PNC-27 Research Guide: HDM-2 Binding Anticancer Peptide
PNC-27 is a chimeric peptide that selectively lyses tumor cells expressing membrane-bound HDM-2 while sparing normal cells.
What is PNC-27?
PNC-27 is a chimeric 32-amino-acid peptide constructed by fusing residues 12–26 of the p53 tumor-suppressor protein (the HDM-2 binding region) with a membrane-penetrating leader derived from Antennapedia. It was developed by Michael and Josephson at NYU School of Medicine.
Mechanism of action
Cancer cells frequently express HDM-2 on the plasma membrane — a hallmark absent in normal tissue. PNC-27 binds this membrane HDM-2, oligomerizes to form transmembrane pores, and induces rapid osmotic necrosis. The mechanism is independent of p53 status, making it relevant to tumors with p53 mutations.
Sourcing & purity
Research-grade material should be ≥99% pure by HPLC with peptide content confirmed via mass spectrometry. Redline Bio material ships with batch documentation; independent third-party COAs are published on the lab reports page as testing returns.
Compliance reminder
Sold and distributed for laboratory research use only. Not approved by the FDA for human consumption, diagnosis, treatment, or cure of any disease. Researchers are responsible for compliance with all applicable institutional, state, and federal regulations.
Frequently asked questions
What is PNC-27?
PNC-27 is a 32-residue peptide combining the HDM-2 binding domain of p53 (residues 12–26) with a transmembrane-penetrating leader sequence. It is one of the most-studied p53-derived anticancer research peptides.
Mechanism?
PNC-27 binds HDM-2 that is aberrantly expressed on the plasma membrane of tumor cells (but not normal cells). Binding induces pore formation and rapid necrotic lysis — a mechanism distinct from apoptosis and independent of p53 status.
Tumor selectivity?
Selectivity derives entirely from the presence of membrane HDM-2 on cancer cells. Normal cells sequester HDM-2 intracellularly and are not lysed in published in vitro studies.