کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2048174 | 1074067 | 2011 | 6 صفحه PDF | دانلود رایگان |
Substantial evidence implicates that the aggregation of α-synuclein (αSyn) is a critical factor in the pathogenesis of Parkinson’s disease. This study focuses on the role of αSyn 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 α-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 α-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 αSyn and thus prevent αSyn from changing conformation, which is a critical step for fibrillation.
Journal: FEBS Letters - Volume 585, Issue 3, 4 February 2011, Pages 561–566