Carbonic anhydrase inhibitors. The beta-carbonic anhydrases from the fungal pathogens Cryptococcus neoformans and Candida albicans are strongly inhibited by substituted-phenyl-1H-indole-5-sulfonamides

Güzel, Ozlen, Maresca, Alfonso, Hall, Rebecca A., Scozzafava, Andrea, Mastrolorenzo, Antonio, Mühlschlegel, Fritz A., Supuran, Claudiu T. (2010) Carbonic anhydrase inhibitors. The beta-carbonic anhydrases from the fungal pathogens Cryptococcus neoformans and Candida albicans are strongly inhibited by substituted-phenyl-1H-indole-5-sulfonamides. Bioorganic & Medicinal Chemistry Letters, 20 (8). pp. 2508-11. ISSN 0960-894X. (doi:10.1016/j.bmcl.2010.02.103) (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:27483)

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.2010.02.103

Abstract

A series of 2-(hydrazinocarbonyl)-3-substituted-phenyl-1H-indole-5-sulfonamides and 1-({[5-(aminosulfonyl)-3-phenyl-1H-indol-2-yl]carbonyl}amino)-2,4,6 trimethylpyridinium perchlorates possessing various 2-, 3- or 4-substituted phenyl groups with methyl-, halogeno- and methoxy-functionalities, as well as the perfluorophenyl moiety, have been evaluated as inhibitors of the beta-carbonic anhydrases (CAs, EC 4.2.1.1) from the pathogenic fungi Cryptococcus neoformans (Can2) and Candida albicans (CaNce103). Both enzymes were potently inhibited by these sulfonamides, K(I)s in the range of 4.4-118 nM against Can2, and of 5.1-128 against CaNce103, respectively. Minor structural changes in the 3-substituted phenyl moiety contribute significantly to the inhibitory activity. Some of the investigated sulfonamides showed promising selectivity ratios for inhibiting Can2 over the host, human enzymes CA I and II.

Item Type:	Article
DOI/Identification number:	10.1016/j.bmcl.2010.02.103
Subjects:	Q Science
Divisions:	Divisions > Division of Natural Sciences > Biosciences
Depositing User:	Susan Davies
Date Deposited:	29 Jun 2011 16:34 UTC
Last Modified:	05 Nov 2024 10:08 UTC
Resource URI:	https://kar.kent.ac.uk/id/eprint/27483 (The current URI for this page, for reference purposes)

University of Kent Author Information

Hall, Rebecca A..

Creator's ORCID:	https://orcid.org/0000-0002-4908-8168
CReDIT Contributor Roles:

Mühlschlegel, Fritz A..

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