The effect of histidyl residues on the complexation of bis(imidazolyl) containing tripeptides with copper(II) ion

Abstract

Copper(II) complexes of tripeptide derivatives of bis(imidazol-2-yl) group have been studied by potentiometric, UV–visible and EPR spectroscopic methods. The peptide molecules correspond to the amino acid sequence of collagen containing histidyl residues in different locations and were connected to the bis(imidazol-2-yl) group either on the C-termini (BOC–Pro–Leu–His–BIMA, BOC–His–Leu–Gly–BIMA) or on the N-termini (BIP–His–Ala–Gly–OEt, BIP–Ile–Ala–His–OMe). It was concluded that the imidazole nitrogen donor atoms of the bis(imidazol-2-yl) moiety are the primary metal binding sites, but the histidyl imidazole nitrogens in the side chains have also some effect on the stability and the coordination mode of the complexes. All ligands can coordinate tridentately to copper(II) ion forming a six-membered chelate and a macrochelate in the [CuL] 2+ complexes, which results in a slight distortion in the coordination geometry of [CuL 2] 2+ complexes. The deprotonation and coordination of amide nitrogens, however, were not observed in any cases.