α-D-mannose derivatives as models designed for selective inhibition of Golgi α-mannosidase II

Eur J Med Chem. 2011 Mar;46(3):944-52. doi: 10.1016/j.ejmech.2011.01.012. Epub 2011 Jan 15.

Abstract

Human Golgi α-mannosidase II (hGM) is a pharmaceutical target for the design of inhibitors with anti-tumor activity. Nanomolar inhibitors of hGM exhibit unwanted co-inhibition of the human lysosomal α-mannosidase (hLM). Hence, improving specificity of the inhibitors directed toward hGM is desired in order to use them in cancer chemotherapy. We report on the rapid synthesis of D-mannose derivatives having one of the RS-, R(SO)- or R(SO(2))- groups at the α-anomeric position. Inhibitory properties of thirteen synthesized α-D-mannopyranosides were tested against the recombinant enzyme Drosophila melanogaster homolog of hGM (dGMIIb) and hLM (dLM408). Derivatives with the sulfonyl [R(SO(2))-] group exhibited inhibitory activities at the mM level toward both dGMIIb (IC(50) = 1.5-2.5 mM) and dLM408 (IC(50) = 1.0-2.0 mM). Among synthesized, only the benzylsulfonyl derivative showed selectivity toward dGMIIb. Its inhibitory activity was explained based on structural analysis of the built 3-D complexes of the enzyme with the docked compounds.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / pharmacology*
  • Humans
  • Inhibitory Concentration 50
  • Mannose / analogs & derivatives*
  • Mannose / pharmacology*
  • Mannosidases / antagonists & inhibitors*
  • Mannosidases / metabolism
  • Models, Molecular
  • Protein Binding
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / pharmacology
  • Sulfur Compounds / chemistry
  • Sulfur Compounds / pharmacology
  • alpha-Mannosidase / antagonists & inhibitors*
  • alpha-Mannosidase / metabolism

Substances

  • Enzyme Inhibitors
  • Recombinant Proteins
  • Sulfur Compounds
  • Mannosidases
  • mannosyl-oligosaccharide 1,3 - 1,6-alpha-mannosidase
  • alpha-Mannosidase
  • Mannose