Nonaromatic sulfonamide group as an ideal anchor for potent human carbonic anhydrase inhibitors: role of hydrogen-bonding networks in ligand binding and drug design.

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Abbate F, Supuran CT, Scozzafava A, Orioli P, Stubbs MT, Klebe G

Nonaromatic sulfonamide group as an ideal anchor for potent human carbonic anhydrase inhibitors: role of hydrogen-bonding networks in ligand binding and drug design.

J Med Chem. 2002 Aug 15;45(17):3583-7.

PubMed ID

12166931 [ View in PubMed

]

Abstract

X-ray crystal structures of the adducts of human carbonic anhydrase (hCA) isozyme II with derivatives incorporating a sulfamide or sulfamic acid moiety are reported. The absence of a C-SO(2)NH(2) bond in the first type of compound can be exploited for the design of more potent and selective CA inhibitors. This study also explains why sulfate is a several-orders-of-magnitude weaker CA inhibitor compared to derivatives incorporating sulfonamide/sulfamide moieties.

DrugBank Data that Cites this Article

Binding Properties

Drug	Target	Property	Measurement	pH	Temperature (°C)
Topiramate	Carbonic anhydrase 1	Ki (nM)	250	N/A	N/A	Details
Topiramate	Carbonic anhydrase 2	Ki (nM)	5	N/A	N/A	Details