PNC-27

PNC-27 was created by a supercomputer at SUNY Downstate Medical Center in New York in 2000 . It is a membrane-active peptide that binds to the HDM-2 protein expressed in the cancer cell membranes of solid tissue tumor cells . The peptide induces transmembrane pore formation in cancer cells, but not in normal cells, resulting in tumor cell necrosis (cell death) .

The peptide contains p53 protein amino acid residues 12–26 of its HDM-2 binding domain attached to a transmembrane-penetrating sequence, also called the membrane residency peptide (MRP) . This structure allows PNC-27 to selectively target and kill cancer cells without relying on the master regulator of apoptosis, p53 .

PNC-27 has shown to be highly effective in selectively targeting a wide variety of specific forms of cancer, including pancreatic cancer, breast cancer, leukemia, melanoma, and additional cancer lines . It works by binding to the HDM-2 protein in the cell membranes of cancerous cells, creating pores or holes in the cell membrane, leading to the destruction of the cancer cell .

Research has demonstrated that PNC-27 induces necrosis in breast cancer cells and interacts with MDM2 in human leukemia K562 cancer cells, causing pore formation and resulting in cell death . The peptide’s ability to bind to the cell membrane and lyse the cell makes it a promising candidate for cancer treatment .

Clinical trials for PNC-27 and its counterpart, PNC-28, have been successful . These immunotherapy agents have the ability to bind to the cell membrane and lyse the cell, ensuring that a relapse does not occur . Research illustrates that this form of immunotherapy can be a successful strategy in eliminating cancer and ensuring that a relapse does not occur .