Effect of dye localization and self-interactions on the photosensitized generation of singlet oxygen by rose bengal bound to bovine serum albumin

Autores
Espeche Turbay, Maria Beatriz; Rey, Valentina; Argañaraz, Natalia Mariel; Moran Vieyra, Faustino Eduardo; Aspée, Alexis; Lissi, Eduardo A.; Borsarelli, Claudio Darío
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The spectroscopic and photophysical properties of rose bengal (RB) encased in bovine serum albumin (BSA) have been examined to evaluate the photosensitized generation of singlet molecular oxygen (1O2). The results show that RB photophysical and photosensitizing properties are highly modulated by the average number of dye molecules per protein (n). At n 蠐1, the dye molecule is tightly located into the hydrophobic nanocavity site I of the BSA molecule with a binding constant Kb = 0.15 ± 0.01 μM-1. The interaction with surrounding amino acids induces heterogeneous decay of both singlet and triplet excited states of RB and partially reduce its triplet quantum yield as compared with that in buffer solution. However, despite of the diffusive barrier imposed by the protein nanocavity to 3O2, the quenching of 3RBBSA generates 1O2 with quantum yield ΦΔ = 0.35 ± 0.05. In turns, the intraprotein generated 1O2 is able to diffuse through the bulk solution, where is dynamically quenched by BSA itself with an overall quenching rate constant of 7.3 × 108 M-1 s-1. However, at n > 1, nonspecific binding of up to ≈6 RB molecules per BSA is produced, allowing efficient static quenching of excited states of RB preventing photosensitization of 1O2. These results provide useful information for development of dye-protein adducts suitable for using as potential intracellular photosensitizers.
Fil: Espeche Turbay, Maria Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
Fil: Rey, Valentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
Fil: Argañaraz, Natalia Mariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
Fil: Moran Vieyra, Faustino Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
Fil: Aspée, Alexis. Universidad de Santiago de Chile; Chile
Fil: Lissi, Eduardo A.. Universidad de Santiago de Chile; Chile
Fil: Borsarelli, Claudio Darío. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
Materia
Rose Bengal
Bovine Serum Albumin
Photosensitization
Singlet Oxygen
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:11336/36508
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/36508
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Effect of dye localization and self-interactions on the photosensitized generation of singlet oxygen by rose bengal bound to bovine serum albuminEspeche Turbay, Maria BeatrizRey, ValentinaArgañaraz, Natalia MarielMoran Vieyra, Faustino EduardoAspée, AlexisLissi, Eduardo A.Borsarelli, Claudio DaríoRose BengalBovine Serum AlbuminPhotosensitizationSinglet Oxygenhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1The spectroscopic and photophysical properties of rose bengal (RB) encased in bovine serum albumin (BSA) have been examined to evaluate the photosensitized generation of singlet molecular oxygen (1O2). The results show that RB photophysical and photosensitizing properties are highly modulated by the average number of dye molecules per protein (n). At n 蠐1, the dye molecule is tightly located into the hydrophobic nanocavity site I of the BSA molecule with a binding constant Kb = 0.15 ± 0.01 μM-1. The interaction with surrounding amino acids induces heterogeneous decay of both singlet and triplet excited states of RB and partially reduce its triplet quantum yield as compared with that in buffer solution. However, despite of the diffusive barrier imposed by the protein nanocavity to 3O2, the quenching of 3RBBSA generates 1O2 with quantum yield ΦΔ = 0.35 ± 0.05. In turns, the intraprotein generated 1O2 is able to diffuse through the bulk solution, where is dynamically quenched by BSA itself with an overall quenching rate constant of 7.3 × 108 M-1 s-1. However, at n > 1, nonspecific binding of up to ≈6 RB molecules per BSA is produced, allowing efficient static quenching of excited states of RB preventing photosensitization of 1O2. These results provide useful information for development of dye-protein adducts suitable for using as potential intracellular photosensitizers.Fil: Espeche Turbay, Maria Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; ArgentinaFil: Rey, Valentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; ArgentinaFil: Argañaraz, Natalia Mariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; ArgentinaFil: Moran Vieyra, Faustino Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; ArgentinaFil: Aspée, Alexis. Universidad de Santiago de Chile; ChileFil: Lissi, Eduardo A.. Universidad de Santiago de Chile; ChileFil: Borsarelli, Claudio Darío. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; ArgentinaElsevier Science Sa2014-10info: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/11336/36508Espeche Turbay, Maria Beatriz; Rey, Valentina; Argañaraz, Natalia Mariel; Moran Vieyra, Faustino Eduardo; Aspée, Alexis; et al.; Effect of dye localization and self-interactions on the photosensitized generation of singlet oxygen by rose bengal bound to bovine serum albumin; Elsevier Science Sa; Journal of Photochemistry and Photobiology B: Biology; 141; 10-2014; 275-2821011-1344CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.jphotobiol.2014.09.014info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1011134414002929info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:52:51Zoai:ri.conicet.gov.ar:11336/36508instacron: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:34982025-09-03 09:52:52.28CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Effect of dye localization and self-interactions on the photosensitized generation of singlet oxygen by rose bengal bound to bovine serum albumin
title Effect of dye localization and self-interactions on the photosensitized generation of singlet oxygen by rose bengal bound to bovine serum albumin
spellingShingle Effect of dye localization and self-interactions on the photosensitized generation of singlet oxygen by rose bengal bound to bovine serum albumin
Espeche Turbay, Maria Beatriz
Rose Bengal
Bovine Serum Albumin
Photosensitization
Singlet Oxygen
title_short Effect of dye localization and self-interactions on the photosensitized generation of singlet oxygen by rose bengal bound to bovine serum albumin
title_full Effect of dye localization and self-interactions on the photosensitized generation of singlet oxygen by rose bengal bound to bovine serum albumin
title_fullStr Effect of dye localization and self-interactions on the photosensitized generation of singlet oxygen by rose bengal bound to bovine serum albumin
title_full_unstemmed Effect of dye localization and self-interactions on the photosensitized generation of singlet oxygen by rose bengal bound to bovine serum albumin
title_sort Effect of dye localization and self-interactions on the photosensitized generation of singlet oxygen by rose bengal bound to bovine serum albumin
dc.creator.none.fl_str_mv Espeche Turbay, Maria Beatriz
Rey, Valentina
Argañaraz, Natalia Mariel
Moran Vieyra, Faustino Eduardo
Aspée, Alexis
Lissi, Eduardo A.
Borsarelli, Claudio Darío
author Espeche Turbay, Maria Beatriz
author_facet Espeche Turbay, Maria Beatriz
Rey, Valentina
Argañaraz, Natalia Mariel
Moran Vieyra, Faustino Eduardo
Aspée, Alexis
Lissi, Eduardo A.
Borsarelli, Claudio Darío
author_role author
author2 Rey, Valentina
Argañaraz, Natalia Mariel
Moran Vieyra, Faustino Eduardo
Aspée, Alexis
Lissi, Eduardo A.
Borsarelli, Claudio Darío
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Rose Bengal
Bovine Serum Albumin
Photosensitization
Singlet Oxygen
topic Rose Bengal
Bovine Serum Albumin
Photosensitization
Singlet Oxygen
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 spectroscopic and photophysical properties of rose bengal (RB) encased in bovine serum albumin (BSA) have been examined to evaluate the photosensitized generation of singlet molecular oxygen (1O2). The results show that RB photophysical and photosensitizing properties are highly modulated by the average number of dye molecules per protein (n). At n 蠐1, the dye molecule is tightly located into the hydrophobic nanocavity site I of the BSA molecule with a binding constant Kb = 0.15 ± 0.01 μM-1. The interaction with surrounding amino acids induces heterogeneous decay of both singlet and triplet excited states of RB and partially reduce its triplet quantum yield as compared with that in buffer solution. However, despite of the diffusive barrier imposed by the protein nanocavity to 3O2, the quenching of 3RBBSA generates 1O2 with quantum yield ΦΔ = 0.35 ± 0.05. In turns, the intraprotein generated 1O2 is able to diffuse through the bulk solution, where is dynamically quenched by BSA itself with an overall quenching rate constant of 7.3 × 108 M-1 s-1. However, at n > 1, nonspecific binding of up to ≈6 RB molecules per BSA is produced, allowing efficient static quenching of excited states of RB preventing photosensitization of 1O2. These results provide useful information for development of dye-protein adducts suitable for using as potential intracellular photosensitizers.
Fil: Espeche Turbay, Maria Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
Fil: Rey, Valentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
Fil: Argañaraz, Natalia Mariel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
Fil: Moran Vieyra, Faustino Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
Fil: Aspée, Alexis. Universidad de Santiago de Chile; Chile
Fil: Lissi, Eduardo A.. Universidad de Santiago de Chile; Chile
Fil: Borsarelli, Claudio Darío. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina
description The spectroscopic and photophysical properties of rose bengal (RB) encased in bovine serum albumin (BSA) have been examined to evaluate the photosensitized generation of singlet molecular oxygen (1O2). The results show that RB photophysical and photosensitizing properties are highly modulated by the average number of dye molecules per protein (n). At n 蠐1, the dye molecule is tightly located into the hydrophobic nanocavity site I of the BSA molecule with a binding constant Kb = 0.15 ± 0.01 μM-1. The interaction with surrounding amino acids induces heterogeneous decay of both singlet and triplet excited states of RB and partially reduce its triplet quantum yield as compared with that in buffer solution. However, despite of the diffusive barrier imposed by the protein nanocavity to 3O2, the quenching of 3RBBSA generates 1O2 with quantum yield ΦΔ = 0.35 ± 0.05. In turns, the intraprotein generated 1O2 is able to diffuse through the bulk solution, where is dynamically quenched by BSA itself with an overall quenching rate constant of 7.3 × 108 M-1 s-1. However, at n > 1, nonspecific binding of up to ≈6 RB molecules per BSA is produced, allowing efficient static quenching of excited states of RB preventing photosensitization of 1O2. These results provide useful information for development of dye-protein adducts suitable for using as potential intracellular photosensitizers.
publishDate 2014
dc.date.none.fl_str_mv 2014-10
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/11336/36508
Espeche Turbay, Maria Beatriz; Rey, Valentina; Argañaraz, Natalia Mariel; Moran Vieyra, Faustino Eduardo; Aspée, Alexis; et al.; Effect of dye localization and self-interactions on the photosensitized generation of singlet oxygen by rose bengal bound to bovine serum albumin; Elsevier Science Sa; Journal of Photochemistry and Photobiology B: Biology; 141; 10-2014; 275-282
1011-1344
CONICET Digital
CONICET
url http://hdl.handle.net/11336/36508
identifier_str_mv Espeche Turbay, Maria Beatriz; Rey, Valentina; Argañaraz, Natalia Mariel; Moran Vieyra, Faustino Eduardo; Aspée, Alexis; et al.; Effect of dye localization and self-interactions on the photosensitized generation of singlet oxygen by rose bengal bound to bovine serum albumin; Elsevier Science Sa; Journal of Photochemistry and Photobiology B: Biology; 141; 10-2014; 275-282
1011-1344
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.jphotobiol.2014.09.014
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1011134414002929
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 Sa
publisher.none.fl_str_mv Elsevier Science Sa
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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score 13.13397

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