Structure-based design of novel human Pin1 inhibitors (II)

Bioorg Med Chem Lett. 2010 Apr 1;20(7):2210-4. doi: 10.1016/j.bmcl.2010.02.033. Epub 2010 Feb 14.

Abstract

Following the discovery of a novel series of phosphate-containing small molecular Pin1 inhibitors, the drug design strategy shifted to replacement of the phosphate group with an isostere with potential better pharmaceutical properties. The initial loss in potency of carboxylate analogs was likely due to weaker charge-charge interactions in the putative phosphate binding pocket and was subsequently recovered by structure-based optimization of ligand-protein interactions in the proline binding site, leading to the discovery of a sub-micromolar non-phosphate small molecular Pin1 inhibitor.

MeSH terms

  • Binding Sites
  • Crystallography, X-Ray
  • Drug Design
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / pharmacology*
  • Humans
  • Models, Molecular
  • NIMA-Interacting Peptidylprolyl Isomerase
  • Peptidylprolyl Isomerase / antagonists & inhibitors*
  • Peptidylprolyl Isomerase / chemistry
  • Peptidylprolyl Isomerase / metabolism*
  • Protein Binding
  • Structure-Activity Relationship

Substances

  • Enzyme Inhibitors
  • NIMA-Interacting Peptidylprolyl Isomerase
  • PIN1 protein, human
  • Peptidylprolyl Isomerase