Iron(II) Binding to Amyloid-β, the Alzheimer's Peptide

被引:174
作者
Bousejra-ElGarah, Fatima
Bijani, Christian
Coppel, Yannick
Faller, Peter [1 ]
Hureau, Christelle
机构
[1] CNRS, LCC, F-31077 Toulouse, France
关键词
PRECURSOR PROTEIN; COPPER-BINDING; SENILE PLAQUE; DISEASE; ZINC; COORDINATION; FERRITIN; ALUMINUM; ENVIRONMENT; A-BETA(42);
D O I
10.1021/ic201233b
中图分类号
O61 [无机化学];
学科分类号
070301 [无机化学];
摘要
Iron has been implicated in Alzheimer's disease, but until now no direct proof of Fe-II binding to the amyloid-beta peptide (A beta) has been reported. We used NMR to evidence Fe-II coordination to full-length A beta 40 and truncated A beta 16 peptides at physiological pH and to show that the Fe-II binding site is located in the first 16 amino-acid residues. Fe-II caused selective broadening of some NMR peaks that was dependent on the Fe:A beta stoichiometry and temperature. Analysis of Fe-II broadening effect in the H-1, C-13, and 2D NMR data established that Asp1, Glu3, the three His, but not Tyr10 nor Met35 are the residues mainly involved in Fe-II coordination.
引用
收藏
页码:9024 / 9030
页数:7
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