Deprotonation of the Asp1----Ala2 Peptide Bond Induces Modification of the Dynamic Copper(II) Environment in the Amyloid-β Peptide near Physiological pH

Deprotonation of the Asp1----Ala2 Peptide Bond Induces Modification of the Dynamic Copper(II) Environment in the Amyloid-β Peptide near Physiological pH

Premium bonds: The pH‐dependent coordination of CuII to the Alzheimer′s disease amyloid‐β peptide has been studied by NMR spectroscopy. Several equivalent ligands are in equilibrium for CuII binding near pH 6.6 and 8.7. Fewer conformers are detected at high pH, in line with a reshuffling of the CuII...

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Veröffentlicht in:Angewandte Chemie (International ed.) 2009-12, Vol.48 (50), p.9522-9525
Hauptverfasser: Hureau, Christelle, Coppel, Yannick, Dorlet, Pierre, Solari, Pier Lorenzo, Sayen, Stéphanie, Guillon, Emmanuel, Sabater, Laurent, Faller, Peter
Format: Artikel
Sprache:eng
Schlagworte:
Alanine
Alzheimer Disease
Amyloid beta-Peptides - chemistry
amyloid β-peptides
Aspartic Acid
Binding Sites
copper
Copper - chemistry
deprotonation
Dipeptides - chemistry
Humans
Hydrogen-Ion Concentration
Magnetic Resonance Spectroscopy
NMR spectroscopy
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Zusammenfassung:Premium bonds: The pH‐dependent coordination of CuII to the Alzheimer′s disease amyloid‐β peptide has been studied by NMR spectroscopy. Several equivalent ligands are in equilibrium for CuII binding near pH 6.6 and 8.7. Fewer conformers are detected at high pH, in line with a reshuffling of the CuII binding site induced by deprotonation of the Asp1Ala2 peptide bond (see picture).
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200904512