A quantitative circular dichroic investigation of the binding of the enantiomers of ibuprofen and naproxen to human serum albumin.
The binding constants for racemic, R and S naproxen and ibuprofen to human serum albumin have been determined by a circular dichroic technique. The ibuprofens and naproxens show no measurable extrinsic optical activity on interaction with the protein, and so the extrinsic Cotton effect shown following the diazepam-albumin interaction is used as a probe. The presence of the drugs reduce the amount of diazepam bound as shown by the interaction is used as a probe. The presence of the drugs reduce the amount of diazepam bound as shown by the reduced size of the induced ellipticity. The calculated primary binding constants show that the S form of both drugs bind to the albumin more tightly than the R form and that the racemic forms bind less tightly than either enantiomer.
Cheruvallath
V K
VK
Dura Pharmaceuticals, San Diego, CA 92121, USA.
Riley
C M
CM
Narayanan
S R
SR
Lindenbaum
S
S
Perrin
J H
JH
D000894:Anti-Inflammatory Agents, Non-Steroidal / Q000378:metabolism*; D006801:Humans; D007052:Ibuprofen / Q000378:metabolism*; D009288:Naproxen / Q000378:metabolism*; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D013237:Stereoisomerism
D000894:Anti-Inflammatory Agents, Non-Steroidal; D012709:Serum Albumin; D009288:Naproxen; D007052:Ibuprofen