Mass spectral studies reveal the structure of Aβ1-16-Cu2+ complex resembling ATCUN motif

Inorg Chem. 2012 Aug 6;51(15):7960-2. doi: 10.1021/ic301244x. Epub 2012 Jul 17.

Abstract

In Alzheimer's disease, copper binds to amyloid beta (Aβ) peptide and generates oxidative stress. The coordination of histidine (His) residues to Cu(2+) is still uncertain. We studied Cu(2+) binding to Aβ1-16 peptide using the diethyl pyrocarbonate (DEPC) assay and mass spectrometry. Our results show that only one His is involved in Cu(2+) coordination, which is identified as His6 using mass spectral studies. Novel nickel displacement studies have further supported the proposal that the Cu(2+) binding site of Aβ1-16 peptide resembles the ATCUN motif of human serum albumin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Amyloid beta-Peptides / chemistry*
  • Binding Sites
  • Coordination Complexes / chemistry*
  • Copper / chemistry*
  • Diethyl Pyrocarbonate
  • Histidine / chemistry*
  • Humans
  • Hydrogen-Ion Concentration
  • Molecular Conformation
  • Nickel
  • Peptide Fragments / chemistry*
  • Protein Binding
  • Serum Albumin / chemistry
  • Tandem Mass Spectrometry

Substances

  • Amyloid beta-Peptides
  • Coordination Complexes
  • Peptide Fragments
  • Serum Albumin
  • amyloid beta-protein (1-16)
  • Histidine
  • Copper
  • Nickel
  • Diethyl Pyrocarbonate