Nitration Inhibits Fibrillation of Human α-synuclein in Vitro by Formation of Soluble Oligomers
Document Type
Article
Publication Date
2003
Digital Object Identifier (DOI)
https://doi.org/10.1016/S0014-5793(03)00367-3
Abstract
The aggregation of α-synuclein in dopaminergic neurons is a critical factor in the etiology of Parkinson's disease (PD). Oxidative and nitrative stress is also implicated in PD. We examined the effect of nitration on the propensity of α-synuclein to fibrillate in vitro. Fibril formation of α-synuclein was completely inhibited by nitration, due to the formation of stable soluble oligomers (apparently octamers). More importantly the presence of sub-stoichiometric concentrations of nitrated α-synuclein led to inhibition of fibrillation of non-modified α-synuclein. These observations suggest that nitration of soluble α-synuclein may be a protective factor in PD, rather than a causative one.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
FEBS Letters, v. 542, issue 1-3, p. 147-152
Scholar Commons Citation
Yamin, Ghiam; Uversky, Vladimir N.; and Fink, Anthony L., "Nitration Inhibits Fibrillation of Human α-synuclein in Vitro by Formation of Soluble Oligomers" (2003). Molecular Medicine Faculty Publications. 706.
https://digitalcommons.usf.edu/mme_facpub/706
