Fluorescence anisotropy: A method for early detection of Alzheimer β-peptide (Aβ) aggregation

David Allsop, Linda Swanson, Susan Moore, Yvonne Davies, Amber York, Omar M.A. El-Agnaf, Ian Soutar

Research output: Contribution to journalArticle

49 Citations (Scopus)

Abstract

Time-resolved anisotropy measurements (TRAMS) have been used to study the aggregation of the β-amyloid (Aβ) peptide which is suspected of playing a central role in the pathogenesis of Alzheimer's Disease (AD). The experiments, which employ small quantities of fluorescently-labelled Aβ, in addition to the untagged peptide, have shown that the sensitive TRAMS technique detects the presence of preformed "seed" particles in freshly prepared solutions of Aβ. More importantly, as 100 μM solutions of Aβ containing tagged Aβ at a concentration level of either 0.5 or 1 μM are incubated, the TRAMS prove capable of detection of the peptide aggregation process through the appearance of a continuously increasing "residual anisotropy" within the time-resolved fluorescence data. The method detects Aβ aggregation in its earliest stages, well before complexation becomes apparent in more conventional methods such as the thioflavin T fluorescence assay. The TRAMS approach promises to provide a most attractive route for establishment of a high-throughput procedure for the early detection of the presence of amyloid aggregates in the screening of biological samples.

Original languageEnglish
Pages (from-to)58-63
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume285
Issue number1
DOIs
Publication statusPublished - 1 Jan 2001

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Keywords

  • Alzheimer's disease
  • Amyloid
  • Fluorescein
  • Time-resolved fluorescence anisotropy

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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