Computer aided design and molecular docking study of 1-n-substituted-3, 5-diphenyl-2-pyrazoline derivatives as cox–2 inhibitors.

Abstract

Cyclooxygenase (COX) catalyses the first committed step in the synthesis of prostanoids, a large family of arachidonic acid metabolites and major target of non-steroidal anti-inflammatory drugs (NSAIDs). COX-2 is the inducible isoform, rapidly expressed in several cell types in response to pro-inflammatory molecules. The interaction between the polypeptide and its corresponding receptor is highly selective. Therefore, it is of interest to inhibit COX2 in the context of inflammation. It is a protective attempt by the organism to remove the injurious stimuli and to initiate the healing process. The structure of COX 2 is screened using SP (Standard Precision) method under molecular docking techniques (Computer aided Design) with reference to novel 1-N-substituted-3, 5-diphenyl-2-pyrazoline derivatives. Based on their score and energy few ligands are selected to Induced Fit Docking (IFD) studies and compared with the existing drug molecules. The result showed that the docked ligands maintain favorable interactions with the active site residues of COX-2. All docking studies were performed using the molecular modeling software GLIDE of Schrodinger package.