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 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.
Biometry and Nutrition Group, Agharkar Research Institute, Pune-411004, India.
Yamini P
YP
Ginotra
Shefali N
SN
Ramteke
Rapole
R
Srikanth
Prasad P
PP
Kulkarni
D020816:Amino Acid Motifs; D016229:Amyloid beta-Peptides / Q000737:chemistry*; D001665:Binding Sites; D056831:Coordination Complexes / Q000737:chemistry*; D003300:Copper / Q000737:chemistry*; D004047:Diethyl Pyrocarbonate; D006639:Histidine / Q000737:chemistry*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008968:Molecular Conformation; D009532:Nickel; D010446:Peptide Fragments / Q000737:chemistry*; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry; D053719:Tandem Mass Spectrometry
D016229:Amyloid beta-Peptides; D056831:Coordination Complexes; D010446:Peptide Fragments; D012709:Serum Albumin; C433241:amyloid beta-protein (1-16); D006639:Histidine; D003300:Copper; D009532:Nickel; D004047:Diethyl Pyrocarbonate