PNC-27 from Super Human Peptides UK is a synthetic, 32-amino acid chimeric peptide. It is composed of the HDM-2-binding domain of the p53 tumour suppressor protein, linked to a cell-penetrating sequence (penetratin) derived from the antennapedia protein. In laboratory research, PNC-27 is heavily studied in the field of oncology for its unique membranolytic (membrane-destroying) properties.
Unlike traditional p53-activating agents that work inside the nucleus, researchers utilize PNC-27 to target HDM-2 proteins that are uniquely expressed on the outer cell membranes of various cancer cells. Upon binding to membrane-bound HDM-2, the peptide induces rapid pore formation, leading to tumour cell necrosis while leaving healthy cells (which do not express HDM-2 on their surface) largely unaffected. Produced under GMP-compliant conditions and verified for 99% purity or higher, PNC-27 is a vital tool for targeted cancer therapy models.
- —Targeted Oncology Model: Highly specific for HDM-2 proteins located on cancer cell membranes.
- —Dual-Domain Structure: Combines a p53-derived sequence with a penetratin delivery sequence.
- —Membranolytic Action: Induces rapid pore formation and necrosis in target cells independent of internal p53 pathways.
- —High Purity: 99% purity or higher (verified by HPLC and MS analysis).
- —Quality Standard: GMP / ISO certified manufacturing.
- —Selective Toxicity: Studying the peptide's ability to destroy cancer cells (e.g., breast, pancreatic, melanoma) while sparing healthy fibroblasts.
- —HDM-2 Membrane Localization: Investigating why certain tumour cells express HDM-2 on their plasma membranes and how this can be exploited.
- —Pore Formation Mechanics: Researching the physical disruption of the lipid bilayer leading to rapid cell death. p53-
- —Independent Pathways: Exploring how PNC-27 bypasses the need for functional intracellular p53 to induce cell death
- —Synergistic Therapy Models: Preclinical models combining PNC-27 with traditional chemotherapeutic agents to measure enhanced efficacy.
PNC-27 was developed by researchers Dr. Josef Michl and Dr. Matthew Pincus, who made the groundbreaking discovery that HDM-2 (a protein that normally degrades p53 inside the cell) is highly expressed on the outside of cancer cell membranes.
Laboratory studies demonstrated that when PNC-27 binds to this membrane-bound HDM-2, it undergoes a structural change that allows it to punch holes directly into the cancer cell's plasma membrane, causing it to rupture and die. In multiple in-vitro and in-vivo animal models spanning various cancer lines (including highly aggressive pancreatic and leukemia models), PNC-27 has shown the ability to eradicate tumour cells with near-zero toxicity to surrounding healthy tissue. Because it kills cells by physical membrane disruption rather than relying on complex internal signaling, it remains a major subject of research for overcoming chemo-resistant cancers.
- 1.Michl, J. et al., "PNC-27, a chimeric p53-penetratin peptide, binds to HDM-2 in intact human cancer cells, induces cell-membrane pore formation, and selectively kills cancer cells," International Journal of Cancer, 2006.
- 2.Sarafraz-Yazdi, E. et al., "A peptide derived from p53 targets cancer cells specifically by binding to HDM-2," Anticancer Research, 2010.
- 3.Bowne, P.Z. et al., "The anti-cancer peptide, PNC-27, induces tumor cell necrosis of a poorly differentiated murine B cell lymphoma," Annals of Clinical and Laboratory Science, 2008.
- 4.Wilbur, A. et al., "The anti-cancer peptide, PNC-27, induces rapid tumor cell necrosis of human leukemia cells," Annals of Clinical and Laboratory Science, 2011.
