheimer’s and Parkinson’s diseases are becoming better understood. Proteins that misfold from their native structure to form aggregates of β-sheet fibrils — termed amyloid — are known1,2 to be implicated in these ‘amyloid diseases’. Understanding the early steps of fibril formation is critical, and the conditions, mechanism and kinetics of protein and peptide aggregation are being widely investigated through a variety of in vitro studies. Kinetic aspects of the dispersion of the protein or peptide in solution are thought to influence the fibrillization process by mass-transfer effects. In addition, mixing also leads to shear forces, which can influence fibril growth by perturbing the equilibrium between the isolated and aggregated proteins, causing existing fibrils to fragment and create new nuclei3. Writing in the Journal of the American Chemical Society, David Talaga and co-workers have now highlighted4 an additional factor that can influence the fibrillization of amyloid-forming proteins — the presence of hydrophobic interfaces.

Item Type	Article
URI	https://reading-clone.eprints-hosting.org/id/eprint/17126
Identification Number/DOI	10.1038/nchem.816
Refereed	Yes
Divisions	Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
Publisher	Nature Publishing Group
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