Ultrafast Fluorescence Dynamics in Flurbiprofen–Amino Acid Dyads and in the Supramolecular Drug/Protein Complex
Ignacio Vayá,
M. Consuelo Jiménez,
Miguel A. Miranda,
Aninda Chatterjee,
Thomas Gustavsson
Affiliations
Ignacio Vayá
Departamento de Química/Instituto de Tecnología, Química UPV-CSIC, Universitat Politècnica de València Camino de Vera s/n, 46022 Valencia, Spain, School of Chemistry, University of East Anglia, Norwich
Research Park NR4 7TJ, Norwich, United Kingdom;, Email: [email protected]
M. Consuelo Jiménez
Departamento de Química/Instituto de Tecnología, Química UPV-CSIC, Universitat Politècnica de València Camino de Vera s/n, 46022 Valencia, Spain
Miguel A. Miranda
Departamento de Química/Instituto de Tecnología, Química UPV-CSIC, Universitat Politècnica de València Camino de Vera s/n, 46022 Valencia, Spain
Aninda Chatterjee
LIDYL, Laboratoire Interactions, Dynamiques et Lasers CEA, CNRS, Université Paris-Saclay, CEA Saclay 91191 Gif-sur-Yvette, France
Thomas Gustavsson
LIDYL, Laboratoire Interactions, Dynamiques et Lasers CEA, CNRS, Université Paris-Saclay, CEA Saclay 91191 Gif-sur-Yvette, France;, Email: [email protected]
The interaction dynamics between the drug flurbiprofen (FBP) and human serum albumin (HSA) has been investigated by time-resolved fluorescence spectroscopy, combining femtosecond fluorescence upconversion and picosecond time-correlated single photon counting. In order to obtain additional information on the drug/ protein interaction, several covalently linked model dyads, composed of FBP and tryptophan or tyrosine, were also studied. For all systems, the main feature was a remarkable dynamic FBP fluorescence quenching, more prominent in the dyads than in the protein complex. All systems also displayed a clear stereoselectivity depending on the (S)- or (R)-form of FBP, that was strongly influenced by the conformational arrangement of the investigated chromophores.
