Identification and Structure-Activity Relationship Studies of Small-Molecule Inhibitors of the Methyllysine Reader Protein Spindlin1

ChemMedChem. 2016 Oct 19;11(20):2327-2338. doi: 10.1002/cmdc.201600362. Epub 2016 Sep 16.

Abstract

The methyllysine reader protein Spindlin1 has been implicated in the tumorigenesis of several types of cancer and may be an attractive novel therapeutic target. Small-molecule inhibitors of Spindlin1 should be valuable as chemical probes as well as potential new therapeutics. We applied an iterative virtual screening campaign, encompassing structure- and ligand-based approaches, to identify potential Spindlin1 inhibitors from databases of commercially available compounds. Our in silico studies coupled with in vitro testing were successful in identifying novel Spindlin1 inhibitors. Several 4-aminoquinazoline and quinazolinethione derivatives were among the active hit compounds, which indicated that these scaffolds represent promising lead structures for the development of Spindlin1 inhibitors. Subsequent lead optimization studies were hence carried out, and numerous derivatives of both lead scaffolds were synthesized. This resulted in the discovery of novel inhibitors of Spindlin1 and helped explore the structure-activity relationships of these inhibitor series.

Keywords: AlphaLISA assay; Spindlin1; lead optimization; methyllysine readers; virtual screening.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Cycle Proteins / antagonists & inhibitors*
  • Dose-Response Relationship, Drug
  • Humans
  • Microtubule-Associated Proteins / antagonists & inhibitors*
  • Molecular Structure
  • Phosphoproteins / antagonists & inhibitors*
  • Small Molecule Libraries / chemical synthesis
  • Small Molecule Libraries / chemistry
  • Small Molecule Libraries / pharmacology*
  • Structure-Activity Relationship

Substances

  • Cell Cycle Proteins
  • Microtubule-Associated Proteins
  • Phosphoproteins
  • Small Molecule Libraries
  • spindlin