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p53-HDM2-binding · penetratin-fused research peptide
PeptideXpo buyer fit
This PeptideXpo page is intentionally positioned for distributors, OEM buyers, and procurement teams comparing PNC-27 inside a wider peptide catalog. It is not trying to be the deepest single-molecule monograph; the differentiated intent is assortment planning, export-ready documentation, fill-size comparison, and whether this SKU belongs in a broader buyer program.
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. PeptideXpo 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
Buyers for longevity-class peptides span research labs working on telomere, collagen, and circadian-rhythm models, plus cosmetic-formulation OEMs incorporating peptides like GHK-Cu into anti-aging finished products. Copper peptides in particular require attention to chelator-free water and EDTA-free buffers in downstream formulation work, incompatibility there is the most common cause of "the peptide didn't work" support tickets in this class.
Primary buyer fit: academic and contract research laboratories.
Specifications
Documentation available on request
Regulatory note
Research peptide; CAS is not consistently registered across suppliers. Sold for research use only.
Selected literature
Frequently asked questions
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.
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.