title: X-ray absorption and diffraction studies of the metal binding sites in amyloid beta-peptide.
abstract: A major source of neurodegeneration observed in Alzheimer's disease is believed to be caused by the toxicity from reactive oxygen species produced in the brain mediated by the A beta protein and mainly copper species. An atomic model of an amyloid beta-peptide (A beta) Cu2+ complex or at least the structure of the metal binding site is of great interest. Accurate information about the Cu-binding site of A beta protein can facilitate simulation of redox chemistry using high level quantum mechanics. Complementary X-ray diffraction and X-ray absorption techniques can be employed to obtain such accurate information. This review provides a blend of X-ray diffraction results on amyloid structures and selected works on A beta Cu2+ binding based on spectroscopic measurements with emphasis on the X-ray absorption technique.
authors.affiliation: CSIRO Molecular and Health Technologies, 343 Royal Parade, Parkville, VIC, Australia. victor.streltsov@csiro.au
authors.forename: Victor
authors.initials: V
authors.lastname: Streltsov
mesh_terms: D015502:Absorptiometry, Photon / Q000639:trends*; D000544:Alzheimer Disease / Q000473:pathology; D016229:Amyloid beta-Peptides / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D003300:Copper / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D011487:Protein Conformation; D014961:X-Ray Diffraction / Q000639:trends*; D014965:X-Rays
chemical_list: D016229:Amyloid beta-Peptides; D003300:Copper