PNC-27
p53-HDM2-binding · penetratin-fused research peptide
Overview
PNC-27 is a 32-amino-acid fusion research peptide combining the HDM-2-binding domain of p53 (residues 12-26) at the N-terminus with the penetratin cell-penetrating peptide (residues 43-58 of the Antennapedia homeodomain) at the C-terminus. The fusion produces a molecule that can cross plasma membranes via the penetratin moiety and then engage HDM-2 (the human homolog of MDM2) intracellularly. The most studied property of PNC-27 is selective induction of membrane pore formation in cells expressing high levels of HDM-2 on the cell surface, a property associated with malignant transformation in several tumor types but absent from most healthy cells. This selectivity is the basis for PNC-27's broad use in tumor-selective membrane-disruption research. Lyochem supplies PNC-27 as a lyophilized powder at ≥99.0% HPLC purity. The 32-residue sequence with mixed hydrophobic and cationic regions is at the more demanding end of routine SPPS, and the analytical packet covers peak-integration HPLC, mass spec, water content, and on-request sequence verification by LC-MS/MS. The penetratin moiety makes PNC-27 prone to surface adsorption like LL-37, so working dilutions should be prepared in low-bind plasticware with BSA or Tween-20 carrier to suppress concentration loss at sub-μg/mL working concentrations.
Who buys this, and why
Longevity-class peptides — Epitalon, FoxO4-DRI, PNC-27 — ship to research labs studying telomere maintenance, senescence-clearance, and tumour-suppressor pathways. The chemistry is well-behaved but solution stability matters: Epitalon and FoxO4-DRI both prefer chelator-free water and storage at −20 °C protected from light. For chronic-exposure in vivo work, request bacterial-endotoxin testing on the specific lot at quote stage.
Primary buyer fit: academic and contract research laboratories.
Specifications
- CAS
- (verification pending, please confirm via COA)
- Sequence
- PPLSQETFSDLWKLLKKWKMRRNQFWVKVQRG
- Purity (HPLC)
- ≥ 99.0%
- Common vial sizes
- 10 mg
- MOQ
- On request
- Lead time
- 14–21 days
- Storage
- -20°C, protect from light
Documentation available on request
- Lot-specific Certificate of Analysis (CoA)
- RP-HPLC chromatogram with peak integration
- ESI-MS identity confirmation (±0.5 Da)
- Sequence verification by LC-MS/MS
- Water content by Karl Fischer
- SDS / MSDS
- Oxidative-stability series for solution work
- Stability at −20 °C across 12 months
- Solubility in chelator-free water + PBS
Regulatory note
Research peptide; CAS is not consistently registered across suppliers. Sold for research use only.
Frequently asked questions
What's the design rationale for PNC-27's two-domain structure?▾
PNC-27's N-terminal HDM-2-binding domain (derived from p53 residues 12-26) is the bioactive moiety, it engages HDM-2 protein and disrupts the HDM-2/membrane interaction in cells displaying surface HDM-2. The C-terminal penetratin domain (derived from the Antennapedia homeodomain) is the delivery vehicle, it confers cell-penetration capability that the bioactive moiety alone would not have. The fusion is the classic two-domain cell-penetrating-peptide design: a recognition or binding domain attached to a transduction domain, allowing intracellular access for a molecule that would otherwise be excluded by the plasma membrane.
Why does PNC-27 selectively affect cancer cells over normal cells?▾
The selectivity is hypothesized to derive from differential surface display of HDM-2 protein. In normal cells, HDM-2 is primarily a nuclear protein with limited plasma-membrane localization; in many tumor types, HDM-2 is aberrantly displayed on the plasma membrane, where it becomes accessible to extracellular PNC-27 binding. When PNC-27 binds plasma-membrane-displayed HDM-2 in cancer cells, the interaction is hypothesized to drive membrane pore formation and selective tumor-cell death. Normal cells lacking surface HDM-2 are less susceptible. The selectivity is the basis for PNC-27's research interest as a tumor-selective membrane-disruption tool, though the mechanism details continue to be refined in the published literature.