Thermodynamic and structural characterization of the copper(II) complexes of peptides containing both histidyl and aspartyl residues
| dc.contributor.author | Kallay, C. | en |
| dc.contributor.author | Nagy, Z. | en |
| dc.contributor.author | Varnagy, K. | en |
| dc.contributor.author | Malandrinos, G. | en |
| dc.contributor.author | Hadjiliadis, N. | en |
| dc.contributor.author | Sovago, I. | en |
| dc.date.accessioned | 2015-11-24T16:51:30Z | |
| dc.date.available | 2015-11-24T16:51:30Z | |
| dc.identifier.issn | 1565-3633 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/9742 | |
| dc.rights | Default Licence | - |
| dc.subject | octarepeat domain | en |
| dc.subject | binding details | en |
| dc.subject | metal complexes | en |
| dc.subject | prion protein | en |
| dc.subject | oligopeptides | en |
| dc.subject | stability | en |
| dc.subject | cu2+ | en |
| dc.subject | ions | en |
| dc.subject | palladium(ii) | en |
| dc.subject | thymopoietin | en |
| dc.title | Thermodynamic and structural characterization of the copper(II) complexes of peptides containing both histidyl and aspartyl residues | en |
| heal.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. Copyright (c) 2007. | en |
| heal.access | campus | - |
| heal.fullTextAvailability | TRUE | - |
| heal.identifier.primary | Doi 10.1155/2007/30394 | - |
| heal.identifier.secondary | <Go to ISI>://000252032200001 | - |
| heal.identifier.secondary | http://downloads.hindawi.com/journals/bca/2007/030394.pdf | - |
| heal.journalName | Bioinorg Chem Appl | en |
| heal.journalType | peer reviewed | - |
| heal.language | en | - |
| heal.publicationDate | 2007 | - |
| heal.publisher | Hindawi Publishing Corporation | en |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.type | journalArticle | - |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.type.en | Journal article | en |
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