Compound Overview

PNC-27 is a 32-residue synthetic chimeric peptide composed of p53 residues 12–26 linked to a membrane residency peptide leader sequence. Published structural work describes the p53-derived segment as adopting an HDM-2-binding conformation.

This material is supplied as a laboratory research reagent intended for controlled experimental environments, including biochemical binding studies, structural analysis, membrane-interaction experiments, and cell-based membrane studies.

Molecular Information

Compound Type: Synthetic chimeric peptide
Sequence: H-Pro-Pro-Leu-Ser-Gln-Glu-Thr-Phe-Ser-Asp-Leu-Trp-Lys-Leu-Leu-Lys-Lys-Trp-Lys-Met-Arg-Arg-Asn-Gln-Phe-Trp-Val-Lys-Val-Gln-Arg-Gly-OH
Molecular Formula: C₁₈₈H₂₉₃N₅₃O₄₄S
CAS Number: 1159861-00-3
Purity: 99.10%

Research Applications

Published studies place PNC-27 in structure-function investigations centered on HDM-2 recognition at the plasma membrane and on peptide-associated pore architecture. Reported experimental contexts include conformational analysis, membrane colocalization, electron-microscopy imaging, and membrane-integrity measurements in transformed and untransformed cell systems.

Conformational analysis of the p53-derived segment within the HDM-2-binding site
Evaluation of PNC-27/HDM-2 complex formation by energy-minimized structural modeling
Colocalization studies of PNC-27 with membrane-associated HDM-2
Immuno-electron microscopy of peptide-associated plasma membrane pore structures
Comparative membrane-integrity assays in transformed and untransformed cell models
Structure-function comparisons with control peptides and HDM-2 localization constructs