Interaction of Cu(II) and Ni(II) with the 63-93 fragment of histone H2B

Chromatin proteins are believed to represent reactive sites for metal ion binding. We have synthesized the 31 amino acid peptide Ac-NSFVNDIFERIAGEASRLAHYNKRSTITSRE-NH2, corresponding to the 63-93 fragment of the histone H2B and studied its interaction with Cu(II) and Ni(II). Potentiometric and spect...

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Bibliographic Details
Published in:Dalton transactions : an international journal of inorganic chemistry 2008-01 (44), p.6179
Main Authors: Zavitsanos, Kimon, Nunes, Ana Mónica P C, Malandrinos, Gerasimos, Kállay, Csilla, Sóvágó, Imre, Magafa, Vassiliki, Cordopatis, Paul, Hadjiliadis, Nick
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Binding Sites
Copper - chemistry
Copper - metabolism
Histones - chemistry
Histones - metabolism
Molecular Sequence Data
Nickel - chemistry
Nickel - metabolism
Peptides - chemical synthesis
Peptides - chemistry
Peptides - metabolism
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Summary:Chromatin proteins are believed to represent reactive sites for metal ion binding. We have synthesized the 31 amino acid peptide Ac-NSFVNDIFERIAGEASRLAHYNKRSTITSRE-NH2, 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 CuH2L. 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 NiH2L 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.
ISSN:1477-9226
1477-9234
DOI:10.1039/b810354b