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β-amyloid fibril formation is promoted by step edges of highly oriented pyrolytic graphite


Losic, D and Martin, LL and Aguilar, MI and Small, DH, β-amyloid fibril formation is promoted by step edges of highly oriented pyrolytic graphite, Biopolymers: Original Research on Biological Molecules and Assemblies, 84, (5) pp. 519-526. ISSN 0006-3525 (2006) [Refereed Article]

DOI: doi:10.1002/bip.20549


The aggregation of the amyloid--protein (A) is an important step in the pathogenesis of Alzheimer's disease. As A fibrils are not found in all brain regions, endogenous factors may influence A fibril formation. In this study, atomic force microscopy was used to investigate the role of surface phenomena in directing amyloid aggregation. A1-40 was applied to a surface of highly oriented pyrolytic graphite at a concentration of 0.5 M. Steps formed by edge-plane surface defects on the graphite were found to act as a template to promote the assembly of A into fibrils. Initially, after being deposited on the graphite surface, A had a uniform beaded morphology. However, after incubating (aging) the A on the surface for several hours, the A assembled along step edges to form linear aggregates. After more prolonged incubation, the linear A aggregates fused to form mature fibrils with a distinctive helical morphology. The results demonstrate that surface interactions can promote the aggregation of A into amyloid fibrils and they suggest that similar interactions could promote amyloid aggregation in vivo.

Item Details

Item Type:Refereed Article
Research Division:Biomedical and Clinical Sciences
Research Group:Neurosciences
Research Field:Neurosciences not elsewhere classified
Objective Division:Health
Objective Group:Clinical health
Objective Field:Clinical health not elsewhere classified
UTAS Author:Small, DH (Professor David Small)
ID Code:61097
Year Published:2006
Web of Science® Times Cited:42
Deposited By:Menzies Institute for Medical Research
Deposited On:2010-02-25
Last Modified:2010-09-16

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