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


ABSTRACT: Parkinson's disease is characterized by the accumulation of protein aggregates in the brain, termed Lewy bodies. Lewy bodies are predominantly composed of α-synuclein and mutations that increase the aggregation potential of α-synuclein have been associated with early on-set disease. Assays capable of reporting on the solubility of α-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 α-synuclein. Herein, we repurpose our previously reported self-assembling NanoLuc luciferase fragments to engineer a platform for detecting α-synuclein solubility in living cells. This new assay is capable of reporting on changes in α-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 α-synuclein solubility as well as identify potential tool compounds capable of modulating α-synuclein aggregation.

SUBMITTER: Nelson TJ 

PROVIDER: S-EPMC7266166 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature

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

Nelson Travis J TJ   Truong Tiffany T   Truong BaoLong B   Bilyeu Camden V CV   Zhao Jia J   Stains Cliff I CI  

RSC advances 20200428 28


Parkinson's disease is characterized by the accumulation of protein aggregates in the brain, termed Lewy bodies. Lewy bodies are predominantly composed of α-synuclein and mutations that increase the aggregation potential of α-synuclein have been associated with early on-set disease. Assays capable of reporting on the solubility of α-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 th  ...[more]

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