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• W2088121027 endingPage "1694" @default.
• W2088121027 startingPage "1683" @default.
• W2088121027 abstract "A potentiometric, spectroscopic (UV-Vis, CD and EPR) and mass spectrometric (ESI-MS) study of Cu(II) binding to the (1-2,7-21)NPG, Asp1-Ala-Ile7-Ser-His9-Lys-Arg-His12-Lys-Thr-Asp-Ser-Phe-Val-Gly-Leu-Met21-NH2, and Ac-(1-2,7-21)NPG, Ac-Asp1-Ala-Ile7-Ser-His9-Lys-Arg-His12-Lys-Thr-Asp-Ser-Phe-Val-Gly-Leu-Met21-NH2, fragments of neuropeptide gamma were carried out. The results clearly indicate the stabilization of the 1 N {NH2, β-COO−}, 2 N {NH2, β-COO−, NIm} and 3 N {NH2, β-COO−, 2NIm} complexes by the coordination of the β-carboxylate group of the D1 residue. For the (1-2,7-21)NPG the CuH2L complex with 3 N {NH2, β-COO−, 2NIm}, the binding mode dominates in a wide pH range of 4–8.5. With the sequential increase of pH, deprotonated amide nitrogens are involved in copper coordination. For the Ac-(1-2,7-21)NPG peptide the imidazole nitrogen atoms are the primary metal binding sites forming macrochelates in the pH range 4 to 7. The CuHL complex with 4 N {NIm, N−, N−, NIm} coordination mode is formed in pH range 6–9. Deprotonation and co-ordination of the third amide nitrogen were detected at pH ∼8.6. Metal-catalyzed oxidation (MCO) of proteins is mainly a site-specific process in which one or a few amino acids at metal-binding sites on the protein are preferentially oxidized. To elucidate the products of the copper(II)-catalyzed oxidation of the (1-2,7-21)NPG and Ac-(1-2,7-21)NPG, the liquid chromatography-mass spectrometry (LC-MS) method and Cu(II)/hydrogen peroxide as a model oxidizing system were employed. In the presence of hydrogen peroxide with 1 : 4 peptide–H2O2 molar ratio for the Ac-(1-2,7-21)NPG peptide the oxidation of the methionine residue to methionine sulfoxide and for (1-2,7-21)NPG to sulfone was observed. For the Cu(II)–peptide–hydrogen peroxide in 1 : 1 : 4 molar ratio systems, oxidation of the histidine residues to 2-oxohistidines was detected. Under experimental conditions the (1-2,7-21)NPG and Ac-(1-2,7-21)NPG undergo fragmentations by cleavage of the S8-H9, H9-K10, R11-H12 and H12-K13 peptide bonds supporting the participation of the H9 and H12 residues in the coordination of copper(II) ions. For the (1-2,7-21)NPG peptide chain the involvement of the D1 residue in the coordination of metal ions is supported by the alkoxyl radical modification of this amino acid residue." @default.
• W2088121027 created "2016-06-24" @default.
• W2088121027 creator A5009036426 @default.
• W2088121027 creator A5018680099 @default.
• W2088121027 creator A5036664652 @default.
• W2088121027 date "2012-01-01" @default.
• W2088121027 modified "2023-09-27" @default.
• W2088121027 title "Coordination of copper(<scp>ii</scp>) ions by the fragments of neuropeptide gamma containing D¹, H⁹, H¹²residues and products of copper-catalyzed oxidation" @default.
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• W2088121027 doi "https://doi.org/10.1039/c1dt10592b" @default.
• W2088121027 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22159001" @default.
• W2088121027 hasPublicationYear "2012" @default.
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• W2088121027 hasAuthorship W2088121027A5009036426 @default.
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