Jump to main content
Jump to site search

Issue 44, 2010
Previous Article Next Article

Selective hydrophobic pocket binding observed within the carbonic anhydrase II active site accommodate different 4-substituted-ureido-benzenesulfonamides and correlate to inhibitor potency

Author affiliations

Abstract

4-Substituted-ureido benzenesulfonamides showing inhibitory activity against carbonic anhydrase (CA, EC 4.2.1.1) II between 3.3–226 nM were crystallized in complex with the enzyme. Hydrophobic interactions between the scaffold of the inhibitors in different hydrophobic pockets of the enzyme were observed, explaining the diverse inhibitory range of these derivatives.

Graphical abstract: Selective hydrophobic pocket binding observed within the carbonic anhydrase II active site accommodate different 4-substituted-ureido-benzenesulfonamides and correlate to inhibitor potency

Back to tab navigation
Please wait while Download options loads

Supplementary files

Publication details

The article was received on 21 Jul 2010, accepted on 20 Sep 2010 and first published on 05 Oct 2010


Article type: Communication
DOI: 10.1039/C0CC02707C
Citation: Chem. Commun., 2010,46, 8371-8373
  •   Request permissions

    Selective hydrophobic pocket binding observed within the carbonic anhydrase II active site accommodate different 4-substituted-ureido-benzenesulfonamides and correlate to inhibitor potency

    F. Pacchiano, M. Aggarwal, B. S. Avvaru, A. H. Robbins, A. Scozzafava, R. McKenna and C. T. Supuran, Chem. Commun., 2010, 46, 8371
    DOI: 10.1039/C0CC02707C

Search articles by author