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dc.contributor.authorRubio Antolin, Ana Rosa 
dc.contributor.authorFidalgo Zorrilla, Jairo 
dc.contributor.authorMartin Vargas, Judit
dc.contributor.authorPérez Arnáiz, Cristina 
dc.contributor.authorAlonso de la Torre, Sara 
dc.contributor.authorBiver, Tarita
dc.contributor.authorEspino Ordóñez, Gustavo 
dc.contributor.authorBusto Vázquez, Natalia 
dc.contributor.authorGarcía Ruiz, Begoña 
dc.date.accessioned2019-12-16T10:32:02Z
dc.date.available2019-12-16T10:32:02Z
dc.date.issued2020-02
dc.identifier.issn0162-0134
dc.identifier.urihttp://hdl.handle.net/10259/5194
dc.description.abstractThe synthesized 2-(hydroxy-1-naphtyl)imidazo-[4,5-f][1,10]phenanthroline (HNAIP) ligand and its new iridium ([Ir(ppy)2(HNAIP)]Cl) and rhodium ([Rh(ppy)2(HNAIP)]Cl) complexes, being ppy = 2-phenylpiridinate, show cytotoxic effects in SW480 (colon adenocarcinoma) and A549 (epithelial lung adenocarcinoma) cells. They all are cytotoxic in the tested cell lines. HNAIP and [Rh(ppy)2(HNAIP)]+ are the most cytotoxic, whereas [Ir(ppy)2(HNAIP)]+ displays negligible cytotoxicity towards A549 cells and moderate activity towards SW480. The interaction of all three compounds with Bovine Serum Albumin (BSA), l-glutathione reduced (GSH), nicotinamide adenine dinucleotide (NADH) and DNA was studied to explain the differences found in terms of cytotoxicity. None of them are able to interact with BSA, thus excluding bioavailability due to plasma protein interaction as the possible differentiating factor in their biological activity. By contrast, small differences have been observed regarding DNA interaction. In addition, taking advantage of the emission properties of these molecules, they have been visualized in the cytoplasmic region of A549 cells. Inductively coupled plasma mass spectrometry (ICP-MS) experiments show, in turn, that the internalization ability follow the sequence [Rh(ppy)2(HNAIP)]+ > [Ir(ppy)2(HNAIP)]+ > cisplatin. Therefore, it seems clear that the cellular uptake by tumour cells is the key factor affecting the different cytotoxicity of the metal complexes and that this cellular uptake is influenced by the hydrophobicity of the studied complexes. On the other hand, preliminary catalytic experiments performed on the photo-oxidation of GSH and some amino acids such as l-methionine (Met), l-cysteine (Cys) and l-tryptophan (Trp) provide evidence for the photocatalytic activity of the Ir(III) complex in this type of reactions.en
dc.description.sponsorship“la Caixa” Banking Foundation (LCF/PR/PR12/11070003), Ministerio de Ciencia, Innovación y Universidades (RTI2018-102040-B-100 and RTI2018-100709-B-C21), Junta de Castilla y León (BU305P18, FEDER Funds)es
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.publisherElsevieres
dc.relation.ispartofJournal of Inorganic Biochemistry. 2019, V. 203, 110885
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subject2-(hydroxy-1-naphtyl)imidazo-[4,5-f]en
dc.subject[1,10]phenanthrolineen
dc.subjectIridiumen
dc.subjectRhodiumen
dc.subjectCellular testen
dc.subjectDNAen
dc.subjectPhoto-catalysisen
dc.subject.otherBioquímicaes
dc.subject.otherBiochemistryen
dc.subject.otherQuímica inorgánicaes
dc.subject.otherChemistry, Inorganicen
dc.titleBiological activity and photocatalytic properties of a naphthyl-imidazo phenanthroline (HNAIP) ligand and its [Ir(ppy)2(HNAIP)]Cl and [Rh(ppy)2(HNAIP)]Cl complexesen
dc.typeinfo:eu-repo/semantics/articleen
dc.rights.holderAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.accessRightsinfo:eu-repo/semantics/openAccess
dc.relation.publisherversionhttps://doi.org/10.1016/j.jinorgbio.2019.110885
dc.identifier.doi10.1016/j.jinorgbio.2019.110885
dc.relation.projectIDinfo:eu-repo/grantAgreement/MICINN/RTI2018-102040-B-100
dc.relation.projectIDinfo:eu-repo/grantAgreement/MICINN/RTI2018-100709-B-C21
dc.relation.projectIDinfo:eu-repo/grantAgreement/JCyL/BU305P18
dc.relation.projectIDinfo:eu-repo/grantAgreement/FundaciónLaCaixa/LCF/PR/PR12/11070003
dc.type.hasVersioninfo:eu-repo/semantics/acceptedVersion


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