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.
Inhibition of carbonic anhydrases by a substrate analog: benzyl carbamate directly coordinates the catalytic zinc ion mimicking bicarbonate binding / De Simone G.; Angeli A.; Bozdag M.; Supuran C.T.; Winum J.-Y.; Monti S.M.; Alterio V.. - In: CHEMICAL COMMUNICATIONS. - ISSN 1359-7345. - ELETTRONICO. - 54:(2018), pp. 10312-10315. [10.1039/C8CC05755A]
Inhibition of carbonic anhydrases by a substrate analog: benzyl carbamate directly coordinates the catalytic zinc ion mimicking bicarbonate binding
Angeli A.;Bozdag M.;Supuran C. T.;
2018
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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