Paper
9 September 2014 Drug/protein interactions studied by time-resolved fluorescence spectroscopy
Thomas Gustavsson, Dimitra Markovitsi, Ignacio Vayá, Paula Bonancía, M. Consuelo Jiménez, Miguel A. Miranda
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Abstract
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 flurbiprofentryptophan 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.
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Thomas Gustavsson, Dimitra Markovitsi, Ignacio Vayá, Paula Bonancía, M. Consuelo Jiménez, and Miguel A. Miranda "Drug/protein interactions studied by time-resolved fluorescence spectroscopy", Proc. SPIE 9165, Physical Chemistry of Interfaces and Nanomaterials XIII, 91651E (9 September 2014); https://doi.org/10.1117/12.2063917
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KEYWORDS
Luminescence

Time resolved spectroscopy

Proteins

Fluorescence anisotropy

Picosecond phenomena

Femtosecond phenomena

Energy transfer

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