PNC-27

Product Overview

A fundamental standard in oncology and molecular biology research dictates that exploring selective membranolytic agents requires complete structural integrity and verified chemical purity. The PNC-27 formulation addresses these demanding benchmarks, serving as a highly purified synthetic chimeric peptide developed for precise in vitro and in vivo laboratory modeling of targeted cellular necrosis. Each vial provides pure PNC-27, stabilized as a vacuum freeze-dried (lyophilized) powder maintaining a verified purity profile of greater than 98%.

PNC-27 is a 32-amino acid chimeric peptide constructed with two distinct functional segments. The amino-terminal end contains a 15-amino acid sequence (residues 12–26) derived from the HDM-2-binding domain of the human p53 tumor suppressor protein. This recognition sequence is covalently attached at its carboxyl terminus to a 17-amino acid transmembrane-penetrating sequence, often termed the membrane residency peptide (MRP). Characterized by a molecular weight of 4,031.7 g/mol and an amphipathic alpha-helix-loop-alpha-helix conformation in solution, this architecture allows the peptide to selectively recognize specialized cell-surface targets and interact directly with lipid bilayers.

Operating via a highly selective, p53-independent mechanism, PNC-27 targets the HDM-2 (Human Double Minute 2) protein, which is uniquely expressed on the outer plasma membranes of various cancer cell lines but absent on healthy, untransformed cells. Upon binding to membrane-bound HDM-2, the chimeric peptide undergoes a structural shift, inserting its MRP segment into the lipid bilayer. This interaction induces the rapid formation of physical transmembrane pores, causing cell lysis and selective tumor cell necrosis without triggering typical intracellular apoptotic pathways. These unique dynamics allow researchers to investigate cell membrane biochemistry, tumor cell susceptibilities, and targeted cellular disruption within controlled laboratory environments.

Product Specifications

• Form: Lyophilized (vacuum freeze-dried) powder
• Purity: Greater than 98% (verified by HPLC analysis)
• Amino Acid Sequence: 32-residue chimeric chain (p53 domain fused to an MRP leader)
• Molecular Weight: 4,031.7 g/mol
• Primary Research Focus: Selective Membranolysis, HDM-2 Surface Binding, and p53-Independent Necrosis

Container Specifications

The physical attributes of the storage vessel directly impact the shelf life of the compound. All research environments should utilize clean, chemically inert containers. Glass vials provide the highest level of protection against gas permeability and chemical interaction, though high-density polypropylene tubes serve as a valid alternative. Keep all stored peptides away from automatic frost-free freezers, as their internal defrost cycles create regular temperature swings that compromise peptide longevity.