Contribution of a peroxide adduct of copper(II)-peptide complex to modify the secondary structure of albumin.
We have found that copper(II) compounds containing a peptide group in the chelate exhibit high activity for modification or degradation of albumin in the presence of hydrogen peroxide, whereas no activity was detected for the copper(II) compounds without an amide-group. It is suggested that presence of the amide-group in the ligand may play an important role in the formation of a peroxide adduct and in activation of the peroxide ion, leading to cleavage of the peptide bond of a neighboring protein. It is implied that conversion of normal cellular prion protein PrPC into a disease-causing isoform, PrPSc is attributed to the activated peroxide ion coordinated to a copper(II) captured in the NH2-terminal domain of the PrPC.
Department of Chemistry, Faculty of Science, Yamagata University, Japan.
Y
Y
Ishikawa
S
S
Ito
S
S
Nishino
S
S
Ohba
Y
Y
Nishida
D002256:Carbonic Anhydrases / Q000737:chemistry / Q000187:drug effects; D003300:Copper / Q000494:pharmacology*; D003574:Cytochrome c Group / Q000737:chemistry / Q000187:drug effects; D006801:Humans; D006861:Hydrogen Peroxide / Q000494:pharmacology*; D015394:Molecular Structure; D009942:Organometallic Compounds / Q000737:chemistry / Q000494:pharmacology*; D018621:PrPC Proteins / Q000737:chemistry / Q000187:drug effects; D018620:PrPSc Proteins / Q000737:chemistry / Q000187:drug effects; D017433:Protein Structure, Secondary / Q000187:drug effects*; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000187:drug effects
D003574:Cytochrome c Group; D009942:Organometallic Compounds; D018621:PrPC Proteins; D018620:PrPSc Proteins; D012710:Serum Albumin, Bovine; D003300:Copper; D006861:Hydrogen Peroxide; D002256:Carbonic Anhydrases