All Outputs (2)

Evaluation of Cu(I) binding to the E2 domain of the amyloid precursor protein – a lesson in quantification of metal binding to proteins via ligand competition (2017)
Journal Article
Young, T. R., Wedd, A. G., & Xiao, Z. (2018). Evaluation of Cu(I) binding to the E2 domain of the amyloid precursor protein – a lesson in quantification of metal binding to proteins via ligand competition. Metallomics, 10(1), 108-119. https://doi.org/10.1039/c7mt00291b

The extracellular domain E2 of the amyloid precursor protein (APP) features a His-rich metal-binding site (denoted as the M1 site). In conjunction with surrounding basic residues, the site participates in interactions with components of the extracell... Read More about Evaluation of Cu(I) binding to the E2 domain of the amyloid precursor protein – a lesson in quantification of metal binding to proteins via ligand competition.

Copper binding and redox chemistry of the Aβ16 peptide and its variants: insights into determinants of copper-dependent reactivity (2017)
Journal Article
Yako, N., Young, T. R., Cottam Jones, J. M., Hutton, C. A., Wedd, A. G., & Xiao, Z. (2017). Copper binding and redox chemistry of the Aβ16 peptide and its variants: insights into determinants of copper-dependent reactivity. Metallomics, 9(3), 278-291. https://doi.org/10.1039/c6mt00299d

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 wit... Read More about Copper binding and redox chemistry of the Aβ16 peptide and its variants: insights into determinants of copper-dependent reactivity.