ABSTRACT
This study is to investigate the interaction of diltiazem hydrochloride with bovine serum albumin [BSA] in isotonic Sorensen's phosphate buffer of pH 7.4 at room temperature. The equilibrium dialysis technique was used to assess factors influencing diltiazem hydrochloride binding to BSA. Scatchard plot demonstrated marked curvature which indicates the existence of more than one binding site on the BSA molecules. At a fixed protein concentration, the percentage of drug bound was found to be inversely proportional to drug concentration. Whilst, at a given drug concentration, the percentage of drug bound was increased with increasing BSA concentration. Moreover, increasing the temperature and the presence of Fe[+3] and Mg[+2] ions resulted in an increase of binding constants for both classes of sites. On the other hand, decreasing pH values resulted in a decrease in the percentage of drug bound