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4-amino-substituted benzenesulfonamides as inhibitors of human carbonic anhydrases.

ABSTRACT: A series of N-aryl-?-alanine derivatives and diazobenzenesulfonamides containing aliphatic rings were designed, synthesized, and their binding to carbonic anhydrases (CA) I, II, VI, VII, XII, and XIII was studied by the fluorescent thermal shift assay and isothermal titration calorimetry. The results showed that 4-substituted diazobenzenesulfonamides were more potent CA binders than N-aryl-?-alanine derivatives. Most of the N-aryl-?-alanine derivatives showed better affinity for CA II while diazobenzenesulfonamides possessed nanomolar affinities towards CA I isozyme. X-ray crystallographic structures showed the modes of binding of both compound groups.

SUBMITTER: Rutkauskas K

PROVIDER: S-EPMC6271771 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature

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4-amino-substituted benzenesulfonamides as inhibitors of human carbonic anhydrases.

Rutkauskas Kęstutis K Zubrienė Asta A Tumosienė Ingrida I Kantminienė Kristina K Kažemėkaitė Marytė M Smirnov Alexey A Kazokaitė Justina J Morkūnaitė Vaida V Čapkauskaitė Edita E Manakova Elena E Gražulis Saulius S Beresnevičius Zigmuntas J ZJ Matulis Daumantas D

Molecules (Basel, Switzerland) 20141028 11

A series of N-aryl-β-alanine derivatives and diazobenzenesulfonamides containing aliphatic rings were designed, synthesized, and their binding to carbonic anhydrases (CA) I, II, VI, VII, XII, and XIII was studied by the fluorescent thermal shift assay and isothermal titration calorimetry. The results showed that 4-substituted diazobenzenesulfonamides were more potent CA binders than N-aryl-β-alanine derivatives. Most of the N-aryl-β-alanine derivatives showed better affinity for CA II while diaz ...[more]

PMID: 25353386

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