Modulation of human estrogen receptor α activity by multivalent estradiol-peptidomimetic conjugates

Mol Biosyst. 2011 Feb;7(2):337-45. doi: 10.1039/c0mb00189a. Epub 2011 Jan 7.

Abstract

Estradiol-peptidomimetic conjugates (EPCs) are linear, sequence-specific peptoid oligomers that site-specifically display multiple copies of 17β-estradiol (E2), a ligand for the human estrogen receptor α (hERα). We evaluate the ability of multivalent EPCs to activate hERα-mediated transcription. EPCs activated the hERα in both a length- and valence-dependent manner, with the highest levels of activation generated by divalent peptoid 6-mers, divalent 18-mers, and trivalent 9-mers. Hexavalent EPCs did not activate hERα, but instead blocked E2-mediated hERα activation. The physicochemical features of EPCs can be precisely tuned, which may allow the generation of a library of chemical tools for modulating specific effects of estrogens.

Publication types

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

MeSH terms

  • Cell Line
  • Cell Membrane Permeability
  • Estradiol / chemistry
  • Estradiol / pharmacology*
  • Estrogen Receptor alpha / drug effects*
  • Estrogen Receptor alpha / metabolism
  • Estrogen Receptor alpha / physiology
  • Fluorescent Dyes / chemical synthesis
  • Humans
  • Hydrolysis
  • Molecular Mimicry*
  • Peptides / chemistry
  • Peptides / pharmacology*
  • Transcription, Genetic / physiology

Substances

  • Estrogen Receptor alpha
  • Fluorescent Dyes
  • Peptides
  • Estradiol