In vivo amyloid aggregation kinetics tracked by time-lapse confocal microscopy in real-time

Anna Villar-Piqué, Alba Espargaró, Salvador Ventura, Raimon Sabate

Research output: Contribution to journalArticleResearchpeer-review

9 Citations (Scopus)

Abstract

© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. Amyloid polymerization underlies an increasing number of human diseases. Despite this process having been studied extensively in vitro, aggregation is a difficult process to track in vivo due to methodological limitations and the slow kinetics of aggregation reactions in cells and tissues. Herein we exploit the amyloid properties of the inclusions bodies (IBs) formed by amyloidogenic proteins in bacteria to address the kinetics of in vivo amyloid aggregation. To this aim we used time-lapse confocal microscopy and a fusion of the amyloid-beta peptide (A β42) with a fluorescent reporter. This strategy allowed us to follow the intracellular kinetics of amyloid-like aggregation in real-time and to discriminate between variants exhibiting different in vivo aggregation propensity. Overall, the approach opens the possibility to assess the impact of point mutations as well as potential anti-aggregation drugs in the process of amyloid formation in living cells.
Original languageEnglish
Pages (from-to)172-177
JournalBiotechnology Journal
Volume11
Issue number1
DOIs
Publication statusPublished - 1 Jan 2016

Keywords

  • Aggregation kinetics
  • Amyloid aggregation
  • Aβ peptide
  • Fibril formation
  • Inclusion bodies

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