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- W2913403124 abstract "Abstract α-Synuclein is a protein that aggregates as amyloid fibrils in the brains of patients with Parkinson’s disease and dementia with Lewy bodies. Small oligomers of α-synuclein are neurotoxic and are thought to be closely associated with disease. Whereas α-synuclein fibrillization and fibril morphologies have been studied extensively with various methods, the earliest stages of aggregation and the properties of oligomeric intermediates are less well understood because few methods are able to detect and characterize early-stage aggregates. We used fluorescence spectroscopy to investigate the early stages of aggregation by studying pairwise interactions between α-synuclein monomers, as well as between engineered tandem oligomers of various sizes (dimers, tetramers, and octamers). The hydrodynamic radii of these engineered α-synuclein species were first determined by fluorescence correlation spectroscopy and dynamic light scattering. The rate of pairwise aggregation between different species was then monitored using dual-color fluorescence cross-correlation spectroscopy, measuring the extent of association between species labelled with different dyes at various time points during the early aggregation process. The aggregation rate and extent increased with tandem oligomer size. Self-association of the tandem oligomers was found to be the preferred pathway to form larger aggregates: interactions between oligomers occurred faster and to a greater extent than interactions between oligomers and monomers, indicating that the oligomers were not as efficient in seeding further aggregation by addition of monomers. These results suggest that oligomer-oligomer interactions may play an important role in driving aggregation during its early stages." @default.
- W2913403124 created "2019-02-21" @default.
- W2913403124 creator A5003998406 @default.
- W2913403124 creator A5013661873 @default.
- W2913403124 creator A5013883880 @default.
- W2913403124 creator A5020246704 @default.
- W2913403124 creator A5022834816 @default.
- W2913403124 creator A5034855510 @default.
- W2913403124 creator A5056078581 @default.
- W2913403124 date "2019-02-11" @default.
- W2913403124 modified "2023-10-18" @default.
- W2913403124 title "Early stages of aggregation of engineered α-synuclein monomers and oligomers in solution" @default.
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