Products of Cu(II)-catalyzed oxidation in the presence of hydrogen peroxide of the 1-10, 1-16 fragments of human and mouse beta-amyloid peptide.

Abstract:

:The interactions of proteins with reactive oxygen species (ROS) may result in covalent modifications of amino acid residues in proteins, formation of protein-protein cross-linkages, and oxidation of the protein backbone resulting in protein fragmentation. In an attempt to elucidate the products of the metal-catalyzed oxidation of the human (H) and mouse (M) (1-10H), (1-10M), (1-16H) and (1-16M) fragments of beta-amyloid peptide, the high performance liquid chromatography (HPLC) and matrix-assisted laser desorption/ionization mass spectrometry (MALDI-TOF MS) methods and Cu(II)/H(2)O(2) as a model oxidizing system were employed. Peptide solution (0.50 mM) was incubated at 37 degrees C for 24 h with metal:peptide:H(2)O(2) molar ratio 1:1:1 for the (1-16H), (1-16M) fragments, and 1:1:2 for the (1-10H), (1-10M) peptides in phosphate buffer, pH 7.4. Oxidation targets for all peptide studied are the histidine residues coordinated to the metal ions. For the (1-16H) peptide are likely His(13) and/or His(14), and for the (1-16M) fragment His(6) and/or His(14), which are converted to 2-oxo-His. Metal-binding residue, the aspartic acid (D(1)) undergoes the oxidative decarboxylation and deamination to pyruvate. The cleavages of the peptide bonds by either the diamide or alpha-amidation pathways were also observed.

journal_name

J Inorg Biochem

authors

Kowalik-Jankowska T,Ruta M,Wiśniewska K,Łankiewicz L,Dyba M

doi

10.1016/j.jinorgbio.2004.03.001

subject

Has Abstract

pub_date

2004-06-01 00:00:00

pages

940-50

issue

6

eissn

0162-0134

issn

1873-3344

pii

S0162013404000789

journal_volume

98

pub_type

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