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.
journal_name
Bioinorg Chem Appljournal_title
Bioinorganic chemistry and applicationsauthors
Kállay C,Nagy Z,Várnagy K,Malandrinos G,Hadjiliadis N,Sóvágó Idoi
10.1155/2007/30394subject
Has Abstractpub_date
2007-01-01 00:00:00pages
30394eissn
1565-3633issn
1687-479Xpub_type
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