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Sulfonamides incorporating 1,3,5-triazine moieties selectively and potently inhibit carbonic anhydrase transmembrane isoforms IX, XII and XIV over cytosolic isoforms I and II: Solution and X-ray crystallographic studies.
Carta, Fabrizio; Garaj, Vladimir; Maresca, Alfonso; Wagner, Jason; Avvaru, Balendu Sankara; Robbins, Arthur H; Scozzafava, Andrea; McKenna, Robert; Supuran, Claudiu T.
Afiliación
  • Carta F; Università degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica, Florence, Italy.
Bioorg Med Chem ; 19(10): 3105-19, 2011 May 15.
Article en En | MEDLINE | ID: mdl-21515057
Reaction of cyanuryl chloride with d,l-amino acids and amino alcohols afforded a new series of triazinyl-substituted benzenesulfonamides incorporating amino acyl/hydroxyalkyl-amino moieties. Inhibition studies of physiologically relevant human carbonic anhydrase (CA, EC 4.2.1.1) isoforms, such as CA I, II, IX, XII and XIV with these compounds are reported. They showed moderate-weak inhibition of the cytosolic, offtarget isozymes CA I and II, but many of them were low nanomolar inhibitors of the transmembrane, tumor-associated CA IX and XII (and also of CA XIV). The X-ray crystal structure of two of these compounds in adduct with CA II allowed us to understand the features associated with this strong inhibitory properties and possibly also their selectivity. Two of these compounds were also investigated for the inhibition of other human isoforms, that is, hCA IV, VA, VB, VI, VII and XIII, as well as inhibitors of the fungal pathogenic CAs Nce103 (Candida albicans) and Can2 (Cryptococcus neoformans), showing interesting activity. The 1,3,5-triazinyl-substituted benzenesulfonamides constitute thus a class of compounds with great potential for obtaining inhibitors targeting both α-class mammalian, tumor-associated, and ß-class from pathogenic organisms CAs.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Sulfonamidas / Inhibidores de Anhidrasa Carbónica / Anhidrasa Carbónica I / Anhidrasa Carbónica II Límite: Humans Idioma: En Revista: Bioorg Med Chem Asunto de la revista: BIOQUIMICA / QUIMICA Año: 2011 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Sulfonamidas / Inhibidores de Anhidrasa Carbónica / Anhidrasa Carbónica I / Anhidrasa Carbónica II Límite: Humans Idioma: En Revista: Bioorg Med Chem Asunto de la revista: BIOQUIMICA / QUIMICA Año: 2011 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Reino Unido