Coordination properties of Cu(II) and Ni(II) ions towards the C-terminal peptide fragment-TYTEHA-of histone H4
dc.contributor.author | Karavelas, T. | en |
dc.contributor.author | Malandrinos, G. | en |
dc.contributor.author | Hadjiliadis, N. | en |
dc.contributor.author | Mlynarz, P. | en |
dc.contributor.author | Kozlowski, H. | en |
dc.contributor.author | Barsamd, M. | en |
dc.contributor.author | Butlerd, I. | en |
dc.date.accessioned | 2015-11-24T16:54:54Z | |
dc.date.available | 2015-11-24T16:54:54Z | |
dc.identifier.issn | 1477-9226 | - |
dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/10217 | |
dc.rights | Default Licence | - |
dc.subject | metal-binding sequence | en |
dc.subject | oxidative damage | en |
dc.subject | tail | en |
dc.subject | h2a | en |
dc.subject | complexes | en |
dc.subject | nickel(ii) | en |
dc.subject | h3 | en |
dc.subject | ch3co-cys-ala-ile-his-nh2 | en |
dc.subject | stability | en |
dc.subject | histidine | en |
dc.title | Coordination properties of Cu(II) and Ni(II) ions towards the C-terminal peptide fragment-TYTEHA-of histone H4 | en |
heal.abstract | In order to reveal more information about the toxicity caused by metals and furthermore their influence to the physiological metabolism of the cell, the hexapeptide model Ac-ThrTyrThrGluHisAla-am representing the C-terminal 71-76 fragment of histone H4 which lies into the nucleosome core, was synthesized. A combined pH-metric and spectroscopic UV-VIS, EPR, CD and NMR study of Ni(II) and Cu(II) binding to the blocked hexapeptide, revealed the formation of octahedral complexes involving imidazole nitrogen of histidine, at pH 5 and pH 7 for Cu(II) and Ni(II) ions respectively. In basic solutions a major square-planar 4 N Ni(II)-complex, adopting a {N-Im, 3N(-)} coordination mode, was formed. In the case of Cu(II) ions, a 3 N complex, involving the imidazole nitrogen of histidine and two deprotonated amide nitrogens of the backbone of the peptide, at pH 7 and a series of 4 N complexes starting at pH 6.5, were suggested. In addition Ni(II)-mediated hydrolysis of the peptide bond-Tyr-Thr was evident following our experimental data. | en |
heal.access | campus | - |
heal.fullTextAvailability | TRUE | - |
heal.identifier.primary | Doi 10.1039/B716863b | - |
heal.identifier.secondary | <Go to ISI>://000253492000013 | - |
heal.identifier.secondary | http://pubs.rsc.org/en/content/articlepdf/2008/dt/b716863b | - |
heal.journalName | Dalton Transactions | en |
heal.journalType | peer reviewed | - |
heal.language | en | - |
heal.publicationDate | 2008 | - |
heal.publisher | Royal Society of Chemistry | 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 |
Αρχεία
Φάκελος/Πακέτο αδειών
1 - 1 of 1
Φόρτωση...
- Ονομα:
- license.txt
- Μέγεθος:
- 1.74 KB
- Μορφότυπο:
- Item-specific license agreed upon to submission
- Περιγραφή: