This work was supported by a grant from the Agence Nationale de la Recherche, Programme Blanc NT09-488591, “NEUROMETALS” (P.F. and P.D.) and 05-JCJC-0010-01, “NEUROARPE” (P.D). The staff of the SAMBA beamline at SOLEIL and more particularly Dr. Emiliano Fonda are gratefully acknowledged for help in performing the XAS experiments (SOLEIL Project 20080324).
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Communication
Deprotonation of the Asp1![[BOND]](http://onlinelibrarystatic.wiley.com/undisplayable_characters/00f8ff.gif)
Ala2 Peptide Bond Induces Modification of the Dynamic Copper(II) Environment in the Amyloid-β Peptide near Physiological pH†
Article first published online: 10 NOV 2009
DOI: 10.1002/anie.200904512
Copyright © 2009 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Hureau, C., Coppel, Y., Dorlet, P., Solari, P. L., Sayen, S., Guillon, E., Sabater, L. and Faller, P. (2009), Deprotonation of the Asp1Ala2 Peptide Bond Induces Modification of the Dynamic Copper(II) Environment in the Amyloid-β Peptide near Physiological pH. Angew. Chem. Int. Ed., 48: 9522–9525. doi: 10.1002/anie.200904512
- †
Publication History
- Issue published online: 30 NOV 2009
- Article first published online: 10 NOV 2009
- Manuscript Received: 12 AUG 2009
Funded by
- Agence Nationale de la Recherche. Grant Numbers: NT09-488591, 05-JCJC-0010-01
Keywords:
- amyloid β-peptides;
- binding sites;
- copper;
- deprotonation;
- NMR spectroscopy
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 Asp1Ala2 peptide bond (see picture).