Local atomic structure and oxidation processes of Cu(I) binding site in amyloid beta peptide: XAS Study

There are two different motifs of X-ray absorption spectra for Cu(I) K-edge in amyloid-β peptide which could be due to two different configurations of local Cu(I) environment. Two or three histidine ligands can coordinate copper ion in varying conformations. On the other hand, oxidation of amyloid-β...

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Bibliographic Details
Published in:Journal of physics. Conference series 2016-05, Vol.712 (1), p.12138
Main Authors: Kremennaya, M A, Soldatov, M A, Streltsov, V A, Soldatov, A V
Format: Article
Language:English
Subjects:
Absorption spectra
Atomic structure
Beta rays
Binding sites
Copper
Electronic structure
Histidine
Oxidation
Peptides
Physics
X ray absorption
X ray spectra
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Summary:There are two different motifs of X-ray absorption spectra for Cu(I) K-edge in amyloid-β peptide which could be due to two different configurations of local Cu(I) environment. Two or three histidine ligands can coordinate copper ion in varying conformations. On the other hand, oxidation of amyloid-β peptide could play an additional role in local copper environment. In order to explore the peculiarities of local atomic and electronic structure of Cu(I) binding sites in amyloid-β peptide the x-ray absorption spectra were simulated for various Cu(I) environments including oxidized amyloid-β and compared with experimental data.
ISSN:1742-6588
1742-6596
DOI:10.1088/1742-6596/712/1/012138