Issue 70, 2012
From the journal:

Chemical Communications

Hydroxamate represents a versatile zinc binding group for the development of new carbonic anhydrase inhibitors†

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

* Corresponding authors

a Istituto di Biostrutture e Bioimmagini - CNR, Napoli, Italy
E-mail: gdesimon@unina.it
Fax: +39 0812536642
Tel: +39 0812534579

b Università degli Studi di Firenze, Sesto Fiorentino, Florence, Italy
E-mail: claudiu.supuran@unifi.it
Fax: +39 0554573385
Tel: +39 0554573005

Abstract

Hydroxamates (R–CONHOH) have been scarcely investigated as carbonic anhydrase (CA, EC 4.2.1.1) inhibitors (CAIs). An inhibition/structural study of PhCONHOH is reported against all human isoforms. Comparing aliphatic (R = Me and CF3) and aromatic (R = Ph) hydroxamates as CAIs, we prove that CONHOH is a versatile zinc binding group. Depending on the nature of the R moiety, it can adopt different coordination modes to the catalytic ion within the CA active site.

Graphical abstract: Hydroxamate represents a versatile zinc binding group for the development of new carbonic anhydrase inhibitors

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Article information

DOI
https://doi.org/10.1039/C2CC34275H
Article type
Communication
Submitted
14 Jun 2012
Accepted
16 Jul 2012
First published
17 Jul 2012

Chem. Commun., 2012,48, 8838-8840

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Hydroxamate represents a versatile zinc binding group for the development of new carbonic anhydrase inhibitors

A. Di Fiore, A. Maresca, C. T. Supuran and G. De Simone, Chem. Commun., 2012, 48, 8838 DOI: 10.1039/C2CC34275H

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