LXXLL peptide mimetics as inhibitors of the interaction of vitamin D receptor with coactivators

Bioorg Med Chem Lett. 2010 Mar 1;20(5):1712-7. doi: 10.1016/j.bmcl.2010.01.079. Epub 2010 Jan 21.

Abstract

Suppression of vitamin D receptor (VDR)-mediated transcription is expected be of therapeutic value in Paget's disease. Once an agonist activates VDR, recruitment of additional coactivator proteins is essential for transcription. Neither non-secosteroidal VDR antagonists nor non-peptide coactivator binding inhibitors for VDR have been reported so far. Based on the X-ray structure of VDR and an LXXLL-containing peptide fragment of the coactivator (where L is leucine and X is any amino acid), which adopts a partially alpha-helical conformation, benzodiazepine molecules were rationally designed as non-peptide coactivator mimetics. TR-FRET assay showed that the synthesized compounds inhibited the interaction between VDR and a coactivator peptide fragment. Compound 2 showed an IC(50) of 20microM. Compound 2 also inhibited VDR-mediated transcription, and this activity was independent of the concentration of co-existing agonist. Furthermore, compound 2 did not inhibit estrogen receptor alpha-mediated transcription, indicating that it is not a non-selective inhibitor of other nuclear receptors.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Benzodiazepines / chemistry
  • Binding Sites
  • Crystallography, X-Ray
  • Fluorescence Resonance Energy Transfer
  • Humans
  • Osteitis Deformans / drug therapy
  • Peptides / chemistry*
  • Peptides / therapeutic use
  • Protein Binding
  • Receptors, Calcitriol / antagonists & inhibitors
  • Receptors, Calcitriol / metabolism*
  • Receptors, Cytoplasmic and Nuclear / metabolism
  • Transcriptional Activation

Substances

  • Peptides
  • Receptors, Calcitriol
  • Receptors, Cytoplasmic and Nuclear
  • Benzodiazepines