Polycation-induced Oligomerization and Accelerated Fibrillation of Human α-synuclein in Vitro
Document Type
Article
Publication Date
2009
Digital Object Identifier (DOI)
https://doi.org/10.1110/ps.0230903
Abstract
The aggregation and fibrillation of α-synuclein has been implicated as a causative factor in Parkinson's disease and several other neurodegenerative disorders known as synucleinopathies. The effect of different factors on the process of fibril formation has been intensively studied in vitro. We show here that α-synuclein interacts with different unstructured polycations (spermine, polylysine, polyarginine, and polyethyleneimine) to form specific complexes. In addition, the polycations catalyze α-synuclein oligomerization. The formation of α-synuclein–polycation complexes was not accompanied by significant structural changes in α-synuclein. However, α-synuclein fibrillation was dramatically accelerated in the presence of polycations. The magnitude of the accelerating effect depended on the nature of the polymer, its length, and concentration. The results illustrate the potential critical role of electrostatic interactions in protein aggregation, and the potential role of naturally occurring polycations in modulating α-synuclein aggregation.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Protein Science, v. 12, issue 4, p. 702-707
Scholar Commons Citation
Goers, John; Uversky, Vladimir N.; and Fink, Anthony L., "Polycation-induced Oligomerization and Accelerated Fibrillation of Human α-synuclein in Vitro" (2009). Molecular Medicine Faculty Publications. 704.
https://digitalcommons.usf.edu/mme_facpub/704
