A quantitative circular dichroic investigation of the binding of the enantiomers of ibuprofen and naproxen to human serum albumin
| Autor: | Christopher M. Riley, V.K Cheruvallath, John H. Perrin, Siegfried Lindenbaum, S.R Narayanan |
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| Rok vydání: | 1997 |
| Předmět: |
Naproxen
Circular dichroism Stereochemistry Clinical Biochemistry Serum albumin Pharmaceutical Science Ibuprofen Analytical Chemistry Drug Discovery medicine Humans Serum Albumin Spectroscopy Chromatography biology Chemistry Anti-Inflammatory Agents Non-Steroidal Albumin Stereoisomerism Human serum albumin biology.protein Enantiomer Cotton effect Protein Binding medicine.drug |
| Zdroj: | Journal of Pharmaceutical and Biomedical Analysis. 15:1719-1724 |
| ISSN: | 0731-7085 |
| DOI: | 10.1016/s0731-7085(96)01956-5 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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