Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2006-9-12
pubmed:abstractText
The aggregation of the amyloid-beta-protein (Abeta) is an important step in the pathogenesis of Alzheimer's disease. As Abeta fibrils are not found in all brain regions, endogenous factors may influence Abeta fibril formation. In this study, atomic force microscopy was used to investigate the role of surface phenomena in directing amyloid aggregation. Abeta1-40 was applied to a surface of highly oriented pyrolytic graphite at a concentration of 0.5 microM. Steps formed by edge-plane surface defects on the graphite were found to act as a template to promote the assembly of Abeta into fibrils. Initially, after being deposited on the graphite surface, Abeta had a uniform beaded morphology. However, after incubating (aging) the Abeta on the surface for several hours, the Abeta assembled along step edges to form linear aggregates. After more prolonged incubation, the linear Abeta aggregates fused to form mature fibrils with a distinctive helical morphology. The results demonstrate that surface interactions can promote the aggregation of Abeta into amyloid fibrils and they suggest that similar interactions could promote amyloid aggregation in vivo.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0006-3525
pubmed:author
pubmed:copyrightInfo
(c) 2006 Wiley Periodicals, Inc.
pubmed:issnType
Print
pubmed:volume
84
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
519-26
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Beta-amyloid fibril formation is promoted by step edges of highly oriented pyrolytic graphite.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, Monash University, Victoria 3800, Australia.
pubmed:publicationType
Journal Article