Drug Design of Carbonic Anhydrase Inhibitors as Anticonvulsant Agents

2009 ◽  
pp. 171-191
Author(s):  
Anne Thiry ◽  
Jean-Michel Dogn ◽  
Claudiu T. Supuran ◽  
Bernard Masereel
Keyword(s):  
Drug Design ◽  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Inhibitors ◽  
Anticonvulsant Agents

In Vivo Evaluation of Selective Carbonic Anhydrase Inhibitors as Potential Anticonvulsant Agents

ChemMedChem ◽  
2016 ◽  
Vol 11 (16) ◽  
pp. 1812-1818 ◽  
Author(s):  
Elvira Bruno ◽  
Maria R. Buemi ◽  
Laura De Luca ◽  
Stefania Ferro ◽  
Anna-Maria Monforte ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
In Vivo Evaluation ◽  
Carbonic Anhydrase Inhibitors ◽  
Anticonvulsant Agents

Carbonic Anhydrase Inhibitors as Anticonvulsant Agents

2007 ◽  
Vol 7 (9) ◽  
pp. 855-864 ◽  
Author(s):  
Anne Thiry ◽  
Jean-Michel Dogne ◽  
Claudiu Supuran ◽  
Bernard Masereel
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Inhibitors ◽  
Anticonvulsant Agents

scholarly journals Hydrophobic Substituents of the Phenylmethylsulfamide Moiety Can Be Used for the Development of New Selective Carbonic Anhydrase Inhibitors

2014 ◽  
Vol 2014 ◽  
pp. 1-11 ◽  
Author(s):  
Giuseppina De Simone ◽  
Ginta Pizika ◽  
Simona Maria Monti ◽  
Anna Di Fiore ◽  
Jekaterina Ivanova ◽  
...  
Keyword(s):  
Drug Design ◽  
Carbonic Anhydrase ◽  
Van Der Waals ◽  
Van Der Waals Interactions ◽  
Zinc Binding ◽  
Binding Mechanism ◽  
Carbonic Anhydrase Inhibitors ◽  
X Ray ◽  
Human Carbonic Anhydrase ◽  
Hydrophobic Cleft

A new series of compounds containing a sulfamide moiety as zinc-binding group (ZBG) has been synthesized and tested for determining inhibitory properties against four human carbonic anhydrase (hCA) isoforms, namely, CAs I, II, IX, and XII. The X-ray structure of the cytosolic dominant isoform hCA II in complex with the best inhibitor of the series has also been determined providing further insights into sulfamide binding mechanism and confirming that such zinc-binding group, if opportunely derivatized, can be usefully exploited for obtaining new potent and selective CAIs. The analysis of the structure also suggests that for drug design purposes the but-2-yn-1-yloxy moiety tail emerges as a very interesting substituent of the phenylmethylsulfamide moiety due to its capability to establish strong van der Waals interactions with a hydrophobic cleft on the hCA II surface, delimited by residues Phe131, Val135, Pro202, and Leu204. Indeed, the complementarity of this tail with the cleft suggests that different substituents could be used to discriminate between isoforms having clefts with different sizes.

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