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 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-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 Aβ 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 Aβ aggregation and the effect of potential anti-aggregating agents.
Highlights
More than 46 million people worldwide suffer from Alzheimer’s disease
amyloid β-peptide (Aβ) 42 aggregation kinetics have been analyzed to assess the effect of the inhibitors in both Aβ variants
In order to show the differences in the Th-S spectra of bacteria over-expressing or not Aβ as well as the potential tracking of amyloid formation in vivo, we measured the kinetics of induced and non-induced bacterial cultures in the presence and absence of inhibitors, by tracking the Th-S fluorescence spectra along the time in a range from 460 to 600 nm, exciting at 440 nm
Summary
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. The proposed method uses bacteria as an in vivo reservoir to track in real-time amyloid aggregation kinetics.
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