Docking and quantitative structure-activity relationship of oxadiazole derivates as inhibitors of GSK3β

Mol Divers. 2014 Feb;18(1):149-59. doi: 10.1007/s11030-013-9483-5. Epub 2013 Oct 1.

Abstract

The binding modes of 42 oxadiazole derivates inside glycogen synthase kinase 3 beta (GSK3β were determined using docking experiments; thus, the preferred active conformations of these inhibitors are proposed. We found that these compounds adopt a scorpion-shaped conformation and they accept a hydrogen bond (HB) from the residue Val135 of the GSK3β ATP-binding site hinge region. In addition, quantitative structure-activity relationship (QSAR) models were constructed to explain the trend of the GSK3β inhibitory activities for the studied compounds. In a first approach, three-dimensional (3D) vectors were calculated using docking conformations and, by using multiple-linear regression, we assessed that GETAWAY vectors were able to describe the reported biological activities. In other QSAR approach, SMILES-based optimal descriptors were calculated. The best model included three-SMILES elements SSSβ leading to the identification of key molecular features that contribute to a high GSK3β inhibitory activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Computer Simulation
  • Glycogen Synthase Kinase 3 / antagonists & inhibitors*
  • Glycogen Synthase Kinase 3 / chemistry
  • Glycogen Synthase Kinase 3 / metabolism*
  • Glycogen Synthase Kinase 3 beta
  • Molecular Docking Simulation*
  • Oxadiazoles / chemistry*
  • Oxadiazoles / metabolism
  • Oxadiazoles / pharmacology*
  • Protein Conformation
  • Protein Kinase Inhibitors / chemistry
  • Protein Kinase Inhibitors / metabolism
  • Protein Kinase Inhibitors / pharmacology
  • Quantitative Structure-Activity Relationship*

Substances

  • Oxadiazoles
  • Protein Kinase Inhibitors
  • Glycogen Synthase Kinase 3 beta
  • Glycogen Synthase Kinase 3