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Carbonic anhydrase inhibitors. The nematode α-carbonic anhydrase of Caenorhabditis elegans CAH-4b is highly inhibited by 2-(hydrazinocarbonyl)-3-substituted-phenyl-1H-indole-5-sulfonamides

Güzel, Özlen, Innocenti, Alessio, Hall, Rebecca A., Scozzafava, Andrea, Mühlschlegel, Fritz A., Supuran, Claudiu T. (2009) Carbonic anhydrase inhibitors. The nematode α-carbonic anhydrase of Caenorhabditis elegans CAH-4b is highly inhibited by 2-(hydrazinocarbonyl)-3-substituted-phenyl-1H-indole-5-sulfonamides. Bioorganic & Medicinal Chemistry, 17 (8). pp. 3212-3215. ISSN 0968-0896. (doi:10.1016/j.bmc.2009.01.048) (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:91843)

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
https://doi.org/10.1016/j.bmc.2009.01.048

Abstract

A series of 2-(hydrazinocarbonyl)-3-substituted-phenyl-1H-indole-5-sulfonamides 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 an alpha-carbonic anhydrase (CA, EC 4.2.1.1) of the nematode model organism Caenorhabditis elegans (CAH-4b, or ceCA). The substitution pattern at the 3-phenyl ring highly influenced the ceCA inhibitory activity of these heterocyclic sulfonamides, with best inhibitors (K(I)s in the range of 6.0-13.4 nM) incorporating 3-methyl-, 4-methyl-, 2-/3-/4-fluoro-, 4-chloro- and 3-/4-bromo-phenyl such moieties. Some of these sulfonamides also showed a good selectivity profile for the inhibition of the nematode over the human isozymes CA I and II (selectivity ratios in the range of 1.78-4.95 for the inhibition of ceCA over hCA II). These data can be used for the design of possibly new antihelmintic drugs, since the genome of many parasitic nematodes encode for a multitude of orthologue CA isozymes to ceCA investigated here.

Item Type: Article
DOI/Identification number: 10.1016/j.bmc.2009.01.048
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: Becky Hall
Date Deposited: 01 Dec 2021 09:26 UTC
Last Modified: 02 Dec 2021 22:42 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/91843 (The current URI for this page, for reference purposes)
Hall, Rebecca A.: https://orcid.org/0000-0002-4908-8168
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