Drug/protein interactions studied by time-resolved fluorescence spectroscopy

[EN] We report here on a recent time-resolved fluorescence study [1] of the interaction between flurbiprofen (FBP), a chiral non-steroidal anti-inflammatory drug, and human serum albumin (HSA), the main transport protein in the human body. We compare the results obtained for the drug-protein complex...

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Autores: Gustavsson, Thomas, Markovitsi, Dimitra, Bonancía Roca, Paula, Miranda Alonso, Miguel Ángel, Vayá Pérez, Ignacio|||0000-0003-1682-9342, Jiménez, M Consuelo|||0000-0002-8057-4316
Tipo de recurso: artículo
Fecha de publicación:2014
País:España
Institución:Universitat Politècnica de València (UPV)
Repositorio:RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia
Idioma:inglés
OAI Identifier:oai:riunet.upv.es:10251/87962
Acceso en línea:https://riunet.upv.es/handle/10251/87962
Access Level:acceso abierto
Palabra clave:Drugs
Flurbiprofen
Albumin
Time-resolved fluorescence
Femtosecond
Fluorescence upconversion
QUIMICA ORGANICA
QUIMICA ANALITICA
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oai_identifier_str oai:riunet.upv.es:10251/87962
network_acronym_str ES
network_name_str España
repository_id_str
spelling Drug/protein interactions studied by time-resolved fluorescence spectroscopyGustavsson, ThomasMarkovitsi, DimitraBonancía Roca, PaulaMiranda Alonso, Miguel ÁngelVayá Pérez, Ignacio|||0000-0003-1682-9342Jiménez, M Consuelo|||0000-0002-8057-4316DrugsFlurbiprofenAlbuminTime-resolved fluorescenceFemtosecondFluorescence upconversionQUIMICA ORGANICAQUIMICA ANALITICA[EN] We report here on a recent time-resolved fluorescence study [1] of the interaction between flurbiprofen (FBP), a chiral non-steroidal anti-inflammatory drug, and human serum albumin (HSA), the main transport protein in the human body. We compare the results obtained for the drug-protein complex with those of various covalently linked flurbiprofen-tryptophan dyads having well-defined geometries. In all cases stereoselective dynamic fluorescence quenching is observed, varying greatly from one system to another. In addition, the fluorescence anisotropy decays also display a clear stereoselectivity. For the drug-protein complexes, this can be interpreted in terms of the protein microenvironment playing a significant role in the conformational relaxation of FBP, which is more restricted in the case of the (R)-enantiomer.Society of Photo-optical Instrumentation Engineers (SPIE)Instituto Universitario Mixto de Tecnología QuímicaDepartamento de QuímicaEscuela Técnica Superior de Ingeniería IndustrialGrupo de estudio de estados excitados: detección, dinámica, transformaciones y campos de aplicaciónRepositorio Institucional de la Universitat Politècnica de València Riunet20142014-01-01journal articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfapplication/pdfhttps://riunet.upv.es/handle/10251/87962reponame:RiuNet. Repositorio Institucional de la Universitat Politécnica de Valénciainstname:Universitat Politècnica de València (UPV)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2Reserva de todos los derechoshttp://rightsstatements.org/vocab/InC/1.0/info:eu-repo/semantics/openAccessoai:riunet.upv.es:10251/879622026-06-13T07:49:27Z
dc.title.none.fl_str_mv Drug/protein interactions studied by time-resolved fluorescence spectroscopy
title Drug/protein interactions studied by time-resolved fluorescence spectroscopy
spellingShingle Drug/protein interactions studied by time-resolved fluorescence spectroscopy
Gustavsson, Thomas
Drugs
Flurbiprofen
Albumin
Time-resolved fluorescence
Femtosecond
Fluorescence upconversion
QUIMICA ORGANICA
QUIMICA ANALITICA
title_short Drug/protein interactions studied by time-resolved fluorescence spectroscopy
title_full Drug/protein interactions studied by time-resolved fluorescence spectroscopy
title_fullStr Drug/protein interactions studied by time-resolved fluorescence spectroscopy
title_full_unstemmed Drug/protein interactions studied by time-resolved fluorescence spectroscopy
title_sort Drug/protein interactions studied by time-resolved fluorescence spectroscopy
dc.creator.none.fl_str_mv Gustavsson, Thomas
Markovitsi, Dimitra
Bonancía Roca, Paula
Miranda Alonso, Miguel Ángel
Vayá Pérez, Ignacio|||0000-0003-1682-9342
Jiménez, M Consuelo|||0000-0002-8057-4316
author Gustavsson, Thomas
author_facet Gustavsson, Thomas
Markovitsi, Dimitra
Bonancía Roca, Paula
Miranda Alonso, Miguel Ángel
Vayá Pérez, Ignacio|||0000-0003-1682-9342
Jiménez, M Consuelo|||0000-0002-8057-4316
author_role author
author2 Markovitsi, Dimitra
Bonancía Roca, Paula
Miranda Alonso, Miguel Ángel
Vayá Pérez, Ignacio|||0000-0003-1682-9342
Jiménez, M Consuelo|||0000-0002-8057-4316
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Instituto Universitario Mixto de Tecnología Química
Departamento de Química
Escuela Técnica Superior de Ingeniería Industrial
Grupo de estudio de estados excitados: detección, dinámica, transformaciones y campos de aplicación
Repositorio Institucional de la Universitat Politècnica de València Riunet
dc.subject.none.fl_str_mv Drugs
Flurbiprofen
Albumin
Time-resolved fluorescence
Femtosecond
Fluorescence upconversion
QUIMICA ORGANICA
QUIMICA ANALITICA
topic Drugs
Flurbiprofen
Albumin
Time-resolved fluorescence
Femtosecond
Fluorescence upconversion
QUIMICA ORGANICA
QUIMICA ANALITICA
description [EN] We report here on a recent time-resolved fluorescence study [1] of the interaction between flurbiprofen (FBP), a chiral non-steroidal anti-inflammatory drug, and human serum albumin (HSA), the main transport protein in the human body. We compare the results obtained for the drug-protein complex with those of various covalently linked flurbiprofen-tryptophan dyads having well-defined geometries. In all cases stereoselective dynamic fluorescence quenching is observed, varying greatly from one system to another. In addition, the fluorescence anisotropy decays also display a clear stereoselectivity. For the drug-protein complexes, this can be interpreted in terms of the protein microenvironment playing a significant role in the conformational relaxation of FBP, which is more restricted in the case of the (R)-enantiomer.
publishDate 2014
dc.date.none.fl_str_mv 2014
2014-01-01
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://riunet.upv.es/handle/10251/87962
url https://riunet.upv.es/handle/10251/87962
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Reserva de todos los derechos
http://rightsstatements.org/vocab/InC/1.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Reserva de todos los derechos
http://rightsstatements.org/vocab/InC/1.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Society of Photo-optical Instrumentation Engineers (SPIE)
publisher.none.fl_str_mv Society of Photo-optical Instrumentation Engineers (SPIE)
dc.source.none.fl_str_mv reponame:RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia
instname:Universitat Politècnica de València (UPV)
instname_str Universitat Politècnica de València (UPV)
reponame_str RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia
collection RiuNet. Repositorio Institucional de la Universitat Politécnica de Valéncia
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,300719

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