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
N1 - Funding Information:
We thank The Alzheimer’s Disease Society, The Parkinson’s Disease Society UK (Dr. Omar El-Agnaf), and Lancaster University for financial support, and Peter Diggle for statistical advice.
PY - 2001
Y1 - 2001
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
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U2 - 10.1006/bbrc.2001.5123
DO - 10.1006/bbrc.2001.5123
M3 - Article
C2 - 11437372
AN - SCOPUS:0034789110
SN - 0006-291X
VL - 285
SP - 58
EP - 63
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -