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

Research output: Contribution to journalJournal article

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  • David Allsop
  • Linda Swanson
  • Susan Moore
  • Yvonne Davies
  • Amber York
  • Omar M. A. El-Agnaf
  • Ian Soutar
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<mark>Journal publication date</mark>6/07/2001
<mark>Journal</mark>Biochemical and Biophysical Research Communications
Issue number1
Volume285
Number of pages6
Pages (from-to)58-63
Publication statusPublished
Original languageEnglish

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.