A potent transactivation domain mimic with activity in living cells

J Am Chem Soc. 2005 Jun 15;127(23):8254-5. doi: 10.1021/ja0515295.

Abstract

Transcriptional coactivator-binding peptoids were isolated from a large combinatorial library. One of these molecules is shown to function as a potent activation domain surrogate in mammalian cells. Up to a 900-fold increase in expression of a Gal4-responsive reporter gene is observed when a steroid conjugate of the peptoid is incubated with HeLa cells expressing a Gal4 DNA-binding domain (DBD)-glucocorticoid receptor ligand-binding domain (GRLBD) fusion protein.

Publication types

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

MeSH terms

  • Animals
  • Biomimetic Materials / chemistry
  • Biomimetic Materials / metabolism
  • CREB-Binding Protein
  • Cell Membrane Permeability
  • Combinatorial Chemistry Techniques
  • Dexamethasone / chemistry
  • Dexamethasone / metabolism
  • Humans
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / metabolism
  • Oligopeptides / chemistry*
  • Oligopeptides / metabolism
  • Protein Structure, Tertiary
  • Receptors, Glucocorticoid / agonists
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / metabolism
  • Trans-Activators / chemistry*
  • Trans-Activators / metabolism

Substances

  • Nuclear Proteins
  • Oligopeptides
  • Receptors, Glucocorticoid
  • Recombinant Fusion Proteins
  • Trans-Activators
  • Dexamethasone
  • CREB-Binding Protein
  • CREBBP protein, human