PNC-27
A synthetic peptide containing an HDM2-binding domain and a membrane-penetrating sequence, studied for selective cytotoxicity against cancer cells expressing surface-bound HDM2.
This name primarily lives in the research market and should not be read like an approved pharmaceutical product.
This profile is grouped by its dominant research and market lane, not by vendor shelf placement.
No major aliases are tracked for this profile yet.
No FDA label signal · 0 trials · 23 PubMed results
Current evidence for PNC-27 is limited to laboratory or animal studies — there are no name-matched human trials with reported results. Any claims about effects in people are not yet backed by clinical data.
PNC-27 has no clinical trials that name it and 23 PubMed-indexed publications and is not FDA-approved. Current evidence is preclinical or mechanistic.
Re-checked nightly against the registries — tracked since 2026-07-09. No band changes yet.
Grades evidence strength, not efficacy or safety. Research-use context; not medical advice. Graded 2026-07-13 from PubMed, ClinicalTrials.gov, ISRCTN, openFDA, Health Canada, and OpenAlex — computed deterministically and refreshed nightly, with a retraction check. How we grade →
What is PNC-27?
PNC-27 is a synthetic peptide composed of an HDM2 (human double minute 2) binding domain fused to a cell-penetrating leader sequence. It was designed to selectively kill cancer cells by targeting an unusual feature: many transformed cells express HDM2 (also called MDM2) on their outer membrane surface, while normal cells keep HDM2 intracellular.
How it works
- Surface HDM2 targeting — normal cells express HDM2 exclusively in the cytoplasm/nucleus where it regulates p53 degradation. Many cancer cell lines aberrantly express HDM2 on the outer cell membrane (Puca et al., International Journal of Oncology, 2008)
- Membrane disruption — PNC-27 binds to surface HDM2 and creates pore-like structures in the cancer cell membrane, leading to necrosis rather than classical apoptosis (Bowne et al., Annals of Surgical Oncology, 2008)
- Selectivity — because normal cells do not express HDM2 on their surface, PNC-27 showed no cytotoxicity against non-transformed cell lines in culture (Kanovsky et al., International Journal of Molecular Medicine, 2003)
Research status
Published data comes from a small group of collaborating researchers:
- Kanovsky et al. (2003) first reported that PNC-27 selectively kills cancer cells expressing surface HDM2 (International Journal of Molecular Medicine, 11(3):285–291)
- Bowne et al. (2008) showed PNC-27 induced rapid membrane lysis in pancreatic cancer cells (Annals of Surgical Oncology, 15(12):3583–3592)
- Puca et al. (2008) characterized the surface HDM2 expression pattern across multiple cancer cell lines (International Journal of Oncology, 33(4):765–770)
No clinical trials have been registered. All studies are in vitro or in small animal models. The selective cytotoxicity has not been demonstrated in human clinical settings.
Key considerations
- The mechanism is scientifically interesting but the evidence base is narrow — primarily from one research collaboration
- Cancer peptide research has a long history of preclinical promise that does not translate clinically
- Available from a limited number of research vendors, often at high prices due to synthesis complexity
- Self-administration of research-grade anticancer peptides outside a clinical trial context carries significant safety unknowns