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

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.

SUBMITTER: Morkunaite V

PROVIDER: S-EPMC4168026 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

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

Morkūnaitė Vaida V Baranauskienė Lina L Zubrienė Asta A Kairys Visvaldas V Ivanova Jekaterina J Trapencieris Pēteris P Matulis Daumantas D

BioMed research international 20140903

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 partic ...[more]

PMID: 25276805

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