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Cited by 195

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Pulse EPR Spectroscopy Reveals the Coordination Sphere of Copper(II) Ions in the 1–16 Amyloid‐β Peptide: A Key Role of the First Two N‐Terminus Residues

Dorlet, Pierre, Gambarelli, Serge, Faller, Peter, Hureau, Christelle·2009·Angewandte Chemie International Edition

Abstract

Ligand sphere revealed: Cu ions were proposed to be linked to the aggregation of the amyloid-β peptide in Alzheimer's disease. However, unambiguous identification of the Cu ligands has remained difficult. The use of various EPR spectroscopies with specific isotopic labeling now allowed the assignment of the CuII ligands for both complexes present at physiological pH value (see 3D plots and structures). The results indicate that the peptide's first two amino acids are important for coordination and probably aggregation.

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Crossref · 10.1002/anie.200904567

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Metadata

Authors
Dorlet, P., Gambarelli, S., Faller, P., & Hureau, C.
Venue
Angewandte Chemie International Edition
Publisher
Wiley
Published
2009-11-17
Volume
48
Issue
49
Pages
9273-9276
ISSN
  • 1433-7851 (ISSN-L)
  • 1521-3773
OpenAlex
W2154225956
Cited by
195
References
2
FWCI
12.60
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Pulse EPR Spectroscopy Reveals the Coordination Sphere of Copper(II) Ions in the 1–16 Amyloid‐β Peptide: A Key Role of the First Two N‐Terminus Residues. https://app.cochat.ai/papers/10.1002/anie.200904567
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Dorlet, P., Gambarelli, S., Faller, P., & Hureau, C. (2009). Pulse EPR Spectroscopy Reveals the Coordination Sphere of Copper(II) Ions in the 1–16 Amyloid‐β Peptide: A Key Role of the First Two N‐Terminus Residues. Angewandte Chemie International Edition. https://doi.org/10.1002/anie.200904567

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