PNC-27 (5mg)

€138.00

Size: 5mg
Contents: PNC-27
Form: Lyophilized powder
Purity: >99%
SKU: PNC-27

Categories: Peptides for Sale, Research Peptides for Sale

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PNC-27 (5mg) – Research Peptide

PNC-27 (5mg) is a synthetic research peptide investigated in molecular biology and cancer-cell research, particularly in relation to the HDM-2/MDM-2 protein, membrane interactions and mechanisms of tumour-cell death.

PNC-27 is derived from a region of the p53 protein involved in HDM-2 binding and incorporates a cell-penetrating or membrane-residency sequence. Scientific studies have investigated its ability to interact with membrane-associated HDM-2 and induce membrane-pore formation in experimental cancer-cell models.

The referenced Core Peptides product is supplied as 5mg of lyophilised PNC-27 powder with a reported purity of >99%. The supplier specifies that the material is intended exclusively for research, laboratory and analytical purposes and is not intended for human or animal consumption.

PNC-27 is particularly interesting to researchers because its proposed mechanism differs from conventional approaches that target intracellular apoptotic pathways.

Published experimental research suggests that PNC-27 can associate with HDM-2 at the plasma membrane of certain tumour cells and promote the formation of membrane pores, resulting in rapid loss of membrane integrity and necrotic cell death in the models studied.

These findings remain an area of experimental research. Results observed in cultured cells or animal models should not be interpreted as evidence that PNC-27 is an approved cancer treatment or that it is safe or effective for use in humans.

What Is PNC-27?

PNC-27 is a synthetic peptide designed around the HDM-2-binding region of p53 and a membrane-penetrating or membrane-residency sequence. It was developed as part of research investigating the interaction between p53-derived peptides and HDM-2/MDM-2, a protein that is frequently studied in cancer biology.

Published structural research describes PNC-27 as a peptide containing residues 12–26 of p53 linked to a cell-penetrating leader sequence. This design allows researchers to investigate both target recognition and membrane-associated peptide activity within the same molecular construct.

The Core Peptides product page describes its PNC-27 material as a 27-amino-acid peptide, while several peer-reviewed publications describe the experimentally studied PNC-27 construct as a 32-residue peptide. Researchers should therefore rely on the batch-specific analytical documentation supplied with the material when exact construct identity and sequence are critical to an experiment.

PNC-27 (5mg) Product Specifications

Specification	Details
Product Name	PNC-27
Quantity	5mg
Product Form	Lyophilised powder
Reported Purity	>99%
Research Classification	Synthetic peptide research material
Primary Research Area	HDM-2/MDM-2, p53 signalling and cancer-cell membrane biology
Research Models	Cell-based and experimental biological models
Intended Use	Laboratory, analytical and in-vitro research

The product quantity, physical form and reported purity correspond to the current Core Peptides listing.

PNC-27 and the p53–HDM-2 Interaction

Understanding PNC-27 research requires some background on the p53–HDM-2 pathway. The p53 protein is a major tumour-suppressor protein involved in cellular responses to DNA damage and other forms of cellular stress. HDM-2, also known as MDM-2, is an important regulatory protein that interacts with p53 and contributes to the control of p53 activity.

PNC-27 was designed using a portion of the p53 sequence that participates in HDM-2 binding. The peptide therefore provides researchers with a molecular tool for studying this interaction independently of the complete p53 protein.

Rather than simply acting as a conventional inhibitor of intracellular MDM-2, published studies propose that PNC-27 can associate with HDM-2 located at the plasma membrane. This membrane-associated interaction forms the basis of much of the research surrounding PNC-27.

How Does PNC-27 Work in Research Models?

The proposed mechanism of PNC-27 involves several stages. First, the peptide is able to access cellular membranes through its membrane-penetrating or membrane-residency component. It can then interact with HDM-2 associated with the plasma membrane of susceptible tumour cells.

Experimental research suggests that PNC-27–HDM-2 complexes can participate in the formation of transmembrane pores. These pores compromise the integrity of the plasma membrane, allowing ions and intracellular components to move across the membrane. The resulting loss of membrane integrity can lead to rapid necrotic cell death in susceptible experimental cancer cells.

A 2022 study used structural calculations and immuno-electron microscopy to investigate the proposed interaction. The researchers observed ring-shaped structures at membrane pore sites containing PNC-27 and HDM-2 signals and proposed that these complexes contribute to pore formation.

This mechanism is still a subject of research and should not be presented as an established therapeutic mechanism in humans.

PNC-27 and Membrane-Pore Formation

Membrane-pore formation is one of the defining areas of PNC-27 research.

Unlike conventional cytotoxic mechanisms that primarily depend on intracellular signalling cascades, membrane-active peptides can affect cells by altering the physical properties of their plasma membranes. PNC-27 has been investigated as a membrane-active peptide whose association with HDM-2 may facilitate the formation of transmembrane structures.

Researchers have used microscopy, fluorescence labelling and biochemical markers such as lactate dehydrogenase (LDH) release to investigate this process. Increased LDH release is consistent with loss of membrane integrity and cellular lysis in experimental systems.

A 2010 study reported that PNC-27 remained intact during the membrane-lysis process observed in its experimental cancer-cell model, supporting the hypothesis that the complete peptide rather than isolated fragments is important for its membrane activity.

PNC-27 and Necrotic Cell Death

Research into PNC-27 has primarily focused on necrosis rather than conventional apoptosis.

Necrosis involves loss of cellular membrane integrity and leakage of intracellular contents. This differs from apoptosis, which is a regulated form of programmed cell death involving characteristic biochemical and morphological changes.

Several studies have reported that PNC-27-treated tumour cells demonstrate markers consistent with membrane disruption and necrotic cell death. In a study involving K562 human leukaemia cells, PNC-27 exposure was associated with LDH release and cell death, while caspase-based measurements did not indicate the same apoptotic mechanism.

The distinction between necrosis and apoptosis is important for researchers investigating the peptide’s molecular mechanism and comparing PNC-27 with other experimental anticancer compounds.

PNC-27 and HDM-2/MDM-2

HDM-2 and MDM-2 refer to the human and mouse forms, respectively, of a protein involved in regulation of p53. PNC-27 research has placed particular emphasis on HDM-2 present at the surface of tumour cells.

Published studies suggest that PNC-27 can co-localise with membrane-associated HDM-2 in susceptible tumour cells. This observation has led researchers to investigate HDM-2 as a possible molecular determinant of PNC-27 membrane activity.

A 2024 study further investigated this mechanism by examining whether an antibody directed against the p53-binding region of HDM-2 could interfere with PNC-27-induced cancer-cell necrosis. The reported findings supported the involvement of this HDM-2 region in the observed activity.

PNC-27 and Cancer-Cell Research

PNC-27 has been investigated across multiple experimental cancer-cell models, including pancreatic cancer, breast cancer, colon cancer and leukaemia models.

The research objective is generally not to establish a clinical treatment but to understand whether differences in membrane-associated HDM-2 can provide a molecular basis for differential peptide activity.

In experimental studies, PNC-27 has demonstrated cytotoxic activity against several tumour-cell lines. For example, research involving K562 leukaemia cells reported substantial cell death associated with membrane HDM-2 and PNC-27 co-localisation.

Research involving colon cancer models has also investigated PNC-27 against tumour cells with stem-like characteristics. One study reported tumour-cell necrosis and investigated effects on tumour growth in an animal model.

Such findings are scientifically relevant but remain preclinical. Cell-line and animal-model outcomes cannot be directly translated into clinical efficacy or safety.

PNC-27 in Leukaemia Research

PNC-27 has been studied in several leukaemia cell models. This research is particularly relevant because some leukaemia cells can express HDM-2 at their plasma membrane, providing an experimental system for studying the peptide’s proposed target.

A 2014 study examined PNC-27 in K562 cells, a human leukaemia cell line lacking functional p53 expression. The investigators reported membrane HDM-2 expression and PNC-27-associated necrosis, suggesting that the observed activity could occur through a pathway that does not depend on functional intracellular p53.

Later research examined additional acute myeloid leukaemia cell lines and investigated membrane HDM-2 as a potential determinant of PNC-27 activity.

These studies provide useful models for investigating membrane-associated tumour biology, peptide selectivity and non-apoptotic mechanisms of cell death.

PNC-27 and Pancreatic Cancer Research

Pancreatic cancer models have been among the experimental systems used to investigate PNC-27.

Research has examined whether PNC-27 can interact with membrane-associated HDM-2 on pancreatic tumour cells and whether this interaction contributes to membrane-pore formation and necrosis. More recent research has also investigated possible mitochondrial effects following PNC-27 exposure.

The 2024 study reported evidence of mitochondrial disruption in PNC-27-treated pancreatic cancer cells and further investigated the role of the HDM-2 binding site in the peptide’s activity.

These findings expand the mechanistic research surrounding PNC-27 but remain experimental and do not establish the peptide as a treatment for pancreatic cancer.

PNC-27 and Colon Cancer Research

Colon cancer is another area in which PNC-27 has been investigated.

A study examining colon cancer cells and stem-like colon cancer populations reported that PNC-27 co-localised with membrane HDM-2 in tumour cells and induced cell death.

The study also used an animal model to investigate tumour growth and reported necrosis within tumour nodules without the same observed effect in normal tissue.

These observations have encouraged further research into membrane-associated HDM-2 as a possible target for experimental peptide approaches.

Nevertheless, results from preclinical models require independent validation and clinical investigation before any conclusions about human therapeutic use can be made.

PNC-27 and Selectivity Research

One of the most frequently investigated characteristics of PNC-27 is its apparent selectivity in certain experimental models.

Researchers have reported that PNC-27 can produce pronounced membrane disruption in tumour cells while producing substantially less activity in particular untransformed control cells.

The proposed explanation is that tumour-cell membranes may contain HDM-2 in a configuration or abundance that allows PNC-27 to bind and form membrane-associated complexes.

However, biological selectivity observed in a particular cell model should not be interpreted as universal selectivity in all human tissues. Membrane composition, HDM-2 expression, peptide concentration, experimental conditions and cellular phenotype can all influence observed activity.

PNC-27 and Mitochondrial Research

More recent research has expanded the investigation of PNC-27 beyond the plasma membrane.

A 2024 study reported evidence of mitochondrial disruption following PNC-27 exposure in pancreatic cancer cells. The investigators used mitochondrial and lysosomal markers alongside immuno-electron microscopy to examine the intracellular effects of the peptide.

The study also reported that an antibody targeting the p53-binding site of HDM-2 could block PNC-27-induced tumour-cell necrosis, providing further evidence that HDM-2 binding is important to the observed mechanism.

Mitochondrial effects are therefore an emerging area of PNC-27 research, alongside the more established focus on membrane-pore formation.

PNC-27 Structural Research

Structural studies have been important in understanding how PNC-27 may interact with HDM-2 and cellular membranes.

NMR research published in Biochemistry examined the structure of PNC-27 in aqueous and membrane-mimetic environments. The study reported helical structural elements and proposed that the peptide adopts an amphipathic structure in membrane-like conditions.

Such structural characteristics are relevant because amphipathic helices can participate in interactions with lipid membranes. Researchers have therefore investigated whether the peptide’s structural transition contributes to its membrane activity.

Structural analysis also provides a basis for comparing PNC-27 with related peptides and designing modified constructs for experimental investigation.

PNC-27 and Cell-Penetrating Peptide Research

PNC-27 incorporates a cell-penetrating or membrane-residency sequence that forms an important part of its experimental design.

Cell-penetrating peptides are sequences investigated for their ability to facilitate transport across cellular membranes or interact with membrane structures. In PNC-27, the leader sequence is linked to a p53-derived HDM-2-binding region, creating a combined construct with both targeting and membrane-associated properties.

This design enables researchers to investigate how a target-binding peptide can behave when connected to a membrane-active sequence.

PNC-27 Compared With PNC-28

Feature	PNC-27	PNC-28
Research origin	p53-derived peptide construct	Related p53-derived peptide construct
HDM-2-related region	Includes p53 residues 12–26	Includes p53 residues 17–26
Research focus	HDM-2 binding, membrane pores and necrosis	Related membrane and tumour-cell research
Experimental models	Multiple tumour-cell and animal models	Multiple tumour-cell and animal models

PNC-27 and PNC-28 are structurally related but are not identical peptides. Early research specifically distinguished the p53 regions incorporated into each construct.

PNC-27 Research Applications

Qualified laboratories may investigate PNC-27 in areas including:

HDM-2/MDM-2 research involving protein–peptide interactions.
p53 research involving the HDM-2-binding region of p53.
Cancer-cell membrane biology involving membrane-associated proteins.
Membrane-pore research examining peptide-induced membrane disruption.
Necrosis research investigating non-apoptotic cell-death pathways.
Cell-penetrating peptide research examining peptide transport and membrane interaction.
Structural biology involving peptide conformation and target binding.
Leukaemia research using experimental cell-line models.
Pancreatic and colon cancer research using preclinical models.
Mitochondrial research examining intracellular effects of membrane-active peptides.
Peptide engineering involving modifications of targeting or membrane-active domains.
Analytical peptide research involving identity, purity and structural verification.

PNC-27 Analytical Characterisation

Analytical verification is particularly important when studying biologically active research peptides. Researchers may evaluate PNC-27 using appropriate analytical techniques to confirm the identity and quality of a specific batch.

Potential analytical considerations include:

Identity confirmation: Verification of the expected PNC-27 construct.
Purity analysis: Assessment of the principal peptide peak and related impurities.
Mass spectrometry: Confirmation of molecular mass.
Chromatographic analysis: Examination of peptide purity and composition.
Batch consistency: Comparison of analytical results between production batches.
Stability studies: Monitoring the material under defined storage conditions.

Core Peptides reports >99% purity for the referenced 5mg PNC-27 product and provides links to HPLC and mass-spectrometry documentation on the product page. Researchers should review the batch-specific Certificate of Analysis before commencing experimental work.

PNC-27 (5mg) Storage Considerations

The referenced PNC-27 material is supplied as a lyophilised powder. Appropriate storage is important for maintaining the integrity of synthetic peptide research materials.

Laboratories should:

Keep the peptide in its original, clearly labelled container.
Follow the supplier’s current storage instructions.
Protect the material from unnecessary moisture exposure.
Minimise inappropriate temperature fluctuations.
Limit unnecessary exposure to environmental contaminants.
Review the batch-specific Certificate of Analysis and technical documentation.
Use suitable laboratory handling and containment procedures.

Exact storage requirements can depend on the peptide formulation, packaging and intended experimental application. The manufacturer’s current technical documentation should take precedence over generic storage recommendations.

Frequently Asked Questions About PNC-27 (5mg)

What is PNC-27?

PNC-27 is a synthetic research peptide derived from a p53 region involved in HDM-2 binding and linked to a membrane-penetrating or membrane-residency sequence. It has been investigated primarily in experimental cancer-cell and molecular-biology research.

What is PNC-27 studied for?

PNC-27 is studied for its interaction with HDM-2, membrane-pore formation, necrotic cell death and related mechanisms in experimental cancer-cell models.

What is HDM-2?

HDM-2, commonly referred to as MDM-2 in the mouse system, is a protein involved in regulation of the tumour-suppressor protein p53. PNC-27 research focuses particularly on HDM-2 associated with the plasma membrane of certain tumour cells.

How does PNC-27 interact with cancer cells in research models?

Published studies propose that PNC-27 binds membrane-associated HDM-2 and participates in transmembrane pore formation. The resulting disruption of the plasma membrane can lead to loss of cellular integrity and necrotic cell death in susceptible experimental models.

Does PNC-27 induce apoptosis?

The principal mechanism reported in PNC-27 research is membrane disruption followed by necrotic cell death rather than conventional apoptosis. Experimental studies have used markers such as LDH release and caspase activity to distinguish these mechanisms.

Has PNC-27 been studied in leukaemia cells?

Yes. PNC-27 has been investigated in K562 and other experimental leukaemia-cell models. Studies have examined membrane HDM-2 expression and its relationship with PNC-27-associated cell death.

Has PNC-27 been studied in animal models?

Yes. Preclinical studies have investigated PNC-27 in animal tumour models, including research involving colon cancer. These studies are experimental and do not establish safety or efficacy in humans.

Is PNC-27 an approved cancer treatment?

No. PNC-27 should not be represented as an approved cancer medicine. The available literature is predominantly preclinical, involving cell-based experiments and animal models. The Core Peptides product is supplied for research purposes only.

Is PNC-27 suitable for human consumption?

No. The referenced Core Peptides product is explicitly designated for research, laboratory and analytical purposes only, with human and animal consumption prohibited.

What is the form of PNC-27 (5mg)?

The referenced product is supplied as 5mg of lyophilised PNC-27 powder with a reported purity of greater than 99%.

What is the difference between PNC-27 and PNC-28?

PNC-27 and PNC-28 are related p53-derived research peptides but contain different portions of the p53 HDM-2-binding region. PNC-27 includes residues 12–26, whereas PNC-28 contains residues 17–26 in the original constructs described in the literature.

Why is PNC-27 important in peptide research?

PNC-27 provides a model for studying how a peptide containing a protein-binding domain and membrane-active sequence can interact with membrane-associated HDM-2 and influence membrane integrity. This makes it relevant to research into peptide targeting, membrane biology and experimental cancer-cell mechanisms.

What analytical testing is relevant to PNC-27?

Researchers may use HPLC, mass spectrometry and other suitable analytical methods to verify peptide identity, purity and batch consistency. Core Peptides provides links to HPLC and mass-spectrometry information for the referenced product.

Why Choose PNC-27 (5mg) for Research?

PNC-27 (5mg) provides a defined synthetic peptide material for laboratories investigating HDM-2 biology, p53-derived peptide structures and membrane-associated mechanisms of experimental tumour-cell death.

Defined research material: PNC-27 synthetic peptide.
5mg format: Supplied as a controlled research quantity.
Lyophilised powder: Convenient format for laboratory handling.
Reported purity: Greater than 99% according to the referenced supplier listing.
Research documentation: Product information includes access to HPLC and mass-spectrometry documentation.
Broad research relevance: Suitable for investigations involving HDM-2, p53, membrane biology and experimental cell-death mechanisms.

Researchers should review the applicable batch-specific Certificate of Analysis and technical documentation before using the material in an experiment.

PNC-27 (5mg) Research Summary

PNC-27 (5mg) is a synthetic peptide investigated extensively in preclinical research involving HDM-2/MDM-2, p53-derived peptide structures and tumour-cell membrane biology. Its distinctive research interest comes from the proposed ability to associate with membrane-bound HDM-2 and promote membrane-pore formation in susceptible experimental cancer cells.

Studies have examined PNC-27 in pancreatic cancer, colon cancer, breast cancer and leukaemia models, with reported effects including membrane disruption, LDH release, necrotic cell death and, in more recent work, mitochondrial disruption.

The scientific literature provides a useful foundation for investigating PNC-27’s molecular structure and biological activity, but the evidence remains preclinical. Experimental results should therefore be interpreted within the context of the specific cell line, animal model, concentration and study design used.

For qualified researchers, the 5mg lyophilised PNC-27 format provides a defined research material for controlled laboratory studies involving peptide chemistry, protein–peptide interactions, membrane biology and experimental mechanisms of cell death.

Research-Use Disclaimer

PNC-27 (5mg) is intended solely for qualified research, laboratory, analytical and in-vitro experimental purposes. It is not intended for human or veterinary consumption, self-administration, diagnosis, treatment, cure or prevention of any disease.

References to cancer cells, tumour-cell death, membrane disruption, HDM-2, p53 or other biological effects describe areas of scientific investigation and should not be interpreted as claims of clinical efficacy or as evidence that PNC-27 is an approved cancer treatment.

Researchers should review the applicable Certificate of Analysis, safety information and supplier documentation for the specific batch before conducting experiments. All handling, storage and disposal should be performed by appropriately trained personnel in accordance with institutional procedures and applicable legislation.

For research use only. Human and animal consumption prohibited.

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