Hydroxamates (R-CONHOH) have been scarcely investigated as carbonic anhydrase (CA, EC 4.2.1.1) inhibitors (CAIs). An inhibition/structural study of PhCONHOH is reported against all human isoforms. Comparing aliphatic (R = Me and CF(3)) and aromatic (R = Ph) hydroxamates as CAIs, we prove that CONHOH is a versatile zinc binding group. Depending on the nature of the R moiety, it can adopt different coordination modes to the catalytic ion within the CA active site.
Hydroxamate represents a versatile zinc binding group for the development of new carbonic anhydrase inhibitors / A. D. Fiore;A. Maresca;C. T. Supuran;G. D. Simone. - In: CHEMICAL COMMUNICATIONS. - ISSN 1359-7345. - STAMPA. - 48:(2012), pp. 8838-8840. [10.1039/c2cc34275h]
Hydroxamate represents a versatile zinc binding group for the development of new carbonic anhydrase inhibitors.
SUPURAN, CLAUDIU TRANDAFIR;
2012
Abstract
Hydroxamates (R-CONHOH) have been scarcely investigated as carbonic anhydrase (CA, EC 4.2.1.1) inhibitors (CAIs). An inhibition/structural study of PhCONHOH is reported against all human isoforms. Comparing aliphatic (R = Me and CF(3)) and aromatic (R = Ph) hydroxamates as CAIs, we prove that CONHOH is a versatile zinc binding group. Depending on the nature of the R moiety, it can adopt different coordination modes to the catalytic ion within the CA active site.I documenti in FLORE sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.