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Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale
Published on: March 14, 2019
Ultrafast Fluorescence Dynamics in Flurbiprofen-Amino Acid Dyads and in the Supramolecular Drug/Protein Complex
Ignacio Vayá1, M Consuelo Jiménez2, Miguel A Miranda2
1Departamento 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;,
Abstract:
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.
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