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 lambda(irr) > 320 nm and transient absorption spectroscopy with lambda(exc) = 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 mus 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.
journal_name
Photochem Photobioljournal_title
Photochemistry and photobiologyauthors
Monti S,Manet I,Manoli F,Morrone R,Nicolosi G,Sortino Sdoi
10.1562/2005-07-11-RA-608subject
Has Abstractpub_date
2006-01-01 00:00:00pages
13-9issue
1eissn
0031-8655issn
1751-1097pii
2005-07-11-RA-608journal_volume
82pub_type
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