Találati lista | Tudóstér

001-es BibID:	BIBFORM016459
Első szerző:	Csapó Edit (vegyész)
Cím:	Syntheses and characterization of Cu2+, Ni2+ and Zn2+ binding capability of histidinehydroxamic acid derivatives / Edit Csapó, Péter Buglyó, Nóra Veronika Nagy, M. Amélia Santos, Alma Coronad, Etelka Farkas
Dátum:	2010
ISSN:	0277-5387
Megjegyzések:	Two histidinehydroxamic acid derivatives (N-methyl-histidinehydroxamic acid, N-Me-Hisha and Z-histidinehydroxamic acid, Z-Hisha) have been synthesized and their complexation with Cu2+-, Ni2+- and Zn2+-ions has been studied by using pH-potentiometric, UV-Vis, CD, H-1 NMR, EPR and ESI-MS methods. Both of the two new derivatives contain one donor atom less compared to the histidinehydroxamic acid (Hisha). In the case of N-Me-Hisha the hydroxamate-N as donor is eliminated, while the coordination of the amino-N of Z-Hisha is not possible at all. With the ambidentate N-Me-Hisha, the histamine-type coordination mode is favoured if the metal ion is Ni2+ and the bis-[NH2,N-imid] complex is the most stable in this system. The mixed type, [NH2,N-imid] + [O,O], coordination mode dominates in the Cu2+- N-Me-Hisha complexes, while different low stability mono-chelated linkage isomers are formed with Zn2+. With Z-Hisha (having poor water solubility) hydroxamate-type coordination mode predominates in low stability complexes in the Ni2+ and Zn2+ containing systems. Interestingly, the interaction with Cu2+ is very strong and results in the formation of a high stability 12-MC-4 type metallacrown with involvement of 5-membered and 7-membered chelates. (C) 2010 Elsevier Ltd. All rights reserved.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban Histidinehydroxamic acid derivatives Cu2+-, Ni2+-, Zn2+-complexes Solution equilibrium Potential metalloenzyme inhibitors matrix-metalloproteinase inhibitors mixed-ligand complexes aqueous-solution hydroxamic acids aminohydroxamic acids copper(ii) complexes methioninehydroxamic acids dissociation-constants metal complexation coordination
Megjelenés:	Polyhedron. - 29 : 16 (2010), p. 3137-3145. -
További szerzők:	Buglyó Péter (1965-) (vegyész) Nagy Nóra Veronika Santos, Amélia M. Corona, Alma Farkas Etelka (1948-) (vegyész)
Internet cím:	DOI Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon:

001-es BibID:	BIBFORM010515
Első szerző:	Farkas Etelka (vegyész)
Cím:	Metal-binding ability of histidine-containing peptidehydroxamic acids: Imidazole versus hydroxamate coordination / Etelka Farkas, Edit Csapó, Péter Buglyó, Chiara A. Damante, Giuseppe Di Natale
Dátum:	2009
ISSN:	0020-1693
Megjegyzések:	Three new peptidehydroxamic acids (L-alanyl-L-histidinehydroxamic acid, L-Ala-L-HisNHOH, L-alanyl-L-alanyl-L-histidinehydroxamic acid, L-Ala-L-Ala-L-HisNHOH and L-histidyl-L-alaninehydroxamic acid, LHis-L- AlaNHOH) were synthesized and their complexation with Cu(II), Ni(II) and Zn(II) were studied by pH-potentiometric, UV-Vis, CD, H-1 NMR, EPR and ESI-MS methods. Each of the studied peptide derivatives involves one side-chain imidazole unit and the effect of this group on the metal binding of the hydroxamic moiety is evaluated in the paper. The obtained results are compared to those of the complexes of some histidine-containing di- or tripeptides and also to those of hydroxamic derivatives of aliphatic peptides. A competition between the hydroxamate and imidazole functions occurs in all systems, but the extent differs from metal to metal, from ligand to ligand and depends very much on the pH. The imidazole was found to play the most determinant role in the Cu(II) complexes, somewhat less in the Ni(II)-containing ones, while (except the case of L-Ala-L-HisNHOH) negligible role was found in the Zn(II)- complexes. Common feature of the Ni(II)- and especially Cu(II)-containing systems is that if an imidazole-N is displaced by a hydroxamate, imidazole-bridged di- and polynuclear complexes are formed. (C) 2008 Elsevier B. V. All rights reserved.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Inorganica Chimica Acta. - 362 : 3 (2009), p. 753-762. -
További szerzők:	Csapó Edit (1983-) (vegyész) Buglyó Péter (1965-) (vegyész) Damante, Chiara A. Di Natale, Giuseppe
Internet cím:	DOI Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon:

001-es BibID:	BIBFORM006191
Első szerző:	Farkas Etelka (vegyész)
Cím:	Effects of imidazole containing Rc substituents on the metal binding capability of potentially metalloenzyme inhibitor hydroxamic acids / Etelka Farkas, Edit Csapó, Péter Buglyó
Dátum:	2008
ISSN:	1257-2535
Megjegyzések:	The role of R-C substituents, involving imidazole moiety, in complexation of various potentially metalloenzyme inhibitor hydroxamic acids, R-C-CO-N(R-N)-OH, (derivatives of amino acids and small peptides) with Cu(II), Ni(II) and Zn(II) ions has been investigated using pH-potentiometry and different spectroscopic methods. Many factors were found to affect the competition of the imidazole with the hydroxamate moiety for the metal ions, e.g. the distance between these two functions, presence/absence of additional donor in the R-C chain, sort of metal ion. The structure effect relation is planned to evaluate in the presentation.N2 - The role of R-C substituents, involving imidazole moiety, in complexation of various potentially metalloenzyme inhibitor hydroxamic acids, R-C-CO-N(R-N)-OH, (derivatives of amino acids and small peptides) with Cu(II), Ni(II) and Zn(II) ions has been investigated using pH-potentiometry and different spectroscopic methods. Many factors were found to affect the competition of the imidazole with the hydroxamate moiety for the metal ions, e.g. the distance between these two functions, presence/absence of additional donor in the R-C chain, sort of metal ion. The structure effect relation is planned to evaluate in the presentation.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban hydroxamic acid imidazole metal complexes metalloenzyme inhibitors Histidyl residues complexes peptides ligands stability
Megjelenés:	Metal ions in biology and medicine. - 10 (2008), p. 393-398. -
További szerzők:	Csapó Edit (1983-) (vegyész) Buglyó Péter (1965-) (vegyész)
Internet cím:	elektronikus változat
Borító:
Saját polcon:

001-es BibID:	BIBFORM003007
035-os BibID:	(WOS)000244439600002
Első szerző:	Farkas Etelka (vegyész)
Cím:	Synthesis and characterization of Cu2+, Ni2+ and Zn2+ binding capability of some amino- and imidazole hydroxamic acids : effects of substitution of side chain amino-N for imidazole-N or hydroxamic-N-H for -N-CH3 on metal complexation / Etelka Farkas, Dávid Bátka, Edit Csapó, Péter Buglyó, Wolfgang Haase, Daniele Sanna
Dátum:	2007
ISSN:	0277-5387
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Polyhedron. - 26 : 3 (2007), p. 543-554. -
További szerzők:	Bátka Dávid (1980-) (vegyész) Csapó Edit (1983-) (vegyész) Buglyó Péter (1965-) (vegyész) Haase, Wolfgang Sanna, Daniele (1956-) (vegyész)
Pályázati támogatás:	OTKA T 049612 OTKA OTKA T 046366 OTKA
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI
Borító:
Saját polcon: