The binding of Ni(II) ions to terminally blocked hexapeptides derived from the metal binding -ESHH- motif of histone H2A
Φόρτωση...
Ημερομηνία
Συγγραφείς
Mylonas, M.
Krezel, A.
Plakatouras, J. C.
Hadjiliadis, N.
Bal, W.
Τίτλος Εφημερίδας
Περιοδικό ISSN
Τίτλος τόμου
Εκδότης
The Royal Society of Chemistry
Περίληψη
Τύπος
Είδος δημοσίευσης σε συνέδριο
Είδος περιοδικού
peer reviewed
Είδος εκπαιδευτικού υλικού
Όνομα συνεδρίου
Όνομα περιοδικού
Journal of the Chemical Society-Dalton Transactions
Όνομα βιβλίου
Σειρά βιβλίου
Έκδοση βιβλίου
Συμπληρωματικός/δευτερεύων τίτλος
Περιγραφή
The coordination properties of Ni(II) ions towards the terminally blocked (CH3CONH- and - CONH2) hexapeptides -TESHHK-, -TASHHK-, -TEAHHK-, -TESAHK- and -TESHAK- were studied by using potentiometric and spectroscopic techniques ( UV/Vis, CD, NMR). The peptides were chosen in such a way as to compare the effect of Glu, Ser and His residues on the stability, the coordination and hydrolytic abilities of the complexes formed. All peptides bind to Ni(II) ions initially through one or two imidazole nitrogens in weakly acidic and neutral solutions forming slightly distorted octahedral complexes. At higher pH values, a series of square-planar complexes are formed, where Ni(II) ions bind simultaneously through an imidazole and three amide nitrogens in an equatorial plane. This proposed conformation includes the participation of only one imidazole nitrogen, in the case of all peptides, in the coordination sphere of Ni(II) ions. In basic solutions, the peptides - TASHHK- and - TESAHK were hydrolyzed in a Ni(II)-assisted fashion. No hydrolytic processes were noticed in peptides - TEAHHK- and - TESHAK- where the Ser or His-5 residues are replaced with the Ala residue. The Ni(II)-assisted hydrolysis of the analogues of - TESHHK- may provide an insight into the novel mechanism of genotoxicity, combining the damage to the nucleosome with the generation of further toxic Ni(II) species.
Περιγραφή
Λέξεις-κλειδιά
oxidative damage, nickel carcinogenesis, copper(ii) complexes, l-histidine, sequence, tail, stability, h3, ch3co-cys-ala-ile-his-nh2, coordination
Θεματική κατηγορία
Παραπομπή
Σύνδεσμος
<Go to ISI>://000179238000033
http://pubs.rsc.org/en/content/articlepdf/2002/dt/b206585a
http://pubs.rsc.org/en/content/articlepdf/2002/dt/b206585a
Γλώσσα
en
Εκδίδον τμήμα/τομέας
Όνομα επιβλέποντος
Εξεταστική επιτροπή
Γενική Περιγραφή / Σχόλια
Ίδρυμα και Σχολή/Τμήμα του υποβάλλοντος
Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας