PNC-27 10 mg

PNC-27 is a synthetic 32-amino-acid chimeric cellular-stress research peptide combining a p53-derived MDM2/HDM-2-binding sequence (residues 12-26 of the p53 protein) with the antennapedia penetratin cellular-penetration domain. The peptide sequence (PPLSQETFSDLWKLLKKWKMRRNQFWVKVQRG) places the p53-derived MDM2-binding fragment N-terminal to the penetratin leader, supporting its use as an investigational laboratory peptide in p53-pathway research models and research-model cell biology.

Research interest in PNC-27 focuses on its role as a chimeric peptide research compound that engages HDM-2 (the human homolog of MDM2) and serves as a mechanistic tool for studying p53-pathway research, peptide-membrane interactions, and cellular-stress research peptide chemistry in research models. Structural and biochemical research has shown that PNC-27 adopts a p53-peptide-like conformation when bound to HDM-2 and supports the formation of membrane pore structures in research-model cell membrane studies (Sarafraz-Yazdi et al., 2022, Biomedicines).

In laboratory research studies, PNC-27 is used to investigate MDM2/HDM-2 ligand-binding research, p53-pathway research models, peptide-membrane interaction research, and penetratin-mediated cellular-penetration mechanisms. Comparative research with truncated p53-derived peptides and isolated penetratin sequences supports laboratory research on chimeric peptide design, p53-pathway peptide pharmacology research, and research-model cell biology investigations of peptide-membrane systems.

The peptide is supplied as a lyophilized powder to ensure optimal stability during storage and handling.

PNC-27 is a chimeric research peptide constructed by fusing residues 12-26 of the human p53 protein (a region that mediates p53 binding to MDM2/HDM-2) with the antennapedia-derived penetratin sequence, a well-characterized cellular-penetration peptide motif. The resulting 32-residue peptide was developed to combine MDM2/HDM-2 ligand-binding research with penetratin-mediated cellular access for use in p53-pathway research models and peptide-membrane interaction research.

MDM2 and its human homolog HDM-2 are E3 ubiquitin-ligase research targets traditionally studied as intracellular regulators of p53 stability. Laboratory research has reported that HDM-2 can also be detected at the surface of certain research-model cell systems, providing an extracellular interaction site that PNC-27 has been used to investigate. Structural research with two-dimensional NMR and conformational-energy modelling has shown that PNC-27 adopts a p53-peptide-like α-helical conformation when engaged with HDM-2, supporting its use as a structural research tool for p53-pathway research.

This positioning at the intersection of p53-pathway research, chimeric peptide chemistry, and peptide-membrane interaction research has made PNC-27 a widely used research compound in cellular-stress research peptide investigations and research-model cell biology studies.

1. MDM2 / HDM-2 Ligand Engagement

The p53-derived N-terminal segment of PNC-27 engages HDM-2 in research models through the same interface used by native p53. Structural research has reported that PNC-27 adopts a p53-peptide-like α-helical conformation when bound to HDM-2, supporting its use as a mechanistic tool in p53-pathway research models and MDM2/HDM-2 ligand-binding research (Sarafraz-Yazdi et al., 2022, Biomedicines).

2. Penetratin-Mediated Cellular Access

The C-terminal penetratin sequence derived from the antennapedia homeodomain provides PNC-27 with cellular-penetration capacity in research models. Penetratin is a well-characterized cell-penetrating peptide motif, and its inclusion in PNC-27 supports laboratory research on peptide-membrane interaction research and chimeric peptide design.

3. Peptide-Membrane Interaction Research

Structural and biophysical research has reported that PNC-27, when engaged with membrane-localized HDM-2 in research-model cell membrane studies, can assemble into pore-like structures observable by transmembrane microscopy. These observations are investigated in laboratory research on peptide-membrane interaction research, membrane-pore-formation research, and research-model cell biology of chimeric peptide systems.

4. Conformational Determinants

Research with conformational-energy calculations and structural assays has mapped the residues required for PNC-27 engagement with HDM-2 and for peptide-membrane research outcomes. These structure-function research studies inform the broader peptide-design research literature on chimeric research peptides combining ligand-binding and cell-penetrating motifs.

Research Applications

Conclusion

PNC-27 is a synthetic chimeric research peptide combining a p53-derived MDM2/HDM-2-binding sequence with the antennapedia penetratin cellular-penetration domain. By integrating ligand-binding and cellular-penetration motifs within a single 32-residue research peptide, PNC-27 supports laboratory research on p53-pathway research models, MDM2/HDM-2 ligand-binding research, peptide-membrane interaction research, and research-model cell biology investigations of chimeric peptide systems.

Research Use Disclaimer

This product is intended for research and laboratory use only. It is designed exclusively for in vitro research purposes. All information provided is for educational and research reference only. This product is not intended for human or animal use. It is not a drug, food, or cosmetic and must not be marketed, labeled, or used as such. Use and handling are restricted to trained and qualified professionals.