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Updated: Jul 7, 2026

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Thermodynamic and structural characterization of the copper(II) complexes of peptides containing both histidyl and
Csilla Kállay1, Zoltán Nagy, Katalin Várnagy
1Department of Inorganic and Analytical Chemistry, University of Debrecen, Debrecen 4010, Hungary.
Abstract:
Terminally protected pentapeptides with 2 histidines (Ac-HHVGD-NH(2) and Ac-HVGDH-NH(2)) and the terminally free peptides containing both internal aspartyl and C-terminal histidyl residues (FDAH and VIDAH) have been synthesized, and copper(II) complexes studied by potentiometric, UV-Vis, CD, and EPR spectroscopic techniques in solution. Both thermodynamic and spectroscopic data reveal that side chain donor atoms of aspartyl and histidyl residues have a significant contribution to the metal binding affinity of peptide molecules. In the case of terminally protected peptides, the role of the imidazole-N donor functions is reflected in the enhanced stability of the 3N and 4N coordinated copper(II) complexes. The amino and beta-carboxylate groups of FDAH and VIDAH create a very effective metal binding site with the (NH(2), N(-), beta-COO(-)) and (NH(2), N(-), N(-), beta-COO(-)) coordination modes including the N-termini, while the histidine sites are available for the formation of the (N(im), N(-), N(-)) binding mode resulting in the preference of dinuclear complex formation.
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