Thermodynamic and structural characterization of the copper(II) complexes of peptides containing both histidyl and aspartyl residues

 
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2007 (EN)
Thermodynamic and structural characterization of the copper(II) complexes of peptides containing both histidyl and aspartyl residues (EN)

Kallay, C. (EN)

Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας (EL)
Kallay, C. (EN)

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. Copyright (c) 2007. (EN)

octarepeat domain (EN)

Πανεπιστήμιο Ιωαννίνων (EL)
University of Ioannina (EN)

Bioinorg Chem Appl (EN)

English

2007

<Go to ISI>://000252032200001

Hindawi Publishing Corporation (EN)



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