Third-Party Tested ≥98% HPLC Purity — USA Shipped

Thymic & Immune Research Guide

PNC-27: Mechanism, Handling & Research Guide

Also known as: PNC27, PNC-27 peptide, p53-HDM2 peptide, p53 peptide, anticancer p53-penetratin peptide, p53-MDM2 binding peptide

Key Facts

PNC-27 is a thymic & immune research peptide (C188H293N53O44S, MW 4031.7 g/mol). p53-derived peptide for selective cancer cell targeting research. It is supplied as a lyophilized powder for laboratory and in-vitro research use only — not for human consumption.

Classification Chimeric p53(12-26)-derived HDM-2/MDM2-binding membranolytic peptide (preclinical anticancer research tool)
Molecular Formula C188H293N53O44S
Molecular Weight 4031.7 g/mol
Research Half-Life Not well characterized; no validated pharmacokinetic half-life is reported (early preclinical, largely in vitro compound).
Form Lyophilized powder
Research Category Thymic & Immune

What is PNC-27?

PNC-27 is a synthetic 32-amino acid peptide containing an HDM-2 binding domain derived from the p53 tumor suppressor protein, linked to a cell-penetrating leader sequence. PNC-27 selectively targets cancer cells by binding to HDM-2 (human double minute 2) protein that is aberrantly expressed on the surface membrane of transformed cells but not on normal cells. Upon binding, PNC-27 induces rapid membrane pore formation and necrosis specifically in HDM-2-overexpressing cells, a mechanism distinct from conventional apoptosis-based chemotherapy. Research by Kanovsky et al. (2001) published in Proceedings of the National Academy of Sciences demonstrated that PNC-27 killed a broad spectrum of cancer cell lines, including breast (MCF-7), pancreatic (MIA PaCa-2), and leukemia cells, while leaving normal fibroblasts and epithelial cells completely unharmed at the same concentrations. Subsequent work by Sookraj et al. in Cancer Biology & Therapy showed that PNC-27 induced rapid membranolysis within 10-15 minutes of contact with HDM-2-positive cancer cells, confirming a necrotic rather than apoptotic mechanism. Studies in ovarian cancer models demonstrated efficacy against platinum-resistant cell lines. Compared to conventional chemotherapeutic agents, PNC-27 offers a fundamentally different selectivity mechanism -- targeting a specific membrane protein (HDM-2) rather than general markers of cell division. This distinguishes it from both traditional cytotoxic agents and newer targeted therapies like tyrosine kinase inhibitors. The peptide HAMLET (human alpha-lactalbumin made lethal to tumor cells) shares the concept of selective cancer cell membrane disruption but operates through different binding targets. Store lyophilized PNC-27 at -20°C. Reconstitute with bacteriostatic water and store at 2-8°C, using within 3 weeks. PNC-27 is researched by cancer biologists, oncology researchers investigating selective antitumor agents, and cell membrane biophysicists studying peptide-membrane interactions.

PNC-27 Research Applications

In published and preclinical research, PNC-27 has been studied across the following areas:

  • Selective cancer cell targeting
  • HDM-2 binding and membrane pore formation
  • Breast and pancreatic cancer models
  • Leukemia and ovarian cancer research

PNC-27 in Research: Study Context

Published preclinical literature characterizes PNC-27 as a peptide combining an HDM-2 (MDM2)-binding domain corresponding to p53 residues ~12-26 with a membrane-penetrating (penetratin-derived) sequence. In vitro studies report that it binds HDM-2 present in the plasma membrane of various cancer cell lines and induces membrane-pore formation and necrosis, with comparatively little effect on untransformed cells that lack appreciable membrane HDM-2 (Sarafraz-Yazdi/Kanovsky et al., PNAS 2010; Davitt et al., Ann Clin Lab Sci 2014). This compound is for laboratory research use only and is NOT FDA-approved; evidence is early-stage and predominantly cell-culture based, with no established in vivo efficacy/safety profile or human. For laboratory handling, the lyophilized powder is reconstituted with bacteriostatic water to a defined concentration (e.g., 10 mg in 1 mL = 10 mg/mL); investigators should reference the primary literature and document the lot-specific COA.

PNC-27 — Frequently Asked Questions

What is the proposed mechanism of PNC-27 in research models?
Published in vitro work proposes that PNC-27 binds HDM-2 (MDM2) located in the plasma membrane of cancer cells and forms transmembrane pores, causing membranolysis/necrosis rather than classical apoptosis. The reported selectivity is attributed to membrane-associated HDM-2 being detected in transformed cells but not in the membranes of the normal cell lines tested. This is a mechanistic research finding, not a clinical claim.
How does PNC-27's mechanism differ from apoptosis-based agents in the literature?
Reported studies describe rapid membrane disruption and LDH release (a necrosis readout) within minutes in HDM-2-membrane-positive cells, which the authors distinguish from the slower, caspase-driven apoptosis seen with many cytotoxic agents. The distinction is drawn from in vitro assays and should not be read as a validated therapeutic mechanism in vivo.
What is the maturity of the PNC-27 evidence base?
The evidence is early and largely in vitro, with limited in vivo work; pharmacokinetics, systemic delivery, and selectivity in whole organisms remain open questions in the literature. PNC-27 is not FDA-approved, has no established human concentration, and is intended only for laboratory research. It is not a cancer treatment.
Is PNC-27 legal to buy for research?
PNC-27 is sold in the United States as a research chemical for laboratory and in-vitro use only. It is not approved by the FDA for human use and is not sold for human consumption. Researchers are responsible for compliance with all applicable federal, state, and institutional regulations.
Does PNC-27 come with a Certificate of Analysis?
Yes. Every batch of PNC-27 from Elyte Peptides ships with a third-party Certificate of Analysis (COA) documenting identity and HPLC purity (≥98%), so research results can be traced to a verified lot.
What is PNC-27 and how does it work?
PNC-27 is a synthetic peptide containing an HDM-2 (human double minute-2) binding domain fused to a membranolytic sequence. It works by selectively binding to HDM-2 protein, which is overexpressed on the surface of cancer cells but not normal cells. Upon binding, PNC-27's membranolytic domain forms pores in the cancer cell membrane, leading to selective cytotoxicity. Normal cells, which express HDM-2 intracellularly rather than on their surface, are not affected.
What research has been done on PNC-27?
Research published in Cancer Research and the International Journal of Cancer demonstrated PNC-27's selective toxicity to cancer cells expressing surface HDM-2 while sparing normal cells. Studies showed efficacy against breast cancer (MCF-7), pancreatic cancer (MIA PaCa-2), leukemia, and ovarian cancer cell lines in vitro. Mechanism studies confirmed that PNC-27 forms transmembrane pores specifically in cancer cell membranes through HDM-2 binding-dependent interactions.
How does PNC-27 compare to conventional chemotherapy approaches?
Unlike conventional chemotherapy, which targets rapidly dividing cells regardless of whether they are cancerous or healthy, PNC-27's selectivity depends on surface HDM-2 expression — a feature specific to cancer cells. This selectivity has shown minimal cytotoxicity to normal cells in in-vitro studies. However, PNC-27 research is still preclinical and its in-vivo efficacy, pharmacokinetics, and delivery challenges are active areas of investigation.

Research References

  1. Sarafraz-Yazdi E, Bowne WB, Adler V, et al. Anticancer peptide PNC-27 adopts an HDM-2-binding conformation and kills cancer cells by binding to HDM-2 in their membranes. Proc Natl Acad Sci USA. 2010.
  2. Davitt K, Babcock BD, Fenelus M, et al. The anti-cancer peptide, PNC-27, induces tumor cell necrosis of a poorly differentiated non-solid tissue human leukemia cell line that depends on expression of HDM-2 in the plasma membrane of these cells. Ann Clin Lab Sci. 2014.