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4-Amino-substituted Benzenesulfonamides as Inhibitors of Human Carbonic Anhydrases

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 result...

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Detalles Bibliográficos
Autores principales: Rutkauskas, Kęstutis, Zubrienė, Asta, Tumosienė, Ingrida, Kantminienė, Kristina, Kažemėkaitė, Marytė, Smirnov, Alexey, Kazokaitė, Justina, Morkūnaitė, Vaida, Čapkauskaitė, Edita, Manakova, Elena, Gražulis, Saulius, Beresnevičius, Zigmuntas J., Matulis, Daumantas
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6271771/
https://www.ncbi.nlm.nih.gov/pubmed/25353386
http://dx.doi.org/10.3390/molecules191117356
Descripción
Sumario: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 diazobenzenesulfonamides possessed nanomolar affinities towards CA I isozyme. X-ray crystallographic structures showed the modes of binding of both compound groups.