Synthesis and biochemical evaluation of guanidino-alkyl-ribitol derivatives as nucleoside hydrolase inhibitors

Eur J Med Chem. 2008 Feb;43(2):315-26. doi: 10.1016/j.ejmech.2007.03.027. Epub 2007 Apr 10.

Abstract

Nucleoside hydrolase (NH) is a key enzyme in the purine salvage pathway. The purine specificity of the IAG-NH from Trypanosoma vivax is at least in part due to cation-pi-stacking interactions. Guanidinium ions can be involved in cation-pi-stacking interactions, therefore a series of guanidino-alkyl-ribitol derivatives were synthesized in order to examine the binding affinity of these compounds towards the target enzyme. The compounds show moderate to good inhibiting activity towards the IAG-NH from T. vivax.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Drug Evaluation, Preclinical
  • Enzyme Inhibitors / chemical synthesis*
  • Enzyme Inhibitors / pharmacology*
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • N-Glycosyl Hydrolases / antagonists & inhibitors*
  • N-Glycosyl Hydrolases / chemistry
  • Spectrometry, Mass, Electrospray Ionization
  • Trypanosoma vivax / enzymology

Substances

  • Enzyme Inhibitors
  • N-Glycosyl Hydrolases