BINDING EFFICACY AND ELUCIDATION OF QUANTITATIVE STRUCTURE ACTIVITY RELATIONSHIP OF ACETANILIDE AND ITS DERIVATIVES WITH BOVINE SERUM ALBUMIN AND THEIR INHIBITION AGAINST COX1

Serum albumins are the most abundant proteins in plasma with many physiological functions. Among them, BSA has a wide range of functions involving the binding, transport and delivery of fatty acids, porphyrins, bilirubin, steroids, etc and it is home to specific binding sites for metals, pharmaceuticals and dyes. Recently, nanotechnology has become a popular term in the current science and technology. Nanotechnology has been introduced for the food and drug industry, including encapsulations and delivery systems. BSA nanoparticles were prepared and their binding efficacy with the available analgesics such as acetanilide and its derivatives were studied. The value of apparent rate constant K_app from the interaction between acetanilide and BSA by UV visible spectroscopic and fluorescence technique was found to be 2.294X10⁶. The quenching rate constant of BSA-Acetanilide was found to be 1.0345X10¹⁵M^-1 S^-1. There are two binding sites in BSA for acetanilide. A QSAR study was performed for the different analgesics. Inhibition of Acetanilide and its derivatives with the Cyclooxygenase (COX 1) was studied using docking mechanism. The electro chemical behavior of acetanilide is studied and it is found to be reversible.