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001-es BibID:	BIBFORM006223
Első szerző:	Zavitsanos, Kimon
Cím:	Interaction of Cu(II) and Ni(II) with the 63-93 fragment of histone H2B / Zavitsanos, K., Nunes, A. M. P. C., Malandrinos, G., Kallay, C., Sovago, I., Magafa, V., Cordopatis, P., Hadjiliadis, N.
Dátum:	2008
ISSN:	1477-9226
Megjegyzések:	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.N2 - 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.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Dalton Transactions. - 44 (2008), p. 6179-6187. -
További szerzők:	Nunes, Ana Mónica P. C. Malandrinos, Gerasimos Kállay Csilla (1978-) (vegyész) Sóvágó Imre (1946-) (vegyész) Magafa, Vassiliki Cordopatis, Paul Hadjiliadis, Nick
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