Structure-based drug design of novel inhibitors of carbonic anhydrase for treatment of glaucoma
Author(s)
Paul, Blessy
Singer, Mathilde
Lopez, Marie
Poulsen, Sally-Ann
Hofmann, Andreas
Griffith University Author(s)
Year published
2009
Metadata
Show full item recordAbstract
In humans, there are twelve carbonic anhydrase (CA) isozymes that possess catalytic activity for the reversible hydration of carbon dioxide. Carbonic anhydrases (CAs) underpin crucial physiological and pathological processes and are thus pharmaceutical targets for a variety of diseases, including glaucoma (CAII). Aromatic sulfonamides are the classical small molecule CA inhibitors and act through coordination of the sulfonamide anion (Ar-SO2NH-) to the active site zinc cation, replacing the zinc-bound hydroxyl anion, thereby impeding the endogenous reaction.In humans, there are twelve carbonic anhydrase (CA) isozymes that possess catalytic activity for the reversible hydration of carbon dioxide. Carbonic anhydrases (CAs) underpin crucial physiological and pathological processes and are thus pharmaceutical targets for a variety of diseases, including glaucoma (CAII). Aromatic sulfonamides are the classical small molecule CA inhibitors and act through coordination of the sulfonamide anion (Ar-SO2NH-) to the active site zinc cation, replacing the zinc-bound hydroxyl anion, thereby impeding the endogenous reaction.
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Conference Title
Structure-based drug design of novel inhibitors of carbonic anhydrase for treatment of glaucoma
Subject
Structural Chemistry and Spectroscopy