Mass Spectral Studies Reveal the Structure of Aβ1–16–Cu2+ Complex Resembling ATCUN Motif

In Alzheimer’s disease, copper binds to amyloid beta (Aβ) peptide and generates oxidative stress. The coordination of histidine (His) residues to Cu2+ is still uncertain. We studied Cu2+ binding to Aβ1–16 peptide using the diethyl pyrocarbonate (DEPC) assay and mass spectrometry. Our results show th...

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Bibliographic Details
Published in:Inorganic chemistry 2012-08, Vol.51 (15), p.7960-7962
Main Authors: Ginotra, Yamini P, Ramteke, Shefali N, Srikanth, Rapole, Kulkarni, Prasad P
Format: Article
Language:English
Subjects:
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
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Summary:In Alzheimer’s disease, copper binds to amyloid beta (Aβ) peptide and generates oxidative stress. The coordination of histidine (His) residues to Cu2+ is still uncertain. We studied Cu2+ binding to Aβ1–16 peptide using the diethyl pyrocarbonate (DEPC) assay and mass spectrometry. Our results show that only one His is involved in Cu2+ coordination, which is identified as His6 using mass spectral studies. Novel nickel displacement studies have further supported the proposal that the Cu2+ binding site of Aβ1–16 peptide resembles the ATCUN motif of human serum albumin.
ISSN:0020-1669
1520-510X
DOI:10.1021/ic301244x