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Drug/protein interactions studied by time-resolved fluorescence spectroscopy

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Drug/protein interactions studied by time-resolved fluorescence spectroscopy

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Nombre: THOMAS GUSTAVSSON ...
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dc.contributor.author Gustavsson, Thomas es_ES
dc.contributor.author Markovitsi, Dimitra es_ES
dc.contributor.author Vayá Pérez, Ignacio es_ES
dc.contributor.author Bonancía Roca, Paula es_ES
dc.contributor.author Jiménez Molero, María Consuelo es_ES
dc.contributor.author Miranda Alonso, Miguel Ángel es_ES
dc.date.accessioned 2017-09-26T11:50:09Z
dc.date.available 2017-09-26T11:50:09Z
dc.date.issued 2014
dc.identifier.issn 0277-786X
dc.identifier.uri http://hdl.handle.net/10251/87962
dc.description.abstract [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. es_ES
dc.language Inglés es_ES
dc.publisher Society of Photo-optical Instrumentation Engineers (SPIE) es_ES
dc.relation.ispartof Proceedings of SPIE es_ES
dc.rights Reserva de todos los derechos es_ES
dc.subject Drugs es_ES
dc.subject Flurbiprofen es_ES
dc.subject Albumin es_ES
dc.subject Time-resolved fluorescence es_ES
dc.subject Femtosecond es_ES
dc.subject Fluorescence upconversion es_ES
dc.subject.classification QUIMICA ORGANICA es_ES
dc.subject.classification QUIMICA ANALITICA es_ES
dc.title Drug/protein interactions studied by time-resolved fluorescence spectroscopy es_ES
dc.type Artículo es_ES
dc.identifier.doi 10.1117/12.2063917
dc.rights.accessRights Abierto es_ES
dc.contributor.affiliation Universitat Politècnica de València. Escuela Técnica Superior de Ingenieros Industriales - Escola Tècnica Superior d'Enginyers Industrials es_ES
dc.contributor.affiliation Universitat Politècnica de València. Departamento de Química - Departament de Química es_ES
dc.description.bibliographicCitation Gustavsson, T.; Markovitsi, D.; Vayá Pérez, I.; Bonancía Roca, P.; Jiménez Molero, MC.; Miranda Alonso, MÁ. (2014). Drug/protein interactions studied by time-resolved fluorescence spectroscopy. Proceedings of SPIE. 9165:1-4. doi:10.1117/12.2063917 es_ES
dc.description.accrualMethod S es_ES
dc.relation.publisherversion http://dx.doi. org/10.1117/12.2063917 es_ES
dc.description.upvformatpinicio 1 es_ES
dc.description.upvformatpfin 4 es_ES
dc.type.version info:eu-repo/semantics/publishedVersion es_ES
dc.description.volume 9165 es_ES
dc.relation.senia 288766 es_ES
dc.identifier.eissn 1996-756X
dc.description.references Vayá, I., Bonancía, P., Jiménez, M. C., Markovitsi, D., Gustavsson, T., & Miranda, M. A. (2013). Excited state interactions between flurbiprofen and tryptophan in drug–protein complexes and in model dyads. Fluorescence studies from the femtosecond to the nanosecond time domains. Physical Chemistry Chemical Physics, 15(13), 4727. doi:10.1039/c3cp43847c es_ES
dc.description.references Cohen, B., Martin Álvarez, C., Alarcos Carmona, N., Organero, J. A., & Douhal, A. (2011). Proton-Transfer Reaction Dynamics within the Human Serum Albumin Protein. The Journal of Physical Chemistry B, 115(23), 7637-7647. doi:10.1021/jp200294q es_ES
dc.description.references Vayá, I., Jiménez, M. C., & Miranda, M. A. (2007). Excited-State Interactions in Flurbiprofen−Tryptophan Dyads. The Journal of Physical Chemistry B, 111(31), 9363-9371. doi:10.1021/jp071301z es_ES
dc.description.references Abad, S., Pischel, U., & Miranda, M. A. (2005). Wavelength-Dependent Stereodifferentiation in the Fluorescence Quenching of Asymmetric Naphthalene-Based Dyads by Amines. The Journal of Physical Chemistry A, 109(12), 2711-2717. doi:10.1021/jp047996a es_ES
dc.description.references ChemPhysChem. (s. f.). doi:10.1002/(issn)1439-7641 es_ES
dc.description.references Schröder, G. F., Alexiev, U., & Grubmüller, H. (2005). Simulation of Fluorescence Anisotropy Experiments: Probing Protein Dynamics. Biophysical Journal, 89(6), 3757-3770. doi:10.1529/biophysj.105.069500 es_ES


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