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1 January 2006 Diastereoselectivity and Site Dependency in the Photochemistry of Ketoprofen in the Bovine Serum Albumin Matrix
Sandra Monti, Ilse Manet, Francesco Manoli, Raffaele Morrone, Giovanni Nicolosi, Salvatore Sortino
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Abstract

The photodegradation of the S( )- and R(−)-ketoprofen (KP) enantiomers in the bovine serum albumin matrix was studied by steady-state photolysis with the use of λirr > 320 nm and transient absorption spectroscopy with λexc = 355 nm, at 1/1 and 2/1 KP/BSA molar ratios. R(−)-KP was found to be more labile than S( ). Triplet ketoprofen species were evidenced with lifetimes of 400 ns for S( ) and 600 ns for R(−)-KP. Further longer-lived transients with lifetimes of 2.6 and 6.0 μs for S( ) and R(−), respectively, were detected. On the basis of the binding constants of the drug enantiomers to the two main binding sites of the protein, obtained from circular dichroism experiments, the individual disappearance quantum yields of the 1:1 and 2:1 diastereomeric KP:BSA complexes could be estimated. The photoreactivity in the BSA matrix was rationalized on the basis of diastereoselective photodecarboxylation in the two main protein sites.

Sandra Monti, Ilse Manet, Francesco Manoli, Raffaele Morrone, Giovanni Nicolosi, and Salvatore Sortino "Diastereoselectivity and Site Dependency in the Photochemistry of Ketoprofen in the Bovine Serum Albumin Matrix," Photochemistry and Photobiology 82(1), 13-19, (1 January 2006). https://doi.org/10.1562/2005-07-11-RA-608
Received: 11 July 2005; Accepted: 22 September 2005; Published: 1 January 2006
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