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  • Title: A multi-approach study of the interaction of the Cu(II) and Ni(II) ions with alanylglycylhistamine, a mimicking pseudopeptide of the serum albumine N-terminal residue.
    Author: Gizzi P, Henry B, Rubini P, Giroux S, Wenger E.
    Journal: J Inorg Biochem; 2005 May; 99(5):1182-92. PubMed ID: 15833342.
    Abstract:
    The protonation equilibria of alanylglycylhistamine (Ala-Gly-Ha) and the complexation of this ligand with Cu(II) and Ni(II) have been studied by pH-potentiometry, 1H and 14N NMR spectroscopy, electrospray ionization mass spectrometry (ESI-MS), circular dichroism (CD), UV-Vis spectrophotometry and electron paramagnetic resonance (EPR). From pH approximately 2-12, the following complexes: MLH, MLH(-1), MLH(-2) and MLH(-3) are successively formed in aqueous solutions, the ligand under its neutral form being noted L. At physiological pH, the MLH(-2) complex is predominant. The coordination in this complex is assumed by one amino, two deprotonated peptide and one imidazole nitrogen atoms. The ESI-MS study confirmed the formation of the MLH(-1), MLH(-2) and MLH(-3) complexes. The structure of MLH(-2) was determined by single crystal X-ray analysis. CD and UV-Vis techniques allowed us to propose that the imidazole-N3 nitrogen acts as the anchor group for the coordination to the metal(II) ions rather than the amino group. At high pH values, the further deprotonation of the N-H imidazole group, leading to the formation of MLH(-3), occurs, as revealed by 1H NMR spectroscopy.
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