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a vial of PNC-27 10mg

PNC-27

Price range: $79.00 through $149.00

  • Contents: PNC-27 (32-amino acid chimeric p53-penetratin peptide)
  • Form: Lyophilized powder
  • Purity: >99%
Quantity Discount Price
1 - 3 - -
4 - 7 10% -
8 + 18% -
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Description

PNC-27 is a synthetic 32-amino acid chimeric peptide engineered by fusing residues 12-26 of the human p53 tumor suppressor protein with a membrane residency peptide (MRP) leader sequence derived from penetratin. The two domains are covalently linked and must remain joined for biological activity in experimental models: the p53 residues 12-26 segment targets HDM-2 (the human ortholog of MDM2), while the MRP leader sequence enables membrane interaction and pore formation after target engagement. PNC-27 is studied as a specialty research peptide tool for probing HDM-2 membrane biology and chimeric peptide architecture in oncology research models. It occupies a distinct mechanistic position from other cell-penetrating peptides such as FOXO4-DRI, which targets senescent cells through intranuclear p53 interaction rather than membrane-bound HDM-2.

Chemical Information

  • Chemical Name: PNC-27 (p53 residues 12-26 / penetratin MRP chimeric peptide)
  • Also Known As: PNC27; chimeric p53-penetratin peptide
  • Compound Class: Synthetic chimeric cell-penetrating peptide (bifunctional; HDM-2 targeting domain + membrane residency peptide)
  • Length: 32 amino acids
  • Domain 1: p53 residues 12-26 (HDM-2/MDM2 binding domain)
  • Domain 2: Membrane residency peptide (MRP; penetratin-derived leader sequence)
  • Architecture: Covalently linked bifunctional construct (both domains required for activity)
  • Primary Target: HDM-2 (human MDM2 ortholog) expressed on cancer cell plasma membranes
  • Cell Death Mechanism: Transmembrane pore formation causing necrosis (not apoptosis)
  • Production: Solid-phase peptide synthesis (SPPS)

Applications

  • HDM-2 membrane biology research. HDM-2 is aberrantly expressed on the plasma membranes of cancer-derived cell lines but not on normal untransformed cells. PNC-27 provides a defined molecular tool for studying membrane-associated HDM-2 interaction, localization, and its role in the membrane-directed necrosis mechanism
  • Chimeric bifunctional peptide architecture research.This27 requires covalent linkage of both domains for activity; neither the p53 12-26 segment alone, the MRP leader alone, nor both domains administered separately produce tumor cell killing in experimental models. Thiis architecture dependency makes PNC-27 a research model for studying how bifunctional chimeric peptides require structural integrity for membrane-targeted biological activity
  • Transmembrane pore formation studies. PNC-27 induces pore formation in cancer cell plasma membranes, documentable by transmission electron microscopy. Researchers studying how peptide-lipid bilayer interactions produce pore structures use PNC-27 as a defined experimental system with characterized pore formation kinetics
  • Necrosis versus apoptosis pathway research. PNC-27 induces cell necrosis rather than apoptosis, distinguishing its mechanism from most intracellular apoptosis-targeting approaches. This mechanistic distinction is relevant in models studying which cell death pathways are triggered by membrane disruption versus intracellular signaling
  • Mitochondrial membrane disruption research. In addition to plasma membrane pore formation, PNC-27 enters cancer cells and disrupts mitochondrial membranes. The dual membrane target makes it relevant in models examining how plasma membrane compromise leads to organelle dysfunction
  • HDM-2 selectivity mechanism research. Normal untransformed cells lacking plasma membrane HDM-2 expression are not susceptible to PNC-27-induced lysis; when HDM-2 is artificially transfected into normal cells, susceptibility is conferred. Researchers use this HDM-2 expression dependency to characterize the relationship between membrane protein expression patterns and peptide-mediated membrane targeting in cell culture models

Storage and Handling

Store lyophilized powder at -20C for long-term stability, or at 2-8C for short-term use. Protect from heat, moisture, and direct light. Reconstitute immediately before use and avoid repeated freeze-thaw cycles to preserve chimeric peptide integrity. Both functional domains must remain structurally intact for experimental activity. Suboptimal handling conditions that degrade either the HDM-2 binding domain or the MRP leader sequence will reduce or eliminate observed effects in cell-based assays.

Compliance Notice

PNC-27 is for laboratory research use only. They are not for human or veterinary use and carry no therapeutic, diagnostic, or clinical indication. FDA has not evaluated this product. By purchasing this product, the buyer confirms that they will follow appropriate institutional safety procedures and use it exclusively for controlled research.

Frequently Asked Questions

What is PNC-27 and how does its bifunctional architecture work?

PNC-27 is a 32-amino acid chimeric peptide combining p53 residues 12-26 with a membrane residency peptide (MRP) leader sequence through covalent linkage. The p53 segment binds HDM-2 expressed on cancer cell plasma membranes at the p53 binding site (HDM-2 residues 1-109). The MRP leader sequence enables membrane interaction and pore formation after HDM-2 engagement. Critically, both domains must be covalently linked: neither domain alone nor both domains administered as separate peptides produce tumor cell killing in experimental models. This architecture dependency is itself a research variable characterizing how chimeric bifunctional peptides require structural integrity for membrane-targeted activity.

Why does PNC-27 selectively affect cancer cell lines and not normal cells in research models?

The selectivity mechanism studied in published research is differential HDM-2 plasma membrane expression. Cancer-derived cell lines aberrantly express HDM-2 on their plasma membranes, providing the binding target that concentrates PNC-27 at the cell surface and enables pore formation. Normal untransformed cells do not express HDM-2 on their plasma membranes under standard conditions and are not susceptible to PNC-27-induced lysis. Researchers have confirmed this mechanism by transfecting HDM-2 expression constructs into normal cells, which then become susceptible to PNC-27 treatment. This expression-dependent selectivity is the primary research rationale for using PNC-27 as a tool for studying membrane-associated HDM-2 biology.

How does PNC-27 differ from FOXO4-DRI as a cell-penetrating research peptide?

Both PNC-27 and FOXO4-DRI are cell-penetrating peptides that selectively target specific cell populations through protein-protein interaction disruption, but their mechanisms are entirely distinct. PNC-27 targets cancer-derived cell lines through plasma membrane-bound HDM-2 engagement, inducing transmembrane pore formation and necrosis at the cell surface. FOXO4-DRI targets senescent cells through intranuclear FOXO4-p53 complex disruption, inducing mitochondrial apoptosis through nuclear-to-mitochondrial p53 translocation. The two compounds address different cell populations through different spatial mechanisms: membrane-directed necrosis versus intranuclear complex disruption driving apoptosis.

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