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Biomed Res Int. 2014;2014:638902. doi: 10.1155/2014/638902. Epub 2014 Sep 3.

Saccharin sulfonamides as inhibitors of carbonic anhydrases I, II, VII, XII, and XIII.

Author information

1
Department of Biothermodynamics and Drug Design, Institute of Biotechnology, Vilnius University, Graičiūno 8, LT-02241 Vilnius, Lithuania.
2
Department of Bioinformatics, Institute of Biotechnology, Vilnius University, Graičiūno 8, LT-02241 Vilnius, Lithuania.
3
Department of Organic Chemistry, Latvian Institute of Organic Synthesis, Aizkraukles 21, Riga LV-1006, Latvia.

Abstract

A series of modified saccharin sulfonamides have been designed as carbonic anhydrase (CA) inhibitors and synthesized. Their binding to CA isoforms I, II, VII, XII, and XIII was measured by the fluorescent thermal shift assay (FTSA) and isothermal titration calorimetry (ITC). Saccharin bound the CAs weakly, exhibiting the affinities of 1-10 mM for four CAs except CA I where binding could not be detected. Several sulfonamide-bearing saccharines exhibited strong affinities of 1-10 nM towards particular CA isoforms. The functional group binding Gibbs free energy additivity maps are presented which may provide insights into the design of compounds with increased affinity towards selected CAs.

PMID:
25276805
PMCID:
PMC4168026
DOI:
10.1155/2014/638902
[Indexed for MEDLINE]
Free PMC Article

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