PNC-27
Stocked in 5mg vials, 10mg vials at MontanaPep in Great Falls, Montana. Sold for laboratory research use only.
| Size | Catalog no. | Price per vial |
|---|---|---|
| 5mg vials | PC5 | $30 |
| 10mg vials | PC10 | $45 |
Classification
Chimeric anticancer research peptide; in vitro evidence concentrated in one research group
Structure and chemistry
PNC-27 is a 32-residue chimeric peptide with two covalently joined parts: residues 12-26 of p53, which form the HDM-2 (human MDM2) binding domain, attached to a membrane-residency peptide leader sequence derived from penetratin. A finding from the original work is important to the chemistry: neither piece works alone. The isolated p53 12-26 fragment, the leader sequence by itself, and even both peptides mixed together but not covalently linked all failed to induce tumour cell necrosis. The covalent linkage is required.
What the published research shows
The in vitro evidence is consistent and spans many cancer cell lines. The significant limitation is concentration of source: essentially the entire body of PNC-27 research comes from one collaborating group — Pincus, Michl, Bowne and colleagues at SUNY Downstate and Drexel — over roughly two decades, with an associated commercial entity. Independent replication by unaffiliated laboratories is the gap in this literature, and there are no human clinical trials.
Mechanism of action
The proposed mechanism is unusual and does not depend on p53 function. HDM-2, normally an intracellular protein, is reported to be mislocalized to the plasma membrane of cancer cells. PNC-27 binds that membrane-bound HDM-2, and the bound complexes assemble by random movement into oligomers and then into transmembrane pores, causing the cell to lose its contents and die by necrosis rather than apoptosis. Because the trigger is membrane HDM-2 rather than p53 signalling, the effect has been reported in p53-null cell lines. The peptide has also been reported to enter cancer cells and disrupt mitochondrial membranes.
Development history
Developed by Matthew R. Pincus, Josef Michl, Wilbur B. Bowne and colleagues, working primarily at SUNY Downstate Medical Center in Brooklyn with collaborators at Drexel University College of Medicine. A related peptide, PNC-28, was developed in parallel. Commercial development has been associated with NomoCan Pharmaceuticals.
Current regulatory status
PNC-27 is not approved by any regulator, has never been tested in a human clinical trial, and has not been placed on FDA’s bulk drug substances lists. It is a laboratory research compound. The selectivity claim — that it kills cancer cells but spares normal cells — rests on cell-culture comparisons and has not been evaluated in a clinical study.
Analytical testing
A 32-residue chimeric peptide is a demanding synthesis, and truncated or deletion sequences are a realistic impurity class. The covalent-linkage finding makes this consequential: a preparation containing free p53 12-26 fragment or free leader peptide would contain material that published work specifically showed to be inactive. Mass spectrometry against a certified reference standard is necessary to confirm the intact 32-residue chimera rather than its fragments.
Ordering from Great Falls
MontanaPep, also known as Montana Peptides, is an independently owned supplier based at 715 13th Ave S, Great Falls, Montana. Local pickup is available by arrangement, and we ship to research addresses across Montana including Billings, Missoula, Bozeman, Helena, Butte, Kalispell and Havre. Call (406) 799-0812 or email customerservice@montanapep.com.