Molecular basis of cyclooxygenase enzymes (COXs) selective inhibition
Vittorio Limongelli1, Massimiliano Bonomi, Luciana Marinelli
1Computational Science, Department of Chemistry and Applied Biosciences, Eidgenössiche Technische Hochschule Zürich, Università della Svizzera Italiana Campus, Via Giuseppe Buffi 13, CH-6900 Lugano, Switzerland.
Abstract:
The widely used nonsteroidal anti-inflammatory drugs block the cyclooxygenase enzymes (COXs) and are clinically used for the treatment of inflammation, pain, and cancers. A selective inhibition of the different isoforms, particularly COX-2, is desirable, and consequently a deeper understanding of the molecular basis of selective inhibition is of great demand. Using an advanced computational technique we have simulated the full dissociation process of a highly potent and selective inhibitor, SC-558, in both COX-1 and COX-2. We have found a previously unreported alternative binding mode in COX-2 explaining the time-dependent inhibition exhibited by this class of inhibitors and consequently their long residence time inside this isoform. Our metadynamics-based approach allows us to illuminate the highly dynamical character of the ligand/protein recognition process, thus explaining a wealth of experimental data and paving the way to an innovative strategy for designing new COX inhibitors with tuned selectivity.
Related Concept Videos
Pharmacogenetics of Phase I Enzymes: Cytochrome P450 Isozymes
Cycloaddition Reactions: MO Requirements for Thermal Activation
Enzyme Inhibition
Inhibition of Cdk Activity
Inhibition of CDK Activity
Inhibitors of Bacterial DNA Synthesis

