Human serum albumin-mediated stereodifferentiation in the triplet state behavior of (S)- and (R)-carprofen.
A remarkable stereodifferentiation has been observed in the interaction between the excited triplet state of carprofen (CP) and human serum albumin (HSA). Time-resolved measurements using laser flash photolysis reveal the presence of two components with different lifetimes in triplet decay. This is explained by complexation of CP to the two possible HSA binding sites. The shorter-lived components are ascribed to the CP/HSA complexes in site I, where stereodifferentiation is more important (tauR/tauS ca. 4). This is correlated with formation of a dehalogenated photoproduct upon steady-state photolysis.
Instituto de Tecnología Química UPV-CSIC, Universidad Politécnica de Valencia, Avenida de los Naranjos s/n, 46022 Valencia, Spain.
Virginie
V
Lhiaubet-Vallet
Zaideth
Z
Sarabia
Francisco
F
Boscá
Miguel A
MA
Miranda
D000894:Anti-Inflammatory Agents, Non-Steroidal / Q000737:chemistry*; D002227:Carbazoles / Q000737:chemistry*; D006801:Humans; D010777:Photochemistry; D012709:Serum Albumin / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013237:Stereoisomerism
D000894:Anti-Inflammatory Agents, Non-Steroidal; D002227:Carbazoles; D012709:Serum Albumin; C007005:carprofen