Comparación computacional de la afinidad de unión de AINES selectivos y no selectivos hacia la COX-2 mediante docking molecular

Abstract

Cyclooxygenase (COX) is a key enzyme in the synthesis of inflammatory prostaglandins, with two main isoforms: COX-1, which is found in various tissues and is involved in homeostatic functions, and COX-2, which is primarily expressed in inflamed tissues. Non-steroidal anti-inflammatory drugs (NSAIDs) are widely used for their anti-inflammatory, analgesic, and antipyretic effects. These drugs are divided into non-selective NSAIDs, which inhibit both COX-1 and COX-2, and selective NSAIDs, which preferentially inhibit COX-2, thereby reducing gastrointestinal side effects. This research aims to compare, through computational simulations, the binding affinity of selective and non-selective NSAIDs towards the COX-2 enzyme, which plays a key role in inflammatory processes. Using advanced molecular docking techniques, the interactions between drugs and COX-2 were evaluated by analyzing parameters such as binding free energy and inhibition constant. The observed differences between both types of NSAIDs highlight the relevance of these molecular interactions, providing valuable insights for optimizing therapeutic agents that specifically target COX-2. The results of this study offer new perspectives for the design of more effective anti-inflammatory drugs, improving treatment strategies for various inflammatory conditions.