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 NH2-terminal domain of the PrP(C).
|ジャーナル||Zeitschrift fur Naturforschung - Section C Journal of Biosciences|
|出版ステータス||Published - 1998|
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