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Int. J. Mol. Sci. 2016, 17(7), 1150; doi:10.3390/ijms17071150

Non-Classical Inhibition of Carbonic Anhydrase

1
Department of Biochemistry and Molecular Biology, University of Florida, Gainesville, FL 32611, USA
2
Neurofarba Department, University of Florence, Piazza di San Marco, Firenze 50019, Italy
*
Author to whom correspondence should be addressed.
Academic Editor: Ester Boix
Received: 31 May 2016 / Revised: 2 July 2016 / Accepted: 7 July 2016 / Published: 16 July 2016
(This article belongs to the Special Issue Enzyme-Inhibitor Interaction as Examples of Molecular Recognition)
View Full-Text   |   Download PDF [8404 KB, uploaded 16 July 2016]   |  

Abstract

Specific isoforms from the carbonic anhydrase (CA) family of zinc metalloenzymes have been associated with a variety of diseases. Isoform-specific carbonic anhydrase inhibitors (CAIs) are therefore a major focus of attention for specific disease treatments. Classical CAIs, primarily sulfonamide-based compounds and their bioisosteres, are examined as antiglaucoma, antiepileptic, antiobesity, antineuropathic pain and anticancer compounds. However, many sulfonamide compounds inhibit all CA isoforms nonspecifically, diluting drug effectiveness and causing undesired side effects due to off-target inhibition. In addition, a small but significant percentage of the general population cannot be treated with sulfonamide-based compounds due to a sulfa allergy. Therefore, CAIs must be developed that are not only isoform specific, but also non-classical, i.e. not based on sulfonamides, sulfamates, or sulfamides. This review covers the classes of non-classical CAIs and the recent advances in the development of isoform-specific inhibitors based on phenols, polyamines, coumarins and their derivatives. View Full-Text
Keywords: carbonic anhydrase; carboxylate; coumarin; non-classical carbonic anhydrase; carboxylate; coumarin; non-classical
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Lomelino, C.L.; Supuran, C.T.; McKenna, R. Non-Classical Inhibition of Carbonic Anhydrase. Int. J. Mol. Sci. 2016, 17, 1150.

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