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dc.contributor.author
Garcia, Pablo Facundo
dc.contributor.author
Toneatto, Judith
dc.contributor.author
Silvero, María Jazmín
dc.contributor.author
Argüello, Gustavo Alejandro
dc.date.available
2017-12-22T14:59:32Z
dc.date.issued
2014-06
dc.identifier.citation
Argüello, Gustavo Alejandro; Silvero, María Jazmín; Toneatto, Judith; Garcia, Pablo Facundo; Binding of [Cr(phen)3]3+to transferrin at extracellular and endosomalpHs: Potential application in photodynamic therapy; Elsevier Science; Biochimica et Biophysica Acta- General Subjects; 1840; 9; 6-2014; 2695-2701
dc.identifier.issn
0304-4165
dc.identifier.uri
http://hdl.handle.net/11336/31367
dc.description.abstract
Background Transferrin is an iron-binding blood plasma glycoprotein that controls the level of free iron in biological fluids. This protein has been deeply studied in the past few years because of its potential use as a strategy of drug targeting to tumor tissues. Chromium complex, [Cr(phen)3]3+ (phen = 1,10-phenanthroline), has been proposed as photosensitizers for photodynamic therapy (PDT). Thus, we analyzed the binding of chromium complex, [Cr(phen)3]3+, to transferrin for a potential delivery of this diimine complex to tumor cells for PDT. Methods The interaction between [Cr(phen)3]3+ and holotransferrin (holoTf) was studied by fluorescence quenching technique, circular dichroism (CD) and ultraviolet (UV)–visible spectroscopy. Results [Cr(phen)3]3+ binds strongly to holoTf with a binding constant around 105 M−1, that depends on the pH. The thermodynamic parameters indicated that hydrophobic interactions played a major role in the binding processes. The CD studies showed that there are no conformational changes in the secondary and tertiary structures of the protein. Conclusions These results suggest that the binding process would occur in a site different from the specific iron binding sites of the protein and would be the same in both protein states. As secondary and tertiary structures of transferrin do not show remarkable changes, we propose that the TfR could recognize the holoTf despite having a chromium complex associated. General significance Understanding the interaction between [Cr(phen)3]3+ with transferrin is relevant because this protein could be a delivery agent of Cr(III) complex to tumor cells. This can allow us to understand further the role of Cr(III) complex as sensitizer in PDT.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Tris(1,10-Phenanthroline)Chromium(Iii)
dc.subject
Apotransferrin
dc.subject
Holotransferrin
dc.subject
Binding
dc.subject
Drug Delivery
dc.subject
Photodynamic Therapy
dc.subject.classification
Otras Ciencias Químicas
dc.subject.classification
Ciencias Químicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Binding of [Cr(phen)3]3+to transferrin at extracellular and endosomalpHs: Potential application in photodynamic therapy
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-12-21T16:30:12Z
dc.journal.volume
1840
dc.journal.number
9
dc.journal.pagination
2695-2701
dc.journal.pais
Países Bajos
dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Garcia, Pablo Facundo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina
dc.description.fil
Fil: Toneatto, Judith. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina
dc.description.fil
Fil: Silvero, María Jazmín. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina
dc.description.fil
Fil: Argüello, Gustavo Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina
dc.journal.title
Biochimica et Biophysica Acta- General Subjects
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.bbagen.2014.06.010
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S030441651400230X


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