Thioflavin-S staining coupled to flow cytometry. A screening tool to detect in vivo protein aggregation

Alba Espargaró, Raimon Sabate, Salvador Ventura

Research output: Contribution to journalArticleResearchpeer-review

36 Citations (Scopus)

Abstract

Amyloid deposits are associated with an increasing number of human disorders, including Alzheimer's and Parkinson's diseases. Recent studies provide compelling evidence for the existence of amyloid-like conformations in the insoluble bacterial inclusion bodies (IBs) produced during the recombinant expression of amyloidogenic proteins. This makes prokaryotic cells a physiologically relevant system to study the mechanisms of in vivo amyloid deposition. We show here that the application of flow cytometry to detect Thioflavin-S (Th-S) fluorescence provides a fast, robust, quantitative, non-invasive method to screen for the presence of in vivo intracellular amyloid-like aggregates in bacteria, with potential application in the analysis of the impact of genetic mutations or chemical compounds on the aggregation of disease-associated polypeptides. © 2012 The Royal Society of Chemistry.
Original languageEnglish
Pages (from-to)2839-2844
JournalMolecular BioSystems
Volume8
DOIs
Publication statusPublished - 1 Nov 2012

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