Journal article

Copper binding and redox chemistry of the A beta 16 peptide and its variants: insights into determinants of copper-dependent reactivity

Nineveh Yako, Tessa R Young, Jade M Cottam Jones, Craig A Hutton, Anthony G Wedd, Zhiguang Xiao



The metal-binding sites of Aβ peptides are dictated primarily by the coordination preferences of the metal ion. Consequently, Cu(i) is typically bound with two His ligands in a linear mode while Cu(ii) forms a pseudo-square planar stereochemistry with the N-terminal amine nitrogen acting as an anchoring ligand. Several distinct combinations of other groups can act as co-ligands for Cu(ii). A population of multiple binding modes is possible with the equilibrium position shifting sensitively with solution pH and the nature of the residues in the N-terminal region. This work examined the Cu(ii) chemistry of the Aβ16 peptide and several variants that targeted these binding modes. The results are..

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