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  5. Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ
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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/10217
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dc.contributor.authorKaravelas, T.en
dc.contributor.authorMalandrinos, G.en
dc.contributor.authorHadjiliadis, N.en
dc.contributor.authorMlynarz, P.en
dc.contributor.authorKozlowski, H.en
dc.contributor.authorBarsamd, M.en
dc.contributor.authorButlerd, I.en
dc.date.accessioned2015-11-24T16:54:54Z-
dc.date.available2015-11-24T16:54:54Z-
dc.identifier.issn1477-9226-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/10217-
dc.rightsDefault Licence-
dc.subjectmetal-binding sequenceen
dc.subjectoxidative damageen
dc.subjecttailen
dc.subjecth2aen
dc.subjectcomplexesen
dc.subjectnickel(ii)en
dc.subjecth3en
dc.subjectch3co-cys-ala-ile-his-nh2en
dc.subjectstabilityen
dc.subjecthistidineen
dc.titleCoordination properties of Cu(II) and Ni(II) ions towards the C-terminal peptide fragment-TYTEHA-of histone H4en
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primaryDoi 10.1039/B716863b-
heal.identifier.secondary<Go to ISI>://000253492000013-
heal.identifier.secondaryhttp://pubs.rsc.org/en/content/articlepdf/2008/dt/b716863b-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate2008-
heal.abstractIn 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.publisherRoyal Society of Chemistryen
heal.journalNameDalton Transactionsen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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