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Matthew Pincus and colleagues at the State University of New York (SUNY) Downstate Medical Center, combining two functional domains into a single 32-residue sequence: The HDM-2-binding domain — p53 residues 12–26, derived from the amino-terminal transactivation domain of the p53 tumour suppressor protein that naturally binds to HDM-2 (human double minute 2, also known as MDM2) A transmembrane-penetrating (membrane residency) peptide (MRP) — derived from the Antennapedia homeodomain, fused to the C-terminus to enable membrane interaction and insertion upon target engagement What makes PNC-27 unique among anticancer research peptides is its proposed mechanism of action — rather than triggering intracellular apoptosis pathways (the mechanism of most conventional chemotherapeutic approaches), PNC-27 targets HDM-2 expressed on the outer plasma membranes of cancer cells, forming transmembrane pores that cause rapid necrotic cell death through a process researchers have termed “poptosis” (peptide-induced transmembrane pore formation)
