Spectrophotometric study of Interactions 2-{[2-(cyclohexycarbamoyl) benzoyl] amino} propanoic acid (2CMPA) with BSA: Gel exclusion chromatography and molecular modeling study.

Abstract: The interaction of between 2-{[2-(cyclohexycarbamoyl) benzoyl] amino} propanoic acid (2CMPA) 2CMPA and protein BSA was studied using the gel exclusion chromatographic technique. Spectrophotometric data reveals that 2CMPA successfully binds with BSA. The effect of pH on binding affinity was also studied. The Scatchard analysis gives association constants (Kf) values that are found to be 0.6056, 0.5809, and 0.5714 at acetate buffer pH 3, 4, and 5 respectively. It was found that 2CMPA bounds to the BSA more significantly at pH 3 than at pH 4 and 5 which shows that binding is more significant at acidic and decreases with an increase in pH. A molecular modeling study was also done which gives the efficient energy value for complex -235.41 that confirms the binding of titled 2CMPA with BSA.