Thermodynamic and Structural Characterization of the Copper(II) Complexes of Peptides Containing Both Histidyl and Aspartyl Residues

Kállay, Csilla; Nagy, Zoltán; Várnagy, Katalin; Malandrinos, Gerasimos; Hadjiliadis, Nick; Sóvágó, Imre

doi:https://doi.org/10.1155/2007/30394

Bioinorganic Chemistry and Applications

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Research Article | Open Access

Volume 2007 | Article ID 030394 | https://doi.org/10.1155/2007/30394

Thermodynamic and Structural Characterization of the Copper(II) Complexes of Peptides Containing Both Histidyl and Aspartyl Residues

Csilla Kállay,¹Zoltán Nagy,²Katalin Várnagy,¹Gerasimos Malandrinos,³Nick Hadjiliadis,³and Imre Sóvágó¹

Academic Editor: Martin Stillman

Received27 Jun 2007

Accepted07 Nov 2007

Published06 Dec 2007

Abstract

Terminally protected pentapeptides with 2 histidines (Ac-HHVGD-NH2 and Ac-HVGDH-NH2) 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 β-carboxylate groups of FDAH and VIDAH create a very effective metal binding site with the (NH2, N−, β-COO−) and (NH2, N−, N−, β-COO−) coordination modes including the N-termini, while the histidine sites are available for the formation of the (Nim, N−, N−) binding mode resulting in the preference of dinuclear complex formation.

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Copyright © 2007 Csilla Kállay et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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