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

Mol Biosyst. 2012 Nov;8(11):2839-44. doi: 10.1039/c2mb25214g. Epub 2012 Aug 7.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amyloid / metabolism
  • Benzothiazoles
  • Flow Cytometry / methods*
  • Inclusion Bodies / metabolism
  • Protein Binding
  • Proteins / metabolism*
  • Thiazoles / chemistry*


  • Amyloid
  • Benzothiazoles
  • Proteins
  • Thiazoles
  • thioflavin T