Cell-permeable beta-peptide inhibitors of p53/hDM2 complexation

Chembiochem. 2009 Apr 17;10(6):990-3. doi: 10.1002/cbic.200900049.

Abstract

Look at what the cat(ionic motif) dragged in! We report a general strategy to increase the cell permeability of beta(3)-peptides. Introduction of a minimal cationic motif within the folded structure of a high-affinity beta(3)-peptide ligand for hDM2 led to molecules with high 3(14)-helical structure, high hDM2 affinity and sufficient cell permeability to upregulate p53-dependent genes in live mammalian cells. Minimally cationic beta(3)-peptides represent the critical first step towards a class of protease-resistant peptidomimetics that might modulate intracellular biological pathways.

Publication types

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

MeSH terms

  • Cell Membrane Permeability*
  • Circular Dichroism
  • HCT116 Cells
  • Humans
  • Microscopy, Confocal
  • Peptides / metabolism*
  • Peptides / pharmacology*
  • Protein Binding / drug effects
  • RNA-Binding Proteins / metabolism*
  • Tumor Suppressor Protein p53 / metabolism*

Substances

  • CNBP protein, human
  • Peptides
  • RNA-Binding Proteins
  • Tumor Suppressor Protein p53