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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/31367
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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 |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbagen.2014.06.010 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) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
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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1844614381633011712 |
score |
13.070432 |