Inhibition of carbonic anhydrases by a substrate analog: benzyl carbamate directly coordinates the catalytic zinc ion mimicking bicarbonate binding

Giuseppina de Simone; Andrea Angeli; Murat Bozdag; Claudiu Supuran; Jean-Yves Winum; Simona Maria Monti; Vincenzo Alterio

doi:10.1039/c8cc05755a

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Inhibition of carbonic anhydrases by a substrate analog: benzyl carbamate directly coordinates the catalytic zinc ion mimicking bicarbonate binding

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Inhibition of carbonic anhydrases by a substrate analog: benzyl carbamate directly coordinates the catalytic zinc ion mimicking bicarbonate binding

Giuseppina de Simone, Andrea Angeli, Murat Bozdag, Claudiu Supuran, Jean-Yves Winum, Simona Maria Monti and Vincenzo Alterio

Chemical Communications, Vol.54(73), pp.10312-10315

2018

DOI: https://doi.org/10.1039/c8cc05755a

Abstract

N-Unsubstituted carbamates have scarcely been investigated so far as carbonic anhydrase inhibitors (CAIs). By means of kinetic and structural studies, in this paper we demonstrate that such molecules can effectively inhibit hCAs and can be used as lead compounds for the development of CAIs possessing a binding mode similar to one of the CA substrates, bicarbonate.

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Title: Inhibition of carbonic anhydrases by a substrate analog: benzyl carbamate directly coordinates the catalytic zinc ion mimicking bicarbonate binding
Creators - without role: Giuseppina de Simone - Institute of Biostructure and Bioimaging
Andrea Angeli - University of Florence
Murat Bozdag - University of Florence
Claudiu Supuran - University of Florence
Jean-Yves Winum - Université de Montpellier, Institut des Biomolécules Max Mousseron - IBMM
Simona Maria Monti - Institute of Biostructure and Bioimaging
Vincenzo Alterio - Institute of Biostructure and Bioimaging
Publication Details: Chemical Communications, Vol.54(73), pp.10312-10315
Identifiers: 9944586709311
Academic Unit: Institut des Biomolécules Max Mousseron - IBMM
Language: English
Resource Type: Journal article
Local Fields: hal-03551584