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Bioorg Med Chem Lett. 2010 Jun 15;20(12):3601-5. doi: 10.1016/j.bmcl.2010.04.114. Epub 2010 Apr 28.

Carbonic anhydrase inhibitors: crystallographic and solution binding studies for the interaction of a boron-containing aromatic sulfamide with mammalian isoforms I-XV.

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1
Istituto di Biostrutture e Bioimmagini-CNR, Naples, Italy.

Abstract

We investigated the inhibition of carbonic anhydrase (CA, EC 4.2.1.1) isoforms I-XV with 4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenylsulfamide and other simple or sugar sulfamides, a class of less investigated CA inhibitors (CAIs). The crystal structure of the adduct of hCA II with the boron-substituted sulfamide shows the organic scaffold of this compound bound in the hydrophilic half of the active site where it makes a large number of van der Waals contacts with Ile91, Gln92, Val121, Phe131, Leu198, and Thr200. The data here reported provide further insights into sulfamide binding mechanism confirming that this zinc-binding group could be usefully exploited for obtaining new potent and selective CAIs.

PMID:
20472429
DOI:
10.1016/j.bmcl.2010.04.114
[Indexed for MEDLINE]

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