Espargaró Colomé, AlbaMedina, AinaDi Pietro, O.Muñoz-Torrero López-Ibarra, DiegoSabaté Lagunas, Raimon2016-05-192016-05-192016-03-222045-2322https://hdl.handle.net/2445/98697More 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.application/pdfengcc-by-nc-nd (c) Espargaró Colomé, Alba et al., 2016http://creativecommons.org/licenses/by-nc-nd/3.0/esMalaltia d'AlzheimerPèptidsAgregació (Química)Disseny de medicamentsAlzheimer's diseasePeptidesAggregation (Chemistry)Drug designinfo:eu-repo/semantics/article6587402016-05-19info:eu-repo/semantics/openAccess27000658