Advances on the interaction of polypyridyl Cr(III) complexes with transporting proteins and its potential relevance in photodynamic therapy

Autores
Toneatto, Judith; Garcia, Pablo Facundo; Arguello, Gerardo
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The present study reports a detailed investigation into the interaction of [Cr(phen) 2(dppz)] 3+ and [Cr(phen) 3] 3+ with transferrin, the key protein for the transport of Fe 3+ in blood plasma; its cycle holds promise as an attractive system for strategies of drug targeting to tumor tissues. This can allow us to understand further the role of both complexes as sensitizers in photodynamic therapy (PDT). Chromium(III) complexes, [Cr(phen) 2(dppz)] 3+ and [Cr(phen) 3] 3+, (phen = 1,10-phenanthroline and dppz = dipyridophenazine), where dppz is a planar bidentate ligand with an extended π system, have been found to bind strongly with apotransferrin (apoTf) with an intrinsic binding constant, K b, of (1.8 ± 0.3) × 10 5 M - 1 and (1.1 ± 0.1) × 10 5 M - 1 at 299 K, for apoTf-[Cr(phen) 2(dppz)] 3+ and apoTf-[Cr(phen) 3] 3+, respectively. The interactions of apoTf with the different Cr(III) complexes were assessed employing UV-visible absorption, fluorescence and circular dichroism spectroscopy. The relative fluorescence intensity of the protein decreased when the increasing concentration of Cr(III) complex was added, suggesting that perturbation around the Trp and Tyr residues took place. The analysis of the thermodynamic parameters ΔG, ΔH, ΔS indicated that the presence of the Cr(III) complex stabilizes the protein with a strong entropic contribution. The binding distances and transfer efficiencies for apoTf-[Cr(phen) 2(dppz)] 3+ and apoTf-[Cr(phen) 3] 3+ binding reactions were calculated according to Föster theory of non-radiation energy transfer. All these experimental results suggest that [Cr(phen) 2(dppz)] 3+ and [Cr(phen) 3] 3+ bind strongly to apoTf indicating that this protein could act as a carrier of these complexes for further applications in PDT. © 2011 Elsevier Inc. All rights reserved.
Fil: Toneatto, Judith. 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: 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: Arguello, Gerardo. 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
Binding Study
Chromium(Iii) Complexes
Fluorescence Quenching
Thermodynamic Parameters
Transferrin
Transporting Protein
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:11336/61577
Acceder
id CONICETDig_3d282c3085a1dc2321987dc033b83855
oai_identifier_str oai:ri.conicet.gov.ar:11336/61577
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Advances on the interaction of polypyridyl Cr(III) complexes with transporting proteins and its potential relevance in photodynamic therapyToneatto, JudithGarcia, Pablo FacundoArguello, GerardoBinding StudyChromium(Iii) ComplexesFluorescence QuenchingThermodynamic ParametersTransferrinTransporting Proteinhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The present study reports a detailed investigation into the interaction of [Cr(phen) 2(dppz)] 3+ and [Cr(phen) 3] 3+ with transferrin, the key protein for the transport of Fe 3+ in blood plasma; its cycle holds promise as an attractive system for strategies of drug targeting to tumor tissues. This can allow us to understand further the role of both complexes as sensitizers in photodynamic therapy (PDT). Chromium(III) complexes, [Cr(phen) 2(dppz)] 3+ and [Cr(phen) 3] 3+, (phen = 1,10-phenanthroline and dppz = dipyridophenazine), where dppz is a planar bidentate ligand with an extended π system, have been found to bind strongly with apotransferrin (apoTf) with an intrinsic binding constant, K b, of (1.8 ± 0.3) × 10 5 M - 1 and (1.1 ± 0.1) × 10 5 M - 1 at 299 K, for apoTf-[Cr(phen) 2(dppz)] 3+ and apoTf-[Cr(phen) 3] 3+, respectively. The interactions of apoTf with the different Cr(III) complexes were assessed employing UV-visible absorption, fluorescence and circular dichroism spectroscopy. The relative fluorescence intensity of the protein decreased when the increasing concentration of Cr(III) complex was added, suggesting that perturbation around the Trp and Tyr residues took place. The analysis of the thermodynamic parameters ΔG, ΔH, ΔS indicated that the presence of the Cr(III) complex stabilizes the protein with a strong entropic contribution. The binding distances and transfer efficiencies for apoTf-[Cr(phen) 2(dppz)] 3+ and apoTf-[Cr(phen) 3] 3+ binding reactions were calculated according to Föster theory of non-radiation energy transfer. All these experimental results suggest that [Cr(phen) 2(dppz)] 3+ and [Cr(phen) 3] 3+ bind strongly to apoTf indicating that this protein could act as a carrier of these complexes for further applications in PDT. © 2011 Elsevier Inc. All rights reserved.Fil: Toneatto, Judith. 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: 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: Arguello, Gerardo. 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 Science Inc2011-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/61577Toneatto, Judith; Garcia, Pablo Facundo; Arguello, Gerardo; Advances on the interaction of polypyridyl Cr(III) complexes with transporting proteins and its potential relevance in photodynamic therapy; Elsevier Science Inc; Journal of Inorganic Biochemistry; 105; 10; 10-2011; 1299-13050162-0134CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.jinorgbio.2011.07.013info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0162013411001930info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-12-17T14:14:54Zoai:ri.conicet.gov.ar:11336/61577instacron: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:34982025-12-17 14:14:55.022CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Advances on the interaction of polypyridyl Cr(III) complexes with transporting proteins and its potential relevance in photodynamic therapy
title Advances on the interaction of polypyridyl Cr(III) complexes with transporting proteins and its potential relevance in photodynamic therapy
spellingShingle Advances on the interaction of polypyridyl Cr(III) complexes with transporting proteins and its potential relevance in photodynamic therapy
Toneatto, Judith
Binding Study
Chromium(Iii) Complexes
Fluorescence Quenching
Thermodynamic Parameters
Transferrin
Transporting Protein
title_short Advances on the interaction of polypyridyl Cr(III) complexes with transporting proteins and its potential relevance in photodynamic therapy
title_full Advances on the interaction of polypyridyl Cr(III) complexes with transporting proteins and its potential relevance in photodynamic therapy
title_fullStr Advances on the interaction of polypyridyl Cr(III) complexes with transporting proteins and its potential relevance in photodynamic therapy
title_full_unstemmed Advances on the interaction of polypyridyl Cr(III) complexes with transporting proteins and its potential relevance in photodynamic therapy
title_sort Advances on the interaction of polypyridyl Cr(III) complexes with transporting proteins and its potential relevance in photodynamic therapy
dc.creator.none.fl_str_mv Toneatto, Judith
Garcia, Pablo Facundo
Arguello, Gerardo
author Toneatto, Judith
author_facet Toneatto, Judith
Garcia, Pablo Facundo
Arguello, Gerardo
author_role author
author2 Garcia, Pablo Facundo
Arguello, Gerardo
author2_role author
author
dc.subject.none.fl_str_mv Binding Study
Chromium(Iii) Complexes
Fluorescence Quenching
Thermodynamic Parameters
Transferrin
Transporting Protein
topic Binding Study
Chromium(Iii) Complexes
Fluorescence Quenching
Thermodynamic Parameters
Transferrin
Transporting Protein
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The present study reports a detailed investigation into the interaction of [Cr(phen) 2(dppz)] 3+ and [Cr(phen) 3] 3+ with transferrin, the key protein for the transport of Fe 3+ in blood plasma; its cycle holds promise as an attractive system for strategies of drug targeting to tumor tissues. This can allow us to understand further the role of both complexes as sensitizers in photodynamic therapy (PDT). Chromium(III) complexes, [Cr(phen) 2(dppz)] 3+ and [Cr(phen) 3] 3+, (phen = 1,10-phenanthroline and dppz = dipyridophenazine), where dppz is a planar bidentate ligand with an extended π system, have been found to bind strongly with apotransferrin (apoTf) with an intrinsic binding constant, K b, of (1.8 ± 0.3) × 10 5 M - 1 and (1.1 ± 0.1) × 10 5 M - 1 at 299 K, for apoTf-[Cr(phen) 2(dppz)] 3+ and apoTf-[Cr(phen) 3] 3+, respectively. The interactions of apoTf with the different Cr(III) complexes were assessed employing UV-visible absorption, fluorescence and circular dichroism spectroscopy. The relative fluorescence intensity of the protein decreased when the increasing concentration of Cr(III) complex was added, suggesting that perturbation around the Trp and Tyr residues took place. The analysis of the thermodynamic parameters ΔG, ΔH, ΔS indicated that the presence of the Cr(III) complex stabilizes the protein with a strong entropic contribution. The binding distances and transfer efficiencies for apoTf-[Cr(phen) 2(dppz)] 3+ and apoTf-[Cr(phen) 3] 3+ binding reactions were calculated according to Föster theory of non-radiation energy transfer. All these experimental results suggest that [Cr(phen) 2(dppz)] 3+ and [Cr(phen) 3] 3+ bind strongly to apoTf indicating that this protein could act as a carrier of these complexes for further applications in PDT. © 2011 Elsevier Inc. All rights reserved.
Fil: Toneatto, Judith. 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: 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: Arguello, Gerardo. 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 The present study reports a detailed investigation into the interaction of [Cr(phen) 2(dppz)] 3+ and [Cr(phen) 3] 3+ with transferrin, the key protein for the transport of Fe 3+ in blood plasma; its cycle holds promise as an attractive system for strategies of drug targeting to tumor tissues. This can allow us to understand further the role of both complexes as sensitizers in photodynamic therapy (PDT). Chromium(III) complexes, [Cr(phen) 2(dppz)] 3+ and [Cr(phen) 3] 3+, (phen = 1,10-phenanthroline and dppz = dipyridophenazine), where dppz is a planar bidentate ligand with an extended π system, have been found to bind strongly with apotransferrin (apoTf) with an intrinsic binding constant, K b, of (1.8 ± 0.3) × 10 5 M - 1 and (1.1 ± 0.1) × 10 5 M - 1 at 299 K, for apoTf-[Cr(phen) 2(dppz)] 3+ and apoTf-[Cr(phen) 3] 3+, respectively. The interactions of apoTf with the different Cr(III) complexes were assessed employing UV-visible absorption, fluorescence and circular dichroism spectroscopy. The relative fluorescence intensity of the protein decreased when the increasing concentration of Cr(III) complex was added, suggesting that perturbation around the Trp and Tyr residues took place. The analysis of the thermodynamic parameters ΔG, ΔH, ΔS indicated that the presence of the Cr(III) complex stabilizes the protein with a strong entropic contribution. The binding distances and transfer efficiencies for apoTf-[Cr(phen) 2(dppz)] 3+ and apoTf-[Cr(phen) 3] 3+ binding reactions were calculated according to Föster theory of non-radiation energy transfer. All these experimental results suggest that [Cr(phen) 2(dppz)] 3+ and [Cr(phen) 3] 3+ bind strongly to apoTf indicating that this protein could act as a carrier of these complexes for further applications in PDT. © 2011 Elsevier Inc. All rights reserved.
publishDate 2011
dc.date.none.fl_str_mv 2011-10
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/11336/61577
Toneatto, Judith; Garcia, Pablo Facundo; Arguello, Gerardo; Advances on the interaction of polypyridyl Cr(III) complexes with transporting proteins and its potential relevance in photodynamic therapy; Elsevier Science Inc; Journal of Inorganic Biochemistry; 105; 10; 10-2011; 1299-1305
0162-0134
CONICET Digital
CONICET
url http://hdl.handle.net/11336/61577
identifier_str_mv Toneatto, Judith; Garcia, Pablo Facundo; Arguello, Gerardo; Advances on the interaction of polypyridyl Cr(III) complexes with transporting proteins and its potential relevance in photodynamic therapy; Elsevier Science Inc; Journal of Inorganic Biochemistry; 105; 10; 10-2011; 1299-1305
0162-0134
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.jinorgbio.2011.07.013
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0162013411001930
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
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science Inc
publisher.none.fl_str_mv Elsevier Science Inc
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
_version_ 1851851892564426752
score 13.176297

Publicaciones similares