Evaluation of the impact of protein aggregation on cellular oxidative stress in yeast

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© 2018, Journal of Visualized Experiments. All rights reserved. Protein misfolding and aggregation into amyloid conformations have been related to the onset and progression of several neurodegenerative diseases. However, there is still little information about how insoluble protein aggregates exert their toxic effects in vivo. Simple prokaryotic and eukaryotic model organisms, such as bacteria and yeast, have contributed significantly to our present understanding of the mechanisms behind the intracellular amyloid formation, aggregates propagation, and toxicity. In this protocol, the use of yeast is described as a model to dissect the relationship between the formation of protein aggregates and their impact on cellular oxidative stress. The method combines the detection of the intracellular soluble/aggregated state of an amyloidogenic protein with the quantification of the cellular oxidative damage resulting from its expression using flow cytometry (FC). This approach is simple, fast, and quantitative. The study illustrates the technique by correlating the cellular oxidative stress caused by a large set of amyloid-β peptide variants with their respective intrinsic aggregation propensities.
Original languageEnglish
Article numbere57470
JournalJournal of Visualized Experiments
Issue number136
Publication statusPublished - 23 Jun 2018


  • Amyloid peptide
  • Biochemistry
  • Flow cytometry
  • Green fluorescent protein
  • Issue 136
  • Oxidative stress
  • Protein aggregation
  • Protein inclusions
  • Yeast


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