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Proceedings Paper

Drug/protein interactions studied by time-resolved fluorescence spectroscopy
Author(s): Thomas Gustavsson; Dimitra Markovitsi; Ignacio Vayá; Paula Bonancía; M. Consuelo Jiménez; Miguel A. Miranda
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Paper 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.

Paper Details

Date Published: 9 September 2014
PDF: 4 pages
Proc. SPIE 9165, Physical Chemistry of Interfaces and Nanomaterials XIII, 91651E (9 September 2014); doi: 10.1117/12.2063917
Show Author Affiliations
Thomas Gustavsson, Lab. Francis Perrin, CNRS, IRAMIS (France)
Dimitra Markovitsi, Lab. Francis Perrin, CNRS, IRAMIS (France)
Ignacio Vayá, Univ. Politècnica de València (Spain)
Paula Bonancía, Univ. Politècnica de València (Spain)
M. Consuelo Jiménez, Univ. Politècnica de València (Spain)
Miguel A. Miranda, Univ. Politècnica de València (Spain)


Published in SPIE Proceedings Vol. 9165:
Physical Chemistry of Interfaces and Nanomaterials XIII
Natalie Banerji; Sophia C. Hayes; Carlos Silva, Editor(s)

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