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| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Zavitsanos, K. | en |
| dc.contributor.author | Nunes, A. M. | en |
| dc.contributor.author | Malandrinos, G. | en |
| dc.contributor.author | Hadjiliadis, N. | en |
| dc.date.accessioned | 2015-11-24T16:54:55Z | - |
| dc.date.available | 2015-11-24T16:54:55Z | - |
| dc.identifier.issn | 0162-0134 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/10220 | - |
| dc.rights | Default Licence | - |
| dc.subject | histone h2b | en |
| dc.subject | copper(ii) | en |
| dc.subject | toxicity | en |
| dc.subject | potentiometry | en |
| dc.subject | spectroscopy and epr | en |
| dc.subject | oxidative DNA-damage | en |
| dc.subject | n-terminal sequence | en |
| dc.subject | metal-ion complexes | en |
| dc.subject | l-histidine | en |
| dc.subject | coordination properties | en |
| dc.subject | mammalian chromatin | en |
| dc.subject | hydrogen-peroxide | en |
| dc.subject | cu(ii) complexes | en |
| dc.subject | alpha-synuclein | en |
| dc.subject | amino-acids | en |
| dc.title | Copper effective binding with 32-62 and 94-125 peptide fragments of histone H2B | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | DOI 10.1016/j.jinorgbio.2010.09.002 | - |
| heal.identifier.secondary | <Go to ISI>://000285433000015 | - |
| heal.identifier.secondary | http://ac.els-cdn.com/S0162013410002163/1-s2.0-S0162013410002163-main.pdf?_tid=f13e32763d63a53984da13c1a96c0854&acdnat=1333034668_78ca99b25ab9823468f638a5a8e14428 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 2011 | - |
| heal.abstract | In an attempt to investigate the role of histone H2B in Cu(II) induced toxicity and carcinogenesis we synthesized the terminally blocked peptides H2B(32-62) (SRKESYSVYVYKVLKQVH(48)PDTGISSKAMGIM) and H2B(94-125) (IQTAVRLLLPGELAKH(110)AVSEGTKAVTKYTSS) mimicking the N-terminal histone-fold domain and C-terminal tail of histone H2B respectively and studied their interaction with Cu(II) ions by means of potentiometric titrations and spectroscopic techniques (UV-visible CD and EPR) Both peptides H2B(32-62) and H2B(94-125) interacted efficiently with Cu(II) ions forming several species from pH 4 to 11 with His(48) and His(110) serving as anchors for metal binding In H2B(32-62) the effective Cu(II) binding is emphasized by the formation of a soluble Cu(II)-H2B(32-62) complex unlike the unbound peptide that precipitated over pH 79 At physiological pH both peptides form tetragonal 3N species with a {N(im) 2N(-)} coordination mode At this pH H2B(32-62) presented the formation of coordination isomers differentiated by the presence in one of them of an axial coordination of the carboxylate group of Asp50 Copper binding with both H2B(32-62) and H2B(94-125) may induce a conformational change in the peptides original structure At physiological conditions this effect may interfere with nucleosome s structure and dynamics including the ubiquitination of Lys(120) which is linked to gene silencing (C) 2010 Elsevier Inc All rights reserved | en |
| heal.publisher | Elsevier | en |
| heal.journalName | J Inorg Biochem | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Zavitsanos-2011-Copper effective bin.pdf | 1.11 MB | Adobe PDF | View/Open Request a copy |
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