| Literature DB >> 30553625 |
Irena Vaškevičienė1, Vaida Paketurytė2, Nikita Pajanok2, Šarūnas Žukauskas1, Birutė Sapijanskaitė1, Kristina Kantminienė3, Vytautas Mickevičius1, Asta Zubrienė4, Daumantas Matulis2.
Abstract
Two series of benzenesulfonamides bearing methyl groups at ortho/ortho or meta/ortho positions and a pyrrolidinone moiety at para position were synthesized and tested as inhibitors of the twelve catalytically active human carbonic anhydrase (CA) isoforms. Observed binding affinities were determined by fluorescent thermal shift assay and intrinsic binding affinities representing the binding of benzenesulfonamide anion to the Zn(II)-bound water form of CA were calculated. Introduction of dimethyl groups into benzenesulfonamide ring decreased the binding affinity to almost all CA isoforms, but gained in selectivity towards one CA isoform. A chloro group at the meta position of 2,6-dimethylbenzenesulfonamide derivatives did not influence the binding to CA I, but it increased the affinity to all other CAs, especially, CA VII and CA XIII (up to 500 fold). The compounds may be used for further development of CA inhibitors with higher selectivity to particular CA isoforms.Entities:
Keywords: 5-Oxopyrrolidine; Benzenesulfonamide; Carbonic anhydrase; Fluorescent thermal shift assay; Intrinsic thermodynamics
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Year: 2018 PMID: 30553625 DOI: 10.1016/j.bmc.2018.12.011
Source DB: PubMed Journal: Bioorg Med Chem ISSN: 0968-0896 Impact factor: 3.641