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

被引：157

作者：

Dorlet, Pierre ^{[1
,2
]}

Gambarelli, Serge ^{[3
]}

Faller, Peter ^{[4
,5
]}

Hureau, Christelle ^{[4
,5
]}

机构：

[1] CNRS, Lab Stress Oxydant & Detoxicat, URA 2096, F-91191 Gif Sur Yvette, France

[2] CEA, IBiTec S, SB2SM, F-91191 Gif Sur Yvette, France

[3] UJF, INAC SCIB, UMR E3, Lab Resonance Magnet,CEA, F-38054 Grenoble, France

[4] CNRS, LCC Lab Chim Coordinat, F-31077 Toulouse, France

[5] Univ Toulouse, UPS, INPT, LCC, F-31077 Toulouse, France

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2009年 / 48卷 / 49期

关键词：

amyloid-beta peptides; bioinorganic chemistry; copper; EPR spectroscopy; ligand interactions; MULTINUCLEAR SPIN SYSTEMS; ALZHEIMERS-DISEASE; PRION PROTEIN; BINDING; CU(II); STOICHIOMETRY; FRAGMENTS; RELEVANCE; AFFINITY; FEATURES;

D O I：

10.1002/anie.200904567

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Ligand sphere revealed: Cu ions were proposed to be linked to the aggregation of the amyloid-ß 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. Chemical Equitation Presentation © 2009 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：9273 / 9276

页数：4

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