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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
Author(s) -
Dorlet Pierre,
Gambarelli Serge,
Faller Peter,
Hureau Christelle
Publication year - 2009
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200904567
Subject(s) - electron paramagnetic resonance , peptide , coordination sphere , chemistry , crystallography , ligand (biochemistry) , ion , amyloid (mycology) , spectroscopy , copper , amino acid , combinatorial chemistry , biochemistry , nuclear magnetic resonance , inorganic chemistry , organic chemistry , physics , receptor , crystal structure , quantum mechanics
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 Cu II 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.