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• W2314083984 endingPage "1327" @default.
• W2314083984 startingPage "1318" @default.
• W2314083984 abstract "Alzheimer’s disease (AD) patients show abnormally high concentrations of Cu2+ in the amyloid β plaques. This invokes that Cu2+ might play a crucial role in the onset of AD. The last few decades of research have also shown that Cu2+ plays a significant role in the aggregation of Aβ plaques in the brain and the generation of oxidative stress. Because the crystal structures of Cu-Aβ are yet to be obtained, there are various proposed models for the Cu2+ coordination environment of Aβ peptides. In this study, we have used the truncated hydrophilic part of the native Aβ peptide to probe the Cu2+ coordination site of the peptide, using a combination of spectroscopy and exogenous ligand-binding studies. It is evident from our study that Aβ(1–16) binds 1 equiv of Cu2+ and yet shows an equilibrium between two species with a pKa of ∼8.1. Ligand-field analysis of absorption and circular dichroism spectroscopy data indicates five-coordinate geometry for both components. We investigate the effect of azide and 8-hydroxyquinoline binding to Cu-Aβ and demonstrate the presence of a water-derived ligand and a second exchangeable ligand coordinated to copper at physiological pH, along the equatorial plane of a square-pyramidal active site." @default.
• W2314083984 created "2016-06-24" @default.
• W2314083984 creator A5016109754 @default.
• W2314083984 creator A5058550051 @default.
• W2314083984 date "2013-01-18" @default.
• W2314083984 modified "2023-09-24" @default.
• W2314083984 title "Ligand-Field and Ligand-Binding Analysis of the Active Site of Copper-Bound Aβ Associated with Alzheimer’s Disease" @default.
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• W2314083984 doi "https://doi.org/10.1021/ic301865n" @default.
• W2314083984 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23330670" @default.
• W2314083984 hasPublicationYear "2013" @default.
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