Copper(II) complexes of dipeptides containing aspartyl, glutamyl, and histidyl residues in the side chain.
Copper(II) complexes of various dipeptides containing carboxylate and imidazole-N3 donors (alpha- and gamma-GluVal, alpha- and beta-AspGly, beta-AspHis, gamma-GluHis, and homocarnosine) were studied by potentiometric and spectroscopic methods in solution. It was found that the presence of an alpha-carboxylate group in the N-terminal part of a peptide molecule significantly enhances the metal-binding ability of the ligands as a consequence of stable bis complex formation involving amino acid-like coordination. The interaction of copper(II) with beta-AspHis was characterized by the formation of an imidazole-bridged dimeric species, while the formation of bis complexes was detected in the case of gamma-GluHis. Binding of the imidazole N3 and deprotonated amide nitrogen was presumed in the copper(II)-homocarnosine system.
Sóvágó
I
I
Department of Inorganic and Analytical Chemistry, Lajos Kossuth University, Debrecen, Hungary.
Farkas
E
E
Bertalan
C
C
Lebkiri
A
A
Kowalik-Jankowska
T
T
Kozlowski
H
H
D001224:Aspartic Acid / Q000737:chemistry*; D003300:Copper / Q000737:chemistry*; D004151:Dipeptides / Q000737:chemistry*; D005971:Glutamates / Q000737:chemistry*; D018698:Glutamic Acid; D006639:Histidine / Q000737:chemistry*; D008670:Metals / Q000737:chemistry; D011485:Protein Binding
D004151:Dipeptides; D005971:Glutamates; D008670:Metals; D001224:Aspartic Acid; D018698:Glutamic Acid; D006639:Histidine; D003300:Copper