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

Hureau Christelle | Zendy; Coppel Yannick | Zendy; Dorlet Pierre | Zendy; Solari Pier Lorenzo | Zendy; Sayen Stéphanie | Zendy; Guillon Emmanuel | Zendy; Sabater Laurent | Zendy; Faller Peter | Zendy

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

Author(s) -

Hureau Christelle,

Coppel Yannick,

Dorlet Pierre,

Solari Pier Lorenzo,

Sayen Stéphanie,

Guillon Emmanuel,

Sabater Laurent,

Faller Peter

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.200904512

Subject(s) - peptide , deprotonation , copper , chemistry , peptide bond , amyloid (mycology) , biochemistry , organic chemistry , inorganic chemistry , ion

Premium bonds : The pH‐dependent coordination of Cu II to the Alzheimer′s disease amyloid‐β peptide has been studied by NMR spectroscopy. Several equivalent ligands are in equilibrium for Cu II binding near pH 6.6 and 8.7. Fewer conformers are detected at high pH, in line with a reshuffling of the Cu II binding site induced by deprotonation of the Asp1Ala2 peptide bond (see picture).

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