Plasma protein in blood play an important role in transportation of drug. So it is important to know the binding of drug with plasma protein. In this study we successfully observed the interaction of 2-benzamido-4-methylpentanoic acid-2-cyclohexyl carboxamide ligand (2-bmca) with Bovine serum albumin (BSA) using gel exclusion chromatographic technique at different pH. Absorbance value for collected fraction was measured on UV-vis Spectrophotometer. Differences in the absorbance value of collected fraction give the specific binding of interacting species with BSA. Interacting study shows that ligand (L) bounds to the BSA more significantly at pH 3 than at pH 4 and 5, which shows binding is more at acidic pH. Scatchard analysis gives the association constants (Kf) and the saturation value (n) for ligand(L) with BSA. Molecular modeling study gives the efficient energy value–231.16 which confirms the binding of ligand (L) with BSA.
gel exclusion chromatography protein-drug binding Scatchard analysis association constant BSA molecular modeling study
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