[HTML][HTML] Nitration inhibits fibrillation of human α-synuclein in vitro by formation of soluble oligomers

G Yamin, VN Uversky, AL Fink - FEBS letters, 2003 - Elsevier
G Yamin, VN Uversky, AL Fink
FEBS letters, 2003Elsevier
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 …
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.
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