Affinity of sulfamates and sulfamides to carbonic anhydrase II isoform: experimental and molecular modeling approaches.

Luciana Gavernet, Jose L Gonzalez Funes, Luis Bruno Blanch, Guillermina Estiu, Alfonso Maresca, Claudiu T Supuran

Journal: Journal of chemical information and modeling 2010;50(6):1113-22

PMID: 20481572

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Abstract

Sixteen aromatic and aliphatic sulfamides and sulfamates were synthesized and tested in their inhibition to carbonic anhydrase CAII activity. The weaker inhibition pattern shown by sulfamides as compared to sulfamates is interpreted in this research by means of molecular modeling techniques, including known inhibitors (topiramate and its sulfamide cognate) in the analysis. The results nicely explain the origin of the inhibitory activity, which is not only related to positive interactions of the ligand with the active site residues but also to the solvation pattern characteristic of each ligand.

Address: Medicinal Chemistry, Department of Biological Sciences, Faculty of Exact Sciences, National University of La Plata, 47 and 115, La Plata B1900BJW, Argentina. [email protected]

DOI: 10.1021/ci100112s

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MeSH Terms: Carbonic Anhydrase II, Catalytic Domain, Isoenzymes, Ligands, Molecular Dynamics Simulation, Protein Binding, Solvents, Sulfonamides, Sulfonic Acids, Water