Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1366079 | Bioorganic & Medicinal Chemistry Letters | 2007 | 7 Pages |
Abstract
Sulthiame, a clinically used antiepileptic, was investigated for its interaction with 12 catalytically active mammalian carbonic anhydrase (CA, EC 4.2.1.1) isoforms. The drug is a potent inhibitor of CA II, VII, IX, and XII (KIs of 6–56 nM), and a medium potency inhibitor against CA IV, VA, VB, and VI (KIs of 81–134 nM). The high resolution crystal structure of the hCA II-sulthiame adduct revealed a large number of favorable interactions between the drug and the enzyme which explain its strong low nanomolar affinity for this isoform and may also be exploited for the design of effective inhibitors incorporating sultam moieties.
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Related Topics
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Organic Chemistry
Authors
Claudia Temperini, Alessio Innocenti, Antonio Mastrolorenzo, Andrea Scozzafava, Claudiu T. Supuran,