Adenine derived inhibitors of the molecular chaperone HSP90-SAR explained through multiple X-ray structures

Bioorg Med Chem Lett. 2004 Jan 19;14(2):325-8. doi: 10.1016/j.bmcl.2003.11.011.

Abstract

Multiple co-crystal structures of an adenine-based series of inhibitors bound to the molecular chaperone Hsp90 have been determined. These structures explain the observed SAR for previously described compounds and new compounds, which possess up to 8-fold improved potency against the isolated enzyme. Anti-tumour cell potency and mechanism of action data is also described for the most potent compounds. These data should enable the design of more potent Hsp90 inhibitors.

MeSH terms

  • Adenine / analogs & derivatives*
  • Adenine / pharmacology*
  • Cell Line, Tumor
  • Crystallography, X-Ray / methods
  • HSP90 Heat-Shock Proteins / antagonists & inhibitors*
  • HSP90 Heat-Shock Proteins / metabolism
  • Humans
  • Molecular Chaperones / antagonists & inhibitors
  • Molecular Chaperones / metabolism
  • Structure-Activity Relationship

Substances

  • HSP90 Heat-Shock Proteins
  • Molecular Chaperones
  • Adenine