Buy PNC-27 Research Peptide

What is PNC-27?

PNC-27 is a synthetic peptide that joins a p53-derived sequence to a membrane-entering sequence. In lab studies it triggers cell death selectively in cell lines that carry high levels of a protein called HDM-2, while sparing cell lines without it. It is studied as a research tool for this selective cell-death pathway.

• Built to trigger selective cell death in HDM-2-high cell lines in lab studies
• Targets a protein found at high levels on certain cell lines, absent from control lines
• Studied across several HDM-2-high cell lines in the lab
• Used as a research tool for understanding HDM-2-related cell-death signaling

For research use only. Not approved for human therapeutic use.

PNC-27 is a synthetic chimeric peptide with a molecular weight of 4031.72 g/mol, consisting of a p53-derived HDM-2 (human double minute 2) binding domain fused to a cell-penetrating membrane-active sequence. The p53-derived segment corresponds to residues from the transactivation domain of the p53 tumour suppressor protein, the minimal region required for MDM2/HDM-2 binding, while the C-terminal membrane-active domain is designed to facilitate cellular membrane interaction. PNC-27 was designed based on the observation that HDM-2 is overexpressed and aberrantly localised to cell membranes in certain transformed cell populations. Produced via solid-phase peptide synthesis, PNC-27 is associated with MDM2/HDM-2 signalling and membrane integrity pathways.

PNC-27 is a peptide designed to exploit the differential membrane localisation of HDM-2 between normal and transformed cell populations. In vitro studies have documented that PNC-27 binds HDM-2 associated with the plasma membrane of cancer cells and kills them by membranolysis [1]. Structure-function studies have examined the relative contributions of the p53-derived binding domain and the membrane-active leader sequence: a foundational conformational-design study compared three p53-derived fragments and found all three selectively cytotoxic to transformed cells, while sparing normal cells and human cord-blood-derived stem cells [2], and subsequent work has characterised the resulting membrane pores as lined with PNC-27–HDM-2 complexes at approximately 1:1 stoichiometry, with pore formation and cell lysis dependent on membrane-localised HDM-2 expression [3], making PNC-27 a reference compound in preclinical oncology research examining p53-derived, HDM-2-directed membranolytic peptides and the differential membrane localisation of HDM-2 between transformed and normal cell populations.

PNC-27 is produced to research-grade standards and independently verified by third-party HPLC and MS-UPLC analysis before dispatch. Vials are vacuum sealed and stored in a temperature controlled, monitored cold storage system. Certificates of Analysis are available on request.

Sold strictly for in vitro research purposes only. Not for human consumption. Intended for use by qualified researchers in laboratory settings only.

References

1Sarafraz-Yazdi E, Bowne WB, Adler V, Sookraj KA, Wu V, Shteyler V, et al. Anticancer peptide PNC-27 adopts an HDM-2-binding conformation and kills cancer cells by binding to HDM-2 in their membranes. Proc Natl Acad Sci U S A. 2010 Feb 2;107(5):1918–23. ; PubMed Central PMCID: PMC2836618.PubMed PMID: 200806802Kanovsky M, Raffo A, Drew L, Rosal R, Do T, Friedman FK, et al. Peptides from the amino terminal mdm-2-binding domain of p53, designed from conformational analysis, are selectively cytotoxic to transformed cells. Proc Natl Acad Sci U S A. 2001 Oct 23;98(22):12438–43. ; PubMed Central PMCID: PMC60072.PubMed PMID: 116067163Sarafraz-Yazdi E, Mumin S, Cheung D, Fridman D, Lin B, Wong L, et al. PNC-27, a Chimeric p53-Penetratin Peptide Binds to HDM-2 in a p53 Peptide-like Structure, Induces Selective Membrane-Pore Formation and Leads to Cancer Cell Lysis. Biomedicines. 2022 Apr 20;10(5):945. ; PubMed Central PMCID: PMC9138867.PubMed PMID: 35625682

Scientific Review

Dr. Martina Rossi, PhD

Scientific Contributor and Reviewer

Reviewed for scientific accuracy, 14 June 2026

View credentials →

PNC-27 is a synthetic chimeric peptide with a molecular weight of 4031.72 g/mol, consisting of a p53-derived HDM-2 (human double minute 2) binding domain fused to a cell-penetrating membrane-active sequence. The p53-derived segment corresponds to residues from the transactivation domain of the p53 tumour suppressor protein, the minimal region required for MDM2/HDM-2 binding, while the C-terminal membrane-active domain is designed to facilitate cellular membrane interaction. PNC-27 was designed based on the observation that HDM-2 is overexpressed and aberrantly localised to cell membranes in certain transformed cell populations. Produced via solid-phase peptide synthesis, PNC-27 is associated with MDM2/HDM-2 signalling and membrane integrity pathways.

PNC-27 is a peptide designed to exploit the differential membrane localisation of HDM-2 between normal and transformed cell populations. In vitro studies have documented that PNC-27 binds HDM-2 associated with the plasma membrane of cancer cells and kills them by membranolysis [1]. Structure-function studies have examined the relative contributions of the p53-derived binding domain and the membrane-active leader sequence: a foundational conformational-design study compared three p53-derived fragments and found all three selectively cytotoxic to transformed cells, while sparing normal cells and human cord-blood-derived stem cells [2], and subsequent work has characterised the resulting membrane pores as lined with PNC-27–HDM-2 complexes at approximately 1:1 stoichiometry, with pore formation and cell lysis dependent on membrane-localised HDM-2 expression [3], making PNC-27 a reference compound in preclinical oncology research examining p53-derived, HDM-2-directed membranolytic peptides and the differential membrane localisation of HDM-2 between transformed and normal cell populations.

PNC-27 is produced to research-grade standards and independently verified by third-party HPLC and MS-UPLC analysis before dispatch. Vials are vacuum sealed and stored in a temperature controlled, monitored cold storage system. Certificates of Analysis are available on request.

Sold strictly for in vitro research purposes only. Not for human consumption. Intended for use by qualified researchers in laboratory settings only.

References

1Sarafraz-Yazdi E, Bowne WB, Adler V, Sookraj KA, Wu V, Shteyler V, et al. Anticancer peptide PNC-27 adopts an HDM-2-binding conformation and kills cancer cells by binding to HDM-2 in their membranes. Proc Natl Acad Sci U S A. 2010 Feb 2;107(5):1918–23. ; PubMed Central PMCID: PMC2836618.PubMed PMID: 200806802Kanovsky M, Raffo A, Drew L, Rosal R, Do T, Friedman FK, et al. Peptides from the amino terminal mdm-2-binding domain of p53, designed from conformational analysis, are selectively cytotoxic to transformed cells. Proc Natl Acad Sci U S A. 2001 Oct 23;98(22):12438–43. ; PubMed Central PMCID: PMC60072.PubMed PMID: 116067163Sarafraz-Yazdi E, Mumin S, Cheung D, Fridman D, Lin B, Wong L, et al. PNC-27, a Chimeric p53-Penetratin Peptide Binds to HDM-2 in a p53 Peptide-like Structure, Induces Selective Membrane-Pore Formation and Leads to Cancer Cell Lysis. Biomedicines. 2022 Apr 20;10(5):945. ; PubMed Central PMCID: PMC9138867.PubMed PMID: 35625682

Scientific Review

Dr. Martina Rossi, PhD

Scientific Contributor and Reviewer

Reviewed for scientific accuracy, 14 June 2026

View credentials →CAS NumberN/A (novel chimeric research peptide)Molecular Weight~3,500–3,800 g/molPurity≥98%Physical FormLyophilised PowderManufacturingManufactured in an ISO9001 Certified LaboratoryTestingHPLC + MS-UPLCSKURSC-PNC27-6727

Lyophilised powder: store at -20 °C or below, away from light and moisture. Once reconstituted in an appropriate laboratory diluent (e.g. sterile water, PBS, or assay buffer), store at 2–8 °C and use within the validated period for your protocol. Do not refreeze.

PNC-27 is a synthetic chimeric peptide with a molecular weight of 4031.72 g/mol, consisting of a p53-derived HDM-2 (human double minute 2) binding domain fused to a cell-penetrating membrane-active sequence. The p53-derived segment corresponds to residues from the transactivation domain of the p53 tumour suppressor protein, the minimal region required for MDM2/HDM-2 binding, while the C-terminal membrane-active domain is designed to facilitate cellular membrane interaction. PNC-27 was designed based on the observation that HDM-2 is overexpressed and aberrantly localised to cell membranes in certain transformed cell populations. Produced via solid-phase peptide synthesis, PNC-27 is associated with MDM2/HDM-2 signalling and membrane integrity pathways.

PNC-27 is a peptide designed to exploit the differential membrane localisation of HDM-2 between normal and transformed cell populations. In vitro studies have documented that PNC-27 binds HDM-2 associated with the plasma membrane of cancer cells and kills them by membranolysis [1]. Structure-function studies have examined the relative contributions of the p53-derived binding domain and the membrane-active leader sequence: a foundational conformational-design study compared three p53-derived fragments and found all three selectively cytotoxic to transformed cells, while sparing normal cells and human cord-blood-derived stem cells [2], and subsequent work has characterised the resulting membrane pores as lined with PNC-27–HDM-2 complexes at approximately 1:1 stoichiometry, with pore formation and cell lysis dependent on membrane-localised HDM-2 expression [3], making PNC-27 a reference compound in preclinical oncology research examining p53-derived, HDM-2-directed membranolytic peptides and the differential membrane localisation of HDM-2 between transformed and normal cell populations.

PNC-27 is produced to research-grade standards and independently verified by third-party HPLC and MS-UPLC analysis before dispatch. Vials are vacuum sealed and stored in a temperature controlled, monitored cold storage system. Certificates of Analysis are available on request.

Sold strictly for in vitro research purposes only. Not for human consumption. Intended for use by qualified researchers in laboratory settings only.

References

1Sarafraz-Yazdi E, Bowne WB, Adler V, Sookraj KA, Wu V, Shteyler V, et al. Anticancer peptide PNC-27 adopts an HDM-2-binding conformation and kills cancer cells by binding to HDM-2 in their membranes. Proc Natl Acad Sci U S A. 2010 Feb 2;107(5):1918–23. ; PubMed Central PMCID: PMC2836618.PubMed PMID: 200806802Kanovsky M, Raffo A, Drew L, Rosal R, Do T, Friedman FK, et al. Peptides from the amino terminal mdm-2-binding domain of p53, designed from conformational analysis, are selectively cytotoxic to transformed cells. Proc Natl Acad Sci U S A. 2001 Oct 23;98(22):12438–43. ; PubMed Central PMCID: PMC60072.PubMed PMID: 116067163Sarafraz-Yazdi E, Mumin S, Cheung D, Fridman D, Lin B, Wong L, et al. PNC-27, a Chimeric p53-Penetratin Peptide Binds to HDM-2 in a p53 Peptide-like Structure, Induces Selective Membrane-Pore Formation and Leads to Cancer Cell Lysis. Biomedicines. 2022 Apr 20;10(5):945. ; PubMed Central PMCID: PMC9138867.PubMed PMID: 35625682

Scientific Review

Dr. Martina Rossi, PhD

Scientific Contributor and Reviewer

Reviewed for scientific accuracy, 14 June 2026

View credentials →CAS NumberN/A (novel chimeric research peptide)Molecular Weight~3,500–3,800 g/molPurity≥98%Physical FormLyophilised PowderManufacturingManufactured in an ISO9001 Certified LaboratoryTestingHPLC + MS-UPLCSKURSC-PNC27-6727

Lyophilised powder: store at -20 °C or below, away from light and moisture. Once reconstituted in an appropriate laboratory diluent (e.g. sterile water, PBS, or assay buffer), store at 2–8 °C and use within the validated period for your protocol. Do not refreeze.