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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/123456789/8247
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dc.contributor.authorZavitsanos, K.en
dc.contributor.authorNunes, A. M. P. C.en
dc.contributor.authorMalandrinos, G.en
dc.contributor.authorKallay, C.en
dc.contributor.authorSovago, I.en
dc.contributor.authorMagafa, V.en
dc.contributor.authorCordopatis, P.en
dc.contributor.authorHadjiliadis, N.en
dc.date.accessioned2015-11-24T16:40:13Z-
dc.date.available2015-11-24T16:40:13Z-
dc.identifier.issn1477-9226-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/8247-
dc.rightsDefault Licence-
dc.subjectc-terminal tailen
dc.subjectmetal-binding sequenceen
dc.subjectaromatic ring stackingen
dc.subjectbeta-amyloid peptideen
dc.subjectcopper(ii) complexesen
dc.subjectoxidative damageen
dc.subjectsolid-phaseen
dc.subjectcoordination propertiesen
dc.subjecthistidyl residuesen
dc.subjectalpha-synucleinen
dc.titleInteraction of Cu(II) and Ni(II) with the 63-93 fragment of histone H2Ben
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.primaryDoi 10.1039/B810354b-
heal.identifier.secondary<Go to ISI>://000260644000016-
heal.identifier.secondaryhttp://pubs.rsc.org/en/content/articlepdf/2008/dt/b810354b-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείαςel
heal.publicationDate2008-
heal.abstractChromatin proteins are believed to represent reactive sites for metal ion binding. We have synthesized the 31 amino acid peptide Ac-NSFVNDIFERIAGEASRLAHYNKRSTITSRE-NH(2), corresponding to the 63-93 fragment of the histone H2B and studied its interaction with Cu(II) and Ni(II). Potentiometric and spectroscopic studies (UV-vis, CD, NMR and EPR) showed that histidine 21 acts as an anchoring binding site for the metal ion. Complexation of the studied peptide with Cu(II) starts at pH 4 with the formation of the monodentate species CuH(2)L. At physiological pH values, the 3N complex {N(Im), 2N(-)}, CuL is favoured while at basic pH values the 4N {N(Im), 3N(-)} coordination mode is preferred. Ni(II) forms several complexes with the peptide starting from the distorted octahedral NiH(2)L at about neutral pH, to a square planar complex where the peptide is bound through a {N(Im), 3N(-)} mode in an equatorial plane at basic pH values. These results could be important in revealing more information about the mechanism of metal induced toxicity and carcinogenesis.en
heal.publisherRoyal Society of Chemistryen
heal.journalNameDalton Transactionsen
heal.journalTypepeer reviewed-
heal.fullTextAvailabilityTRUE-
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