BINDING OF PIPRINHYDRINATE TO PLASMA PROTEINS AND THEIR SUBSTITUTES

Mohamed, M. S.; Gazy, F. S.; Abu-Zaid, S. S.; Müller, B. W.; Abd ElRahman, M. M.

doi:10.21608/bfsa.1994.69793

BINDING OF PIPRINHYDRINATE TO PLASMA PROTEINS AND THEIR SUBSTITUTES

Document Type : Original Article

Authors

¹ Department of Pharmaceutics, Faculty of Pharmacy, Zagazig University, Zagazig, Egypt

² Department of Pharmaceutics, Institute of Pharmacy, Kiel, Germany

10.21608/bfsa.1994.69793

Abstract

The binding of piprinhydrinate to bovine serum albumin (BSA) was studied in isotonic Sorensen's phosphate buffer pH 7.4 at 25±1°C, using equilibrium dialysis technique. Piprinhydrinate was bound to BSA and the plot was curved indicating the presence of morethan one binding site on the albumin molecule. At fixed protein concentration the percentage of bound drug to bovine serum albumin was inversely proportional to the concentration of the drug. But the binding parameters (binding constants as well as the number of binding sites) were found to be unaffected as the albumin concentration increased. However, binding parameters showed no significant difference due to pH change. Phosphate buffer, Gomori's tris-HCl buffer and Walpole's acetate buffer have different effect on the binding of piprinhydrinate to BSA; the values of the binding parameters can be arranged as follows: Sorensen's phosphate buffer > Gomori's tris-HCl > Walpole's acetate buffer. Also, it was found that chloride ions decrease the amount of the drug bound to BSA. The interaction of the drug with dextrans (40000, 266000 and 500000) in isotonic Sorensen's buffer pH 7.4 was investigated. No interaction was observed between the drug and the tested dextrans under the condition of the experiment. Also laevosan and hetastarch showed no significant interaction.