ESR an optical absorption studies on the copper(II) interaction with small peptides containing aromatic amino acids.
The interaction of Cu(II) with di- and tripeptides each containing phenylalanine, tryptophan or histidine in the amino acid chain has been investigated by means of electron spin resonance (ESR) and optical absorption spectroscopy. Cu(II) complexes of dipeptides and tripeptides exhibit different magnetic and optical parameters. Dipeptide complexes have larger gparallel-values and smaller A parallel values than tripeptide complexes. When compared to dipeptide complexes, the d-d band of the central metal ion is blue shifted for tripeptide complexes. There are no significant difference in the behavior of Cu(II) peptide complexes containing phenylalanine or tryptophan. Complexes of histidine containing peptides, however, show modified spectra caused by the participation of the imidazole nitrogen in the coordination to Cu(II). The imidazole nitrogen seems to coordinate in-plane with other coordinating atoms or in an axial position depending on the kind of peptide.
D002614:Chelating Agents; D003300:Copper; D004151:Dipeptides; D004578:Electron Spin Resonance Spectroscopy; D006639:Histidine; D009842:Oligopeptides; D010649:Phenylalanine; D013053:Spectrophotometry; D014364:Tryptophan
D002614:Chelating Agents; D004151:Dipeptides; D009842:Oligopeptides; D010649:Phenylalanine; D006639:Histidine; D003300:Copper; D014364:Tryptophan