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.

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

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