TY - JOUR

T1 - Fluorescence anisotropy

T2 - a method for early detection of Alzheimer β-peptide (Aβ) aggregation.

AU - Allsop, David

AU - Swanson, Linda

AU - Moore, Susan

AU - Davies, Yvonne

AU - York, Amber

AU - El-Agnaf, Omar M. A.

AU - Soutar, Ian

PY - 2001/7/6

Y1 - 2001/7/6

N2 - 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.

AB - 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.

KW - Alzheimer's disease

KW - amyloid

KW - Aβ

KW - fluorescein

KW - time-resolved fluorescence anisotropy

U2 - 10.1006/bbrc.2001.5123

DO - 10.1006/bbrc.2001.5123

M3 - Journal article

VL - 285

SP - 58

EP - 63

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 1090-2104

IS - 1

ER -