The binding of benzenesulfonamides to carbonic anhydrase enzyme. A molecular mechanics study and quantitative structure-activity relationships
- 30 April 1989
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of Medicinal Chemistry
- Vol. 32 (5) , 951-956
- https://doi.org/10.1021/jm00125a005
Abstract
Molecular mechanics methods have been applied to study the interation between a series of 20 deprotonated benzenesulfonamides and the enzyme carbonic anhydrase. The different contributions to the binding energy have been evalauted and correlated with experimental inhibition data and molecular orbital indices of the sulfonamides in their bound conformation. The results suggest that the discrimination shown by the enzyme toward these inhibitors is dominated by the short-range van der Waals forces.This publication has 9 references indexed in Scilit:
- A nuclear‐magnetic‐resonance study of the binding of novel N‐hydroxybenzenesulphonamide carbonic anhydrase inhibitors to native and cadmium‐111‐substituted carbonic anhydraseEuropean Journal of Biochemistry, 1985
- Lone-pair directionality in hydrogen-bond potential functions for molecular mechanics calculations: the inhibition of human carbonic anhydrase II by sulfonamidesJournal of the American Chemical Society, 1985
- A computational procedure for determining energetically favorable binding sites on biologically important macromoleculesJournal of Medicinal Chemistry, 1985
- A QUANTITATIVE STRUCTURE-ACTIVITY RELATIONSHIP AND MOLECULAR GRAPHICS STUDY OF CARBONIC-ANHYDRASE INHIBITORS1985
- Structure-Activity Relationships of Sulfonamide Drugs and Human Carbonic Anhydrase C: Modeling of Inhibitor Molecules into the Receptor Site of the Enzyme with an Interactive Computer Graphics Display1Journal of Pharmaceutical Sciences, 1984
- Nitrogen-15 nuclear magnetic resonance study of benzenesulfonamide and cyanate binding to carbonic anhydraseBiochemistry, 1983
- 1,3,4-Thiadiazole-5-sulfonamides as carbonic anhydrase inhibitors: Relationship between their electronic and hydrophobic structures and their inhibitory activity.CHEMICAL & PHARMACEUTICAL BULLETIN, 1978
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977
- Kinetic aspects of structure─activity relations: the binding of sulphonamides by carbonic anhydraseProceedings of the Royal Society of London. B. Biological Sciences, 1976