Carbonic anhydrase inhibitors: Inhibition of the ?-class enzyme from the pathogenic yeast Candida glabrata with sulfonamides, sulfamates and sulfamides.

Vullo, Daniela, Leewattanapasuk, Worraanong, Mühlschlegel, Fritz A., Mastrolorenzo, Antonio, Capasso, Clemente, Supuran, Claudiu T. (2013) Carbonic anhydrase inhibitors: Inhibition of the ?-class enzyme from the pathogenic yeast Candida glabrata with sulfonamides, sulfamates and sulfamides. Bioorganic & Medicinal Chemistry Letters, 23 (9). pp. 2647-2652. ISSN 0960-894X. (doi:10.1016/j.bmcl.2013.02.092) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:33684)

The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided.
Official URL: http://dx.doi.org/10.1016/j.bmcl.2013.02.092

Abstract

The fungal pathogen Candida glabrata encodes for a ?-carbonic anhydrase (CA, EC 4.2.1.1), CgNce103, recently discovered. Only anions have been investigated as CgNce103 inhibitors up until now. Here we report the first sulfonamides inhibition study of this enzyme. Simple sulfonamides showed weak or moderate CgNce103 inhibitory properties, whereas acetazolamide, and a series of 4-substituted ureido-benzene-sulfonamides, sulfamates and sulfamides showed effective CgNce103 inhibitory properties, with KIs in the range of 4.1–115 nM, being also ineffective as human CA II inhibitors. As there is significant resistance of C. glabrata clinical isolates to many classical antifungal agents, inhibition of the ?-CA from this organism may allow an interesting means of controlling the pathogen growth, eventually leading to antifungals with a novel mechanism of action.

Item Type:	Article
DOI/Identification number:	10.1016/j.bmcl.2013.02.092
Subjects:	Q Science
Divisions:	Divisions > Division of Natural Sciences > Biosciences
Depositing User:	Susan Davies
Date Deposited:	24 Apr 2013 14:35 UTC
Last Modified:	05 Nov 2024 10:16 UTC
Resource URI:	https://kar.kent.ac.uk/id/eprint/33684 (The current URI for this page, for reference purposes)

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Mühlschlegel, Fritz A..

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