A highly potent and cellularly active beta-peptidic inhibitor of the p53/hDM2 interaction

Chembiochem. 2009 Apr 17;10(6):994-8. doi: 10.1002/cbic.200800803.

Abstract

New and improved: The incorporation of a 6-chlorotryptophan (6-Cl-Trp) into a beta-peptide (M)-3(14) helix leads to a high-affinity hDM2 inhibitor, as demonstrated by fluorescence fluctuation analysis at single molecule resolution. When conjugated to penetratin, the newly derived hDM2 binder specifically inhibits tumour cell growth in vitro.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Biomimetic Materials / chemical synthesis
  • Biomimetic Materials / chemistry
  • Biomimetic Materials / metabolism
  • Biomimetic Materials / pharmacology
  • Cell Line, Tumor
  • Drug Design
  • Humans
  • Ligands
  • Mice
  • Models, Molecular
  • Peptides / chemical synthesis
  • Peptides / chemistry
  • Peptides / metabolism*
  • Peptides / pharmacology*
  • Protein Binding / drug effects
  • Protein Structure, Secondary
  • RNA-Binding Proteins / metabolism*
  • Tumor Suppressor Protein p53 / chemistry
  • Tumor Suppressor Protein p53 / metabolism*

Substances

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