Evaluation of novel hyphodermin derivatives as glycogen phosphorylase a inhibitors

Bioorg Med Chem. 2008 Jun 1;16(11):6172-8. doi: 10.1016/j.bmc.2008.04.047. Epub 2008 Apr 25.

Abstract

The lipophilicity, permeability, solubility, polar surface area and 'rule-of-five' properties were assessed, using QikProp v2.5 (Schrödinger, Inc.) and ALOGPS 2.1 calculations, for 25 Hyphodermin derivatives. These compounds obeyed the 'rule-of-five', and the calculated physicochemical values were generally within desired limits. All compounds were tested against Glycogen Phosphorylase a (GPa). Four phenyl and benzyl substituted 2-oxo-hexahydro and tetrahydrobenzo[cd]indole carboxylic acids were identified as novel inhibitors of GPa with estimated IC(50) values in the range 0.8-1.3mM. Molecular modelling of these novel inhibitors was used to obtain the main structural features of this class of molecule for future structure-activity relationship studies.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allosteric Regulation
  • Animals
  • Basidiomycota / chemistry
  • Basidiomycota / metabolism
  • Cell Membrane Permeability
  • Furans / chemistry
  • Furans / pharmacology*
  • Glycogen Phosphorylase, Muscle Form / antagonists & inhibitors*
  • Glycogen Phosphorylase, Muscle Form / chemistry
  • Hydrogen Bonding
  • Isoenzymes / antagonists & inhibitors
  • Isoenzymes / chemistry
  • Lipids / chemistry
  • Models, Molecular
  • Naphthalenes / chemistry
  • Naphthalenes / pharmacology*
  • Rabbits
  • Solubility
  • Surface Properties

Substances

  • Furans
  • Isoenzymes
  • Lipids
  • Naphthalenes
  • hyphodermin A
  • hyphodermin B
  • hyphodermin D
  • Glycogen Phosphorylase, Muscle Form