boron and sulfamic-acid

boron has been researched along with sulfamic-acid* in 1 studies

Other Studies

1 other study(ies) available for boron and sulfamic-acid

Article	Year
Carbonic anhydrase inhibitors: crystallographic and solution binding studies for the interaction of a boron-containing aromatic sulfamide with mammalian isoforms I-XV. Bioorganic & medicinal chemistry letters, 2010, Jun-15, Volume: 20, Issue:12 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. Topics: Amides; Boron; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Catalytic Domain; Crystallography, X-Ray; Hydrocarbons, Aromatic; Protein Binding; Protein Isoforms; Solutions; Sulfonic Acids; Zinc	2010

Article

Year

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

Bioorganic & medicinal chemistry letters, 2010, Jun-15, Volume: 20, Issue:12

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.

Topics: Amides; Boron; Carbonic Anhydrase Inhibitors; Carbonic Anhydrases; Catalytic Domain; Crystallography, X-Ray; Hydrocarbons, Aromatic; Protein Binding; Protein Isoforms; Solutions; Sulfonic Acids; Zinc

2010