Please use this identifier to cite or link to this item: https://www.arca.fiocruz.br/handle/icict/11955
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dc.contributor.authorGouvea, Ligiane R.
dc.contributor.authorMartins, Darliane A.
dc.contributor.authorBatista, Denise da Gama Jean
dc.contributor.authorSoeiro, Maria de Nazaré C.
dc.contributor.authorLouro, Sônia R. W.
dc.contributor.authorBarbeira, Paulo J. S.
dc.contributor.authorTeixeira, Letícia R.
dc.date.accessioned2015-10-16T12:49:41Z
dc.date.available2015-10-16T12:49:41Z
dc.date.issued2013
dc.identifier.citationGOUVEA, Ligiane R.; et al. Norfloxacin Zn(II)-based complexes: acid base ionization constant determination, DNA and albumin binding properties and the biological effect against Trypanosoma cruzi. Biometals, v.26, n.5, p.813-825, Oct. 2013.
dc.identifier.issn1572-8773
dc.identifier.urihttps://www.arca.fiocruz.br/handle/icict/11955
dc.language.isoeng
dc.publisherSpringer
dc.rightsrestricted access
dc.titleNorfloxacin Zn(II)-based complexes: acid base ionization constant determination, DNA and albumin binding properties and the biological effect against Trypanosoma cruzi
dc.typeArticle
dc.identifier.doi10.1007/s10534-013-9661-z
dc.description.abstractenZn(II) complexes with norfloxacin (NOR) in the absence or in the presence of 1,10-phenanthroline (phen) were obtained and characterized. In both complexes, the ligand NOR was coordinated through a keto and a carboxyl oxygen. Tetrahedral and octahedral geometries were proposed for [ZnCl2(NOR)]H2O (1) and [ZnCl2(NOR)(phen)]2H2O (2), respectively. Since the biological activity of the chemicals depends on the pH value, pH titrations of the Zn(II) complexes were performed. UV spectroscopic studies of the interaction of the complexes with calf-thymus DNA (CT DNA) have suggested that they can bind to CT DNA with moderate affinity in an intercalative mode. The interactions between the Zn(II) complexes and bovine serum albumin (BSA) were investigated by steady-state and time-resolved fluorescence spectroscopy at pH 7.4. The experimental data showed static quenching of BSA fluorescence, indicating that both complexes bind to BSA. A modified Stern–Volmer plot for the quenching by complex 2 demonstrated preferential binding near one of the two tryptophan residues of BSA. The binding constants obtained (Kb) showed that BSA had a two orders of magnitude higher affinity for complex 2 than for 1. The results also showed that the affinity of both complexes for BSA was much higher than for DNA. This preferential interaction with protein sites could be important to their biological mechanisms of action. The analysis in vitro of the Zn(II) complexes and corresponding ligand were assayed against Trypanosoma cruzi, the causative agent of Chagas disease and the data showed that complex 2 was the most active against bloodstream trypomastigotes.
dc.creator.affilliationUniversidade Federal de Minas Gerais. Departamento de Química. Belo Horizonte, MG, Brasil.
dc.creator.affilliationUniversidade Federal de Minas Gerais. Departamento de Química. Belo Horizonte, MG, Brasil.
dc.creator.affilliationFundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Biologia Celular. Rio de Janeiro, RJ, Brasil.
dc.creator.affilliationFundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Biologia Celular. Rio de Janeiro, RJ, Brasil.
dc.creator.affilliationPontifícia Universidade Católica do Rio de Janeiro. Departamento de Fìsica.Rio de Janeiro, RJ, Brasil.
dc.creator.affilliationUniversidade Federal de Minas Gerais. Departamento de Química. Belo Horizonte, MG, Brasil.
dc.creator.affilliationUniversidade Federal de Minas Gerais. Departamento de Química. Belo Horizonte, MG, Brasil.
dc.subject.enNorfloxacin
dc.subject.enZn(II) complexes
dc.subject.enAnti-T. cruzi activity
dc.subject.enAcid ionization constant
dc.subject.enInteraction with bovine serum albumin
dc.subject.enInteraction with DNA
dc.subject.enTrypanosoma cruzi
dc.subject.enChagas disease
dc.subject.decsNorfloxacino
dc.subject.decsTrypanosoma cruzi
dc.subject.decsDoença de Chagas
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