Single-molecule FRET studies on alpha-synuclein oligomerization of Parkinson's disease genetically related mutants.

ABSTRACT: Oligomers of alpha-synuclein are toxic to cells and have been proposed to play a key role in the etiopathogenesis of Parkinson's disease. As certain missense mutations in the gene encoding for alpha-synuclein induce early-onset forms of the disease, it has been suggested that these variants might have an inherent tendency to produce high concentrations of oligomers during aggregation, although a direct experimental evidence for this is still missing. We used single-molecule Förster Resonance Energy Transfer to visualize directly the protein self-assembly process by wild-type alpha-synuclein and A53T, A30P and E46K mutants and to compare the structural properties of the ensemble of oligomers generated. We found that the kinetics of oligomer formation correlates with the natural tendency of

SUBMITTER: Tosatto L 

PROVIDER: S-EPMC4652217 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature