Inhibition of Hsp90 with synthetic macrolactones: synthesis and structural and biological evaluation of ring and conformational analogs of radicicol

Chem Biol. 2006 Nov;13(11):1203-15. doi: 10.1016/j.chembiol.2006.09.015.

Abstract

A series of benzo-macrolactones of varying ring size and conformation has been prepared by chemical synthesis and evaluated by structural and biological techniques. Thus, 12- to 16-membered lactones were obtained by concise routes, involving ring-closing metathesis as a key step. In enzyme assays, the 13-, 15-, and 16-membered analogs are good inhibitors, suggesting that they can adopt the required conformation to fit in the ATP-binding site. This was confirmed by cocrystallization of 13-, 14-, and 15-membered lactones with the N-terminal domain of yeast Hsp90, showing that they bind similarly to the "natural" 14-membered radicicol. The most active compounds in the ATPase assays also showed the greatest growth-inhibitory potency in HCT116 human colon cancer cells and the established molecular signature of Hsp90 inhibition, i.e., depletion of client proteins with upregulation of Hsp70.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Cell Line, Tumor
  • Cell Proliferation / drug effects
  • HSP90 Heat-Shock Proteins / antagonists & inhibitors*
  • Humans
  • Lactones / chemical synthesis*
  • Lactones / chemistry
  • Lactones / pharmacology*
  • Macrolides / chemistry*
  • Macrolides / pharmacology
  • Molecular Structure
  • Protein Conformation

Substances

  • HSP90 Heat-Shock Proteins
  • Lactones
  • Macrolides
  • Adenosine Triphosphatases
  • monorden

Associated data

  • PDB/21WX
  • PDB/2CGF
  • PDB/2IWS
  • PDB/2IWU