Binding of Sulfonylureas to Bovine Serum Albumin

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Abstract
The binding of 7 commercial sulfonylureas (tolbutamide, chlorpropamide, acetohexamide, carbutamide, chlorpentazide, azepinamide and tolazamide) by bovine serum albumin (BSA) was investigated using an equilibrium dialysis procedure. The Scatchard plots of the data of 6 sulfonylureas except tolazamide indicated the presence of 2 kinds of binding sites. Assuming both concentrations of BSA and sulfonylureas are 5 .times. 10-4 M, the results of calculation demonstrated that tolbutamide has large binding percentages (97.2%) and tolazamide is relatively small (88.8%). Although the effect of pH and ionic strength of solvent was investigated, the exact mechanism of binding could not be elucidated. A good correlation was observed between the logarithms of BSA binding constants and octanol-water partition coefficients for sulfonylureas. It seemed that their molecular structure that leads to a higher lipophilicity will result in an enhanced BSA binding.

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