Copper effective binding with 32-62 and 94-125 peptide fragments of histone H2B (EN)

Zavitsanos, K. (EN)

Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας (EL)

Zavitsanos, K. (EN)

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)

histone h2b (EN)

Πανεπιστήμιο Ιωαννίνων

Ιδρυματικό Αποθετήριο Ολυμπιάς

Σχολή Θετικών Επιστημών

Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

ΑΠΟΘΕΤΗΡΙΟ "ΟΛΥΜΠΙΑΣ"

Τμήμα Χημείας

J Inorg Biochem (EN)

Αγγλική γλώσσα

2011

http://olympias.lib.uoi.gr/jspui/handle/123456789/10220

<Go to ISI>://000285433000015

Elsevier (EN)