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 followi...

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Bibliographic Details
Published in:Journal of pharmaceutical and biomedical analysis 1997-07, Vol.15 (11), p.1719-1724
Main Authors: Cheruvallath, V.K, Riley, C.M, Narayanan, S.R, Lindenbaum, S, Perrin, J.H
Format: Article
Language:English
Subjects:
Analysis
Anti-Inflammatory Agents, Non-Steroidal - metabolism
Biological and medical sciences
Diazepam
Enantiomers
Extrinsic cotton effects
Finding constants
General pharmacology
Humans
Ibuprofen
Ibuprofen - metabolism
Medical sciences
Naproxen
Naproxen - metabolism
Pharmacology. Drug treatments
Protein Binding
Racemate
Serum Albumin - metabolism
Stereoisomerism
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Summary: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 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.
ISSN:0731-7085
1873-264X
DOI:10.1016/S0731-7085(96)01956-5