Issue 42, 2011
From the journal:

Chemical Communications

Carbonic anhydrase inhibitors: X-ray crystallographic studies for the binding of N-substituted benzenesulfonamides to human isoform II†

Anna Di Fiore,a   Alfonso Maresca,b   Vincenzo Alterio,a   Claudiu T. Supuran*b  and  Giuseppina De Simone*a  

* Corresponding authors

a Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 80134 Napoli, Italy
E-mail: gdesimon@unina.it
Fax: +39-081-2536642
Tel: +39-081-2534579

b Università degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Rm. 188, Via della Lastruccia 3, 50019 Sesto Fiorentino (Florence), Italy
E-mail: claudiu.supuran@unifi.it
Fax: +39-055-4573385
Tel: +39-055-4573005

Abstract

N-substituted benzenesulfonamides, incorporating the N-amino-, N-hydroxy- and N-methoxy-moieties at the sulfonamide zinc binding group, have been investigated as CAIs by means of inhibition and structural studies, unraveling interesting aspects related to their inhibition mechanism.

Graphical abstract: Carbonic anhydrase inhibitors: X-ray crystallographic studies for the binding of N-substituted benzenesulfonamides to human isoform II

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Article information

DOI
https://doi.org/10.1039/C1CC14575D
Article type
Communication
Submitted
26 Jul 2011
Accepted
08 Sep 2011
First published
26 Sep 2011

Chem. Commun., 2011,47, 11636-11638

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Carbonic anhydrase inhibitors: X-ray crystallographic studies for the binding of N-substituted benzenesulfonamides to human isoform II

A. Di Fiore, A. Maresca, V. Alterio, C. T. Supuran and G. De Simone, Chem. Commun., 2011, 47, 11636 DOI: 10.1039/C1CC14575D

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