NADH fluorescence lifetime is an endogenous reporter of α-synuclein aggregation in live cells.

ABSTRACT: α-Synuclein (aS) aggregation has been amply investigated for its involvement in Parkinson's disease because its amyloid fibrils are the main constituent of Lewy bodies, one of the hallmarks of the disease. aS aggregation was studied here in vitro and in cellular models to correlate aggregation products with toxicity mechanisms. Independent results published elsewhere suggested that aS overexpression and/or aggregation may impair cellular metabolism and cause mitochondrial damage. In this context, we report the characterization of changes in NADH fluorescence properties in vitro and in human embryonic kidney 293 cells upon aS aggregation. The application of the phasor approach to study NADH fluorescence lifetime and emission allowed us to identify changes that correlate with aS aggregation.

SUBMITTER: Plotegher N 

PROVIDER: S-EPMC4447231 | biostudies-literature | 2015 Jun

REPOSITORIES: biostudies-literature