Coupling of the antennapedia third helix to a potent antagonist of the p53/hdm2 protein-protein interaction.
The use of cell-membrane translocating sequences for intracellular delivery of peptides can be a powerful approach to validate drug discovery targets in cellular settings. To accomplish this, a protocol has been implemented to couple the antennapedia third helix (residues 43-58) to a potent antagonist of the p53/hdm2 protein-protein interaction without affecting its in vitro inhibitory activity.
García-Echeverría
C
C
Oncology Research, Novartis Pharma Inc., CH-4002, Basel, Switzerland. carlos.garcia-echeverria@pharma.novartis.com
Furet
P
P
Chène
P
P
D051943:Antennapedia Homeodomain Protein; D001667:Binding, Competitive / Q000187:drug effects; D018398:Homeodomain Proteins / Q000737:chemistry / Q000494:pharmacology*; D006801:Humans; D009687:Nuclear Proteins; D010446:Peptide Fragments / Q000494:pharmacology; D017433:Protein Structure, Secondary; D011518:Proto-Oncogene Proteins / Q000378:metabolism*; D051736:Proto-Oncogene Proteins c-mdm2; D014157:Transcription Factors; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism* / Q000502:physiology
D051943:Antennapedia Homeodomain Protein; D018398:Homeodomain Proteins; D009687:Nuclear Proteins; D010446:Peptide Fragments; D011518:Proto-Oncogene Proteins; D014157:Transcription Factors; D016159:Tumor Suppressor Protein p53; C497206:MDM2 protein, human; D051736:Proto-Oncogene Proteins c-mdm2