A new class of glycogen phosphorylase inhibitors

Bioorg Med Chem Lett. 2003 Nov 17;13(22):4125-8. doi: 10.1016/j.bmcl.2003.08.046.

Abstract

A new class of diacid analogues that binds at the AMP site not only are very potent but have approximately 10-fold selectivity in liver versus muscle glycogen phosphorylase (GP) in the in vitro assay. The synthesis, structure, and in vitro and in vivo biological evaluation of these liver selective glycogen phosphorylase inhibitors are discussed.

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Enzyme Inhibitors / chemical synthesis*
  • Enzyme Inhibitors / pharmacology*
  • Glycogen Phosphorylase / antagonists & inhibitors*
  • Glycogen Phosphorylase / chemistry
  • Kinetics
  • Liver / enzymology
  • Mice
  • Models, Molecular
  • Molecular Conformation
  • Naphthols / chemical synthesis*
  • Naphthols / pharmacology
  • Protein Conformation
  • Rats
  • Structure-Activity Relationship

Substances

  • Enzyme Inhibitors
  • Naphthols
  • Adenosine Triphosphate
  • Glycogen Phosphorylase