A luminescence-based assay for monitoring changes in alpha-synuclein aggregation in living cells

Travis J. Nelson, Tiffany Truong, Bao Long Truong, Camden V. Bilyeu, Jia Zhao, Cliff I. Stains

Research output: Contribution to journalArticle

1 Scopus citations

Abstract

Parkinson's disease is characterized by the accumulation of protein aggregates in the brain, termed Lewy bodies. Lewy bodies are predominantly composed of a-synuclein and mutations that increase the aggregation potential of a-synuclein have been associated with early on-set disease. Assays capable of reporting on the solubility of a-synuclein in living cells could provide a means to interrogate the influence of mutations on aggregation as well as identify small molecules capable of modulating the aggregation of a-synuclein. Herein, we repurpose our previously reported self-assembling NanoLuc luciferase fragments to engineer a platform for detecting a-synuclein solubility in living cells. This new assay is capable of reporting on changes in a-synuclein solubility caused by disease-relevant mutations as well as inhibitors of aggregation. In the long term, this new assay platform provides a means to investigate the influence of mutations on a-synuclein solubility as well as identify potential tool compounds capable of modulating a-synuclein aggregation.

Original languageEnglish (US)
Pages (from-to)16675-16678
Number of pages4
JournalRSC Advances
Volume10
Issue number28
DOIs
StatePublished - Apr 28 2020

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

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