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Investigation on Hydrazonobenzenesulfonamides as Human Carbonic Anhydrase I, II, IX and XII Inhibitors.
Moi, Davide; Vittorio, Serena; Angeli, Andrea; Balboni, Gianfranco; Supuran, Claudiu T; Onnis, Valentina.
Afiliación
  • Moi D; Department of Life and Environmental Sciences, University of Cagliari, University Campus, S.P. 8 CA, 09042 Monserrato, Italy.
  • Vittorio S; Dipartimento di Scienze Farmaceutiche, Università degli Studi di Milano,Via Mangiagalli 25, 20133 Milano, Italy.
  • Angeli A; Laboratorio di Chimica Bioinorganica, Polo Scientifico Neurofarba Department, Università Degli Studi di Firenze, Room 188, Via della Lastruccia 3, Sesto Fiorentino, 50019 Florence, Italy.
  • Balboni G; Department of Life and Environmental Sciences, University of Cagliari, University Campus, S.P. 8 CA, 09042 Monserrato, Italy.
  • Supuran CT; Laboratorio di Chimica Bioinorganica, Polo Scientifico Neurofarba Department, Università Degli Studi di Firenze, Room 188, Via della Lastruccia 3, Sesto Fiorentino, 50019 Florence, Italy.
  • Onnis V; Department of Life and Environmental Sciences, University of Cagliari, University Campus, S.P. 8 CA, 09042 Monserrato, Italy.
Molecules ; 28(1)2022 Dec 22.
Article en En | MEDLINE | ID: mdl-36615285
A small series of hydrazonobenzenesulfonamides was designed, synthesized and studied for their human carbonic anhydrase (hCA) inhibitory activity. The synthesized compounds were evaluated against hCA I, II, IX and XII isoforms using acetazolamide (AAZ) as the standard inhibitor. Various hydrazonosulfonamide derivatives showed inhibitory activity at low nanomolar levels with selectivity against the cytosolic hCA II isoform, as well as the transmembrane, tumor-associated enzymes hCA IX and XII. The most potent and selective hydrazones 8, 9, 10, 11, 19 and 24 were docked into isoforms I, II, IX and XII to better understand their activity and selectivity for the different CA isoforms.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Anhidrasas Carbónicas / Anhidrasa Carbónica I Límite: Humans Idioma: En Revista: Molecules Asunto de la revista: BIOLOGIA Año: 2022 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Suiza
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Anhidrasas Carbónicas / Anhidrasa Carbónica I Límite: Humans Idioma: En Revista: Molecules Asunto de la revista: BIOLOGIA Año: 2022 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Suiza