Inhibition of the α-carbonic anhydrase from Vibrio cholerae with amides and sulfonamides incorporating imidazole moieties

Daniela De Vita, Andrea Angeli, Fabiana Pandolfi, Martina Bortolami, Roberta Costi, Roberto Di Santo, Elisabetta Suffredini, Mariangela Ceruso, Sonia Del Prete, Clemente Capasso, Luigi Scipione, Claudiu T. Supuran

Research output: Contribution to journalArticle

Abstract

We discovered novel and selective sulfonamides/amides acting as inhibitors of the α-carbonic anhydrase (CA, EC 4.2.1.1) from the pathogenic bacterium Vibrio cholerae (VchCA). This Gram-negative bacterium is the causative agent of cholera and colonises the upper small intestine where sodium bicarbonate is present at a high concentration. The secondary sulfonamides and amides investigated here were potent, low nanomolar VchCA inhibitors whereas their inhibition of the human cytosolic isoforms CA I and II was in the micromolar range or higher. The molecules represent an interesting lead for antibacterial agents with a possibly new mechanism of action, although their CA inhibition mechanism is unknown for the moment.

Original languageEnglish
Pages (from-to)798-804
Number of pages7
JournalJournal of Enzyme Inhibition and Medicinal Chemistry
Volume32
Issue number1
DOIs
Publication statusPublished - Jan 1 2017

Keywords

  • antibacterials
  • Carbonic anhydrase
  • inhibitor
  • sulfonamide
  • Vibrio cholerae

ASJC Scopus subject areas

  • Pharmacology
  • Drug Discovery

Fingerprint Dive into the research topics of 'Inhibition of the α-carbonic anhydrase from Vibrio cholerae with amides and sulfonamides incorporating imidazole moieties'. Together they form a unique fingerprint.

  • Cite this

    De Vita, D., Angeli, A., Pandolfi, F., Bortolami, M., Costi, R., Di Santo, R., Suffredini, E., Ceruso, M., Del Prete, S., Capasso, C., Scipione, L., & Supuran, C. T. (2017). Inhibition of the α-carbonic anhydrase from Vibrio cholerae with amides and sulfonamides incorporating imidazole moieties. Journal of Enzyme Inhibition and Medicinal Chemistry, 32(1), 798-804. https://doi.org/10.1080/14756366.2017.1327522