Inhibition of hypoxia inducible factor 1-transcription coactivator interaction by a hydrogen bond surrogate alpha-helix

J Am Chem Soc. 2010 Jan 27;132(3):941-3. doi: 10.1021/ja9082864.

Abstract

Designed ligands that inhibit hypoxia-inducible gene expression could offer new tools for genomic research and, potentially, drug discovery efforts for the treatment of neovascularization in cancers. We report a stabilized alpha-helix designed to target the binding interface between the C-terminal transactivation domain (C-TAD) of hypoxia-inducible factor 1alpha (HIF-1alpha) and cysteine-histidine rich region (CH1) of transcriptional coactivator CBP/p300. The synthetic helix disrupts the structure and function of this complex, resulting in a rapid downregulation of two hypoxia-inducible genes (VEGF and GLUT1) in cell culture.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Cell Survival / drug effects
  • Cells, Cultured
  • Disulfides / pharmacology*
  • HeLa Cells
  • Humans
  • Hydrogen Bonding
  • Hypoxia-Inducible Factor 1 / antagonists & inhibitors*
  • Hypoxia-Inducible Factor 1 / chemistry
  • Hypoxia-Inducible Factor 1 / metabolism
  • Indole Alkaloids / pharmacology*
  • Protein Structure, Secondary
  • Trans-Activators / antagonists & inhibitors*
  • Trans-Activators / chemistry
  • Trans-Activators / metabolism

Substances

  • Disulfides
  • Hypoxia-Inducible Factor 1
  • Indole Alkaloids
  • Trans-Activators
  • chetomin