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

Allsop, David and Swanson, Linda and Moore, Susan and Davies, Yvonne and York, Amber and El-Agnaf, Omar M. A. and Soutar, Ian (2001) Fluorescence anisotropy:a method for early detection of Alzheimer β-peptide (Aβ) aggregation. Biochemical and Biophysical Research Communications, 285 (1). pp. 58-63. ISSN 1090-2104

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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.

Item Type: Article
Journal or Publication Title: Biochemical and Biophysical Research Communications
Uncontrolled Keywords: Alzheimer's disease ; amyloid ; Aβ ; fluorescein ; time-resolved fluorescence anisotropy
Subjects: Q Science > QH Natural history > QH301 Biology
Departments: Faculty of Health and Medicine > Biomedical & Life Sciences
Faculty of Science and Technology > Physics
Faculty of Science and Technology > Lancaster Environment Centre
ID Code: 8861
Deposited By: Prof David Allsop
Deposited On: 15 May 2008 11:43
Refereed?: Yes
Published?: Published
Last Modified: 26 Jul 2012 18:27
Identification Number:
URI: http://eprints.lancs.ac.uk/id/eprint/8861

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