General Treatment of Competitive Binding as Applied to the Potentiometric Ion Probe Technique: Application to the Interaction of Nonsteroidal Anti- Inflammatory Drugs with Bovine Serum Albumin
| Autor: | Evangelos E. Sideris, Alexandra Th. Angelakou, Georgia Valsami, Michael A. Koupparis, Panos Macheras |
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| Rok vydání: | 1994 |
| Předmět: |
Ketoprofen
Naproxen Potentiometric titration Analytical chemistry Serum albumin Pharmaceutical Science Ligands Binding Competitive Anilino Naphthalenesulfonates Ion selective electrode Electroanalytical method medicine Computer Simulation Bovine serum albumin Azapropazone Binding Sites biology Chemistry Anti-Inflammatory Agents Non-Steroidal Serum Albumin Bovine Potentiometry biology.protein Regression Analysis Indicators and Reagents Protein Binding medicine.drug Nuclear chemistry |
| Zdroj: | Journal of Pharmaceutical Sciences. 83:1150-1154 |
| ISSN: | 0022-3549 |
| DOI: | 10.1002/jps.2600830816 |
| Popis: | The binding of naproxen, ketoprofen, phenylbutazone, salicyclic acid, azapropazone, and indobufen to bovine serum albumin was studied by applying the potentiometric ion probe technique. An ion-selective electrode for the ion probe 1-anilino-8-naphthalene-sulfonate was utilized for the purposes of this study. A modified site-oriented competitive binding model was used for the estimation of the drugs' binding parameters, considering different number of binding sites on the competing binding class(es) for the probe and the drug. Calculations were based exclusively on the concentration data of the free probe. The model's ability for accurate estimations of binding parameters was evaluated by simulation studies. The following values of binding parameters were found at 25 °C for the drugs under study; naproxen, n 1 = 9.1, k 1 = 9.4 × 10 5 M − 1 ; ketoprofen, n 1 = 8.8, k 1 = 10.8 × 10 5 M − 1 ; phenylbutazone, n 1 = 3.2, k 1 = 1.4 × 10 5 M − 1 ; salicylic acid, n 1 = 2.6, k 1 = 1.8 × 10 5 M − 1 , n 2 = 21.5, k 2 = 1.0 × 10 4 M − 1 ; azapropazone, n 1 = 0.5, k 1 = 7.8 × 10 5 , M − 1 , n 2 = 26.3, k 2 = 1.9 × 10 4 M − 1 ; indobufen, n 1 = 5.8, k 1 = 5.8 × 10 5 M − 1 , n 2 = 19.9, k 2 = 3.8 × 10 5 M − 1 , where n i the number of binding sites of the i class and k i , the corresponding association constant. |
| Databáze: | OpenAIRE |
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