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cc-by-nc-nd (c) Espargaró Colomé, Alba et al., 2016
Si us plau utilitzeu sempre aquest identificador per citar o enllaçar aquest document: https://hdl.handle.net/2445/98697

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

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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 realtime, 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 antiaggregating agents.

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ESPARGARÓ COLOMÉ, Alba, et al. Ultra rapid in vivo screening for anti-Alzheimer anti-amyloid drugs. Scientific Reports. 2016. Vol. 6, num. 23349. ISSN 2045-2322. [consulted: 17 of August of 2026]. Available at: https://hdl.handle.net/2445/98697

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