Open AccessUltrafast Fluorescence Dynamics in Flurbiprofen–Amino Acid Dyads and in the Supramolecular Drug/Protein Complex
Author(s) -
Ignacio Vayá,
Jiménez Mc,
Miguel A. Miranda,
Amit Chatterjee,
T. Gustavsson
Publication year - 2017
Publication title -
chimia
Language(s) - English
Resource type - Journals
eISSN - 2673-2424
pISSN - 0009-4293
DOI - 10.2533/chimia.2017.18
Subject(s) - flurbiprofen , fluorescence , chemistry , human serum albumin , picosecond , tryptophan , chromophore , biophysics , quenching (fluorescence) , photochemistry , amino acid , biochemistry , biology , laser , physics , optics , pharmacology , quantum mechanics
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.