期刊
FEBS LETTERS
卷 585, 期 3, 页码 561-566出版社
WILEY
DOI: 10.1016/j.febslet.2011.01.009
关键词
C-Terminus; alpha-Synuclein; Aggregation; Parkinson's disease
资金
- NIH [00486855]
- Welch Foundation
Substantial evidence implicates that the aggregation of alpha-synuclein (alpha Syn) is a critical factor in the pathogenesis of Parkinson's disease. This study focuses on the role of alpha Syn C-terminus. We introduced two additional cysteine residues at positions 107 and 124 (A107C and A124C) to our previous construct. Five X-isomers of oxidative-folded mutation of alpha-synuclein with three disulfides were isolated and their secondary structures and aggregating features were analyzed. All isomers showed similar random coil structures as wild-type alpha-synuclein. However, these isomers did not form aggregates or fibrils, even with prolonged incubation, suggesting that the interactions between the C-terminal and N-terminal or central NAC region are important in maintaining the natively unfolded structure of alpha Syn and thus prevent alpha Syn from changing conformation, which is a critical step for fibrillation. Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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