Inhibition of α-, β-, γ-, and δ-carbonic anhydrases from bacteria and diatoms with N'-aryl-N-hydroxy-ureas

J Enzyme Inhib Med Chem. 2018 Dec;33(1):1194-1198. doi: 10.1080/14756366.2018.1490733.

Abstract

The inhibition of α-, β-, γ-, and δ-class carbonic anhydrases (CAs, EC 4.2.1.1) from bacteria (Vibrio cholerae and Porphyromonas gingivalis) and diatoms (Thalassiosira weissflogii) with a panel of N'-aryl-N-hydroxy-ureas is reported. The α-/β-CAs from V. cholerae (VchCAα and VchCAβ) were effectively inhibited by some of these derivatives, with KIs in the range of 97.5 nM - 7.26 µM and 52.5 nM - 1.81 µM, respectively, whereas the γ-class enzyme VchCAγ was less sensitive to inhibition (KIs of 4.75 - 8.87 µM). The β-CA from the pathogenic bacterium Porphyromonas gingivalis (PgiCAβ) was not inhibited by these compounds (KIs > 10 µM) whereas the corresponding γ-class enzyme (PgiCAγ) was effectively inhibited (KIs of 59.8 nM - 6.42 µM). The δ-CA from the diatom Thalassiosira weissflogii (TweCAδ) showed effective inhibition with these derivatives (KIs of 33.3 nM - 8.74 µM). As most of these N-hydroxyureas are also ineffective as inhibitors of the human (h) widespread isoforms hCA I and II (KIs > 10 µM), this class of derivatives may lead to the development of CA inhibitors selective for bacterial/diatom enzymes over their human counterparts and thus to anti-infectives or agents with environmental applications.

Keywords: Carbonic anhydrase; Plasmodium falciparum; activators; metalloenzymes; protozoa.

MeSH terms

  • Carbonic Anhydrase Inhibitors / isolation & purification
  • Carbonic Anhydrase Inhibitors / pharmacology*
  • Diatoms / enzymology*
  • Humans
  • Hydroxyurea / chemistry
  • Hydroxyurea / pharmacology*
  • Isoenzymes / antagonists & inhibitors*
  • Porphyromonas gingivalis / enzymology*
  • Vibrio cholerae / enzymology*

Substances

  • Carbonic Anhydrase Inhibitors
  • Isoenzymes
  • Hydroxyurea

Grants and funding

This research was financed in part by a Distinguished Scientists Fellowship Programme (DSFP) or King Saud University, Riyadh, Saudi Arabia.