Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2008-11-14
pubmed:abstractText
Assembly of Amyloid beta (Abeta) peptides, in particular Abeta-42 is central to the formation of the amyloid plaques associated with neuro-pathologies such as Alzheimer's disease (AD). Molecular assembly of individual Abeta-42 species was observed using a simple fluorescence microscope. From the molecular movements (aka Brownian motion) of the individual peptide assemblies, we calculated a temporal evolution of the hydrodynamic radius (R(H)) of the peptide at physiological temperature and pH. The results clearly show a direct relationship between R(H) of Abeta-42 and incubation period, corresponding to the previously reported peptide's aggregation kinetics. The data correlates highly with in solution-based label-free electrochemical detection of the peptide's aggregation, and Abeta-42 deposited on a solid surface and analysed using atomic force microscopy (AFM). To the best of our knowledge, this is the first analysis and characterisation of Abeta aggregation based on capturing molecular trails of individual assemblies. The technique enables both real-time observation and a semi-quantitative distribution profile of the various stages of Abeta assembly, at microM peptide concentration. Our method is a promising candidate for real-time observation and analysis of the effect of other pathologically-relevant molecules such as metal ions on pathways to Abeta oligomerisation and aggregation. The method is also a promising screening tool for AD therapeutics that target Abeta assembly.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1090-2104
pubmed:author
pubmed:issnType
Electronic
pubmed:day
12
pubmed:volume
377
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
725-8
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Detection of Alzheimer's amyloid beta aggregation by capturing molecular trails of individual assemblies.
pubmed:affiliation
School of Materials Science, Japan Advanced Institute of Science and Technology, 1-1 Asahidai, Nomi City, Ishikawa 923-1292, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't