Carbonic anhydrase inhibitors: Inhibition of human, bacterial, and archaeal isozymes with benzene-1,3-disulfonamides - Solution and crystallographic studies (Articolo in rivista)

Type
Label
  • Carbonic anhydrase inhibitors: Inhibition of human, bacterial, and archaeal isozymes with benzene-1,3-disulfonamides - Solution and crystallographic studies (Articolo in rivista) (literal)
Anno
  • 2007-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.bmcl.2007.05.045 (literal)
Alternative label
  • Alterio V; De Simone G; Monti SM; Scozzafava A; Supuran CT. (2007)
    Carbonic anhydrase inhibitors: Inhibition of human, bacterial, and archaeal isozymes with benzene-1,3-disulfonamides - Solution and crystallographic studies
    in Bioorganic & medicinal chemistry letters (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Alterio V; De Simone G; Monti SM; Scozzafava A; Supuran CT. (literal)
Pagina inizio
  • 4201 (literal)
Pagina fine
  • 4207 (literal)
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  • 17 (literal)
Rivista
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  • Pubblicazione su rivista scientifica (literal)
Note
  • Scopu (literal)
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 80134 Naples, Italy; Università degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Rm. 188, Via della Lastruccia 3, 50019 Sesto Fiorentino (Florence), Italy (literal)
Titolo
  • Carbonic anhydrase inhibitors: Inhibition of human, bacterial, and archaeal isozymes with benzene-1,3-disulfonamides - Solution and crystallographic studies (literal)
Abstract
  • Three benzene-1,3-disulfonamide derivatives were investigated for their interaction with 12 mammalian a-carbonic anhydrases (CAs, EC 4.2.1.1), and three bacterial/archaeal CAs belonging to the ?-, ?-, and ?-CA class, respectively. X-ray crystal structure of the three inhibitors in complex with the dominant human isozyme CA II revealed a particular binding mode within the cavity. The sulfonamide group in meta-position to the Zn2+-coordinated SO2NH2 moiety was oriented toward the hydrophilic side of the active site cleft, establishing hydrogen bonds with His64, Asn67, Gln92, and Thr200. The plane of the phenyl moiety of the inhibitors was rotated by 45° and tilted by 10° with respect to its most recurrent orientation in other CA II-sulfonamide complexes. (literal)
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