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Ultra rapid in vivo screening for anti-Alzheimer anti-amyloid drugs.


ABSTRACT: More than 46 million people worldwide suffer from Alzheimer's disease. A large number of potential treatments have been proposed; among these, the inhibition of the aggregation of amyloid ?-peptide (A?), considered one of the main culprits in Alzheimer's disease. Limitations in monitoring the aggregation of A? in cells and tissues restrict the screening of anti-amyloid drugs to in vitro studies in most cases. We have developed a simple but powerful method to track A? aggregation in vivo in real-time, using bacteria as in vivo amyloid reservoir. We use the specific amyloid dye Thioflavin-S (Th-S) to stain bacterial inclusion bodies (IBs), in this case mainly formed of A? in amyloid conformation. Th-S binding to amyloids leads to an increment of fluorescence that can be monitored. The quantification of the Th-S fluorescence along the time allows tracking A? aggregation and the effect of potential anti-aggregating agents.

SUBMITTER: Espargaro A 

PROVIDER: S-EPMC4802339 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature

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Ultra rapid in vivo screening for anti-Alzheimer anti-amyloid drugs.

Espargaró Alba A   Medina Aina A   Di Pietro Ornella O   Muñoz-Torrero Diego D   Sabate Raimon R  

Scientific reports 20160322


More than 46 million people worldwide suffer from Alzheimer's disease. A large number of potential treatments have been proposed; among these, the inhibition of the aggregation of amyloid β-peptide (Aβ), considered one of the main culprits in Alzheimer's disease. Limitations in monitoring the aggregation of Aβ in cells and tissues restrict the screening of anti-amyloid drugs to in vitro studies in most cases. We have developed a simple but powerful method to track Aβ aggregation in vivo in real-  ...[more]

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