Journal article
The structure of the amyloid-beta peptide high-affinity copper II binding site in Alzheimer disease
Victor A Streltsov, Stephen J Titmuss, V Chandana Epa, Kevin J Barnham, Colin L Masters, Joseph N Varghese
BIOPHYSICAL JOURNAL | CELL PRESS | Published : 2008
Abstract
Neurodegeneration observed in Alzheimer disease (AD) is believed to be related to the toxicity from reactive oxygen species (ROS) produced in the brain by the amyloid-beta (Abeta) protein bound primarily to copper ions. The evidence for an oxidative stress role of Abeta-Cu redox chemistry is still incomplete. Details of the copper binding site in Abeta may be critical to the etiology of AD. Here we present the structure determined by combining x-ray absorption spectroscopy (XAS) and density functional theory analysis of Abeta peptides complexed with Cu(2+) in solution under a range of buffer conditions. Phosphate-buffered saline buffer salt (NaCl) concentration does not affect the high-affin..
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Awarded by U. S. Department of Energy, Office of Science, Office of Basic Energy Sciences
Funding Acknowledgements
The use of APS was supported by the U. S. Department of Energy, Office of Science, Office of Basic Energy Sciences (contract No. DE-AC02-06CH11357). APS synchrotron access was supported by the Australian Synchrotron Research Program, which is funded by the Commonwealth of Australia under the Major National Research Facilities Program. K. J. B. was partially funded by a grant from the National Health and Medical Research Council of Australia.