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Copper(II)-peroxide Adduct, Modification of Protein, Copper(II)-peptide Complex 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 PrP C  into a disease-causing isoform, PrP Sc  is attributed to the activated peroxide ion coordinated to a copper(II) captured in the NH 2 -terminal domain of the PrP C  .

Contribution of a Peroxide Adduct of Copper(II)-Peptide Complex to Modify the Secondary Structure of Albumin