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Cited by 198

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

Bousejra-ElGarah, Fatima, Bijani, Christian, Coppel, Yannick, Faller, Peter, Hureau, Christelle·2011·Inorganic Chemistry
DOI 10.1021/ic201233b
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Abstract

Iron has been implicated in Alzheimer's disease, but until now no direct proof of Fe(II) binding to the amyloid-β peptide (Aβ) has been reported. We used NMR to evidence Fe(II) coordination to full-length Aβ40 and truncated Aβ16 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:Aβ stoichiometry and temperature. Analysis of Fe(II) broadening effect in the (1)H, (13)C, 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.

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Cited by

Metadata

Authors
Bousejra-ElGarah, F., Bijani, C., Coppel, Y., Faller, P., & Hureau, C.
Venue
Inorganic Chemistry
Publisher
American Chemical Society (ACS)
Published
2011-07-29
Volume
50
Issue
18
Pages
9024-9030
ISSN
  • 0020-1669 (ISSN-L)
  • 1520-510X
DOI
10.1021/ic201233b
OpenAlex
W2327309337
Cited by
198
References
7
FWCI
7.70
Type
journal article
Language
en
Open access
closed

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.