Binding of [Cr(phen)3]3+to transferrin at extracellular and endosomalpHs: Potential application in photodynamic therapy

Autores
Garcia, Pablo Facundo; Toneatto, Judith; Silvero, María Jazmín; Argüello, Gustavo Alejandro
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
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
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
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
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
Materia
Tris(1,10-Phenanthroline)Chromium(Iii)
Apotransferrin
Holotransferrin
Binding
Drug Delivery
Photodynamic Therapy
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/31367

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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Binding of [Cr(phen)3]3+to transferrin at extracellular and endosomalpHs: Potential application in photodynamic therapyGarcia, Pablo FacundoToneatto, JudithSilvero, María JazmínArgüello, Gustavo AlejandroTris(1,10-Phenanthroline)Chromium(Iii)ApotransferrinHolotransferrinBindingDrug DeliveryPhotodynamic Therapyhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Background 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.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; ArgentinaFil: 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; ArgentinaFil: 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; ArgentinaFil: 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; ArgentinaElsevier Science2014-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/31367Argüello, 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; 2695-27010304-4165CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbagen.2014.06.010info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S030441651400230Xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:36:10Zoai:ri.conicet.gov.ar:11336/31367instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:36:11.017CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Binding of [Cr(phen)3]3+to transferrin at extracellular and endosomalpHs: Potential application in photodynamic therapy
title Binding of [Cr(phen)3]3+to transferrin at extracellular and endosomalpHs: Potential application in photodynamic therapy
spellingShingle Binding of [Cr(phen)3]3+to transferrin at extracellular and endosomalpHs: Potential application in photodynamic therapy
Garcia, Pablo Facundo
Tris(1,10-Phenanthroline)Chromium(Iii)
Apotransferrin
Holotransferrin
Binding
Drug Delivery
Photodynamic Therapy
title_short Binding of [Cr(phen)3]3+to transferrin at extracellular and endosomalpHs: Potential application in photodynamic therapy
title_full Binding of [Cr(phen)3]3+to transferrin at extracellular and endosomalpHs: Potential application in photodynamic therapy
title_fullStr Binding of [Cr(phen)3]3+to transferrin at extracellular and endosomalpHs: Potential application in photodynamic therapy
title_full_unstemmed Binding of [Cr(phen)3]3+to transferrin at extracellular and endosomalpHs: Potential application in photodynamic therapy
title_sort Binding of [Cr(phen)3]3+to transferrin at extracellular and endosomalpHs: Potential application in photodynamic therapy
dc.creator.none.fl_str_mv Garcia, Pablo Facundo
Toneatto, Judith
Silvero, María Jazmín
Argüello, Gustavo Alejandro
author Garcia, Pablo Facundo
author_facet Garcia, Pablo Facundo
Toneatto, Judith
Silvero, María Jazmín
Argüello, Gustavo Alejandro
author_role author
author2 Toneatto, Judith
Silvero, María Jazmín
Argüello, Gustavo Alejandro
author2_role author
author
author
dc.subject.none.fl_str_mv Tris(1,10-Phenanthroline)Chromium(Iii)
Apotransferrin
Holotransferrin
Binding
Drug Delivery
Photodynamic Therapy
topic Tris(1,10-Phenanthroline)Chromium(Iii)
Apotransferrin
Holotransferrin
Binding
Drug Delivery
Photodynamic Therapy
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv 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.
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
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
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
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
description 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.
publishDate 2014
dc.date.none.fl_str_mv 2014-06
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/31367
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
0304-4165
CONICET Digital
CONICET
url http://hdl.handle.net/11336/31367
identifier_str_mv 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
0304-4165
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
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info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S030441651400230X
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
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reponame_str CONICET Digital (CONICET)
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instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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