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.
2012
48
8838
8840
A. D. Fiore;A. Maresca;C. T. Supuran;G. D. Simone
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/776378
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