{"id":71484,"date":"2026-05-20T10:05:00","date_gmt":"2026-05-20T10:05:00","guid":{"rendered":"https:\/\/medsbase.com\/pnc-27\/"},"modified":"2026-05-21T07:14:09","modified_gmt":"2026-05-21T07:14:09","slug":"pnc-27","status":"publish","type":"product","link":"https:\/\/medsbase.com\/ro\/product\/pnc-27\/","title":{"rendered":"PNC-27 (p53-HDM2 Membrane-Targeting Chimeric Peptide)"},"content":{"rendered":"

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Quick Answer \u2014 What is PNC-27?<\/h3>\n

PNC-27<\/strong> is a synthetic chimeric peptide (~32 amino acids) developed at Albert Einstein College of Medicine (Bowne, Pinto, Michl, Rauschmayer, Brower et\u00a0al.) that fuses two functional domains: an HDM2-binding helix<\/strong> derived from p53 transactivation-domain residues 12\u201326 (sequence PPLSQETFSDLWKLL) and a membrane-residency peptide (MRP)<\/strong> appended to anchor and disrupt cancer-cell plasma membranes. The mechanistic premise is that HDM2 (the human homologue of MDM2) is anomalously expressed on the plasma membrane surface<\/em> of cancer cells \u2014 not just in the nucleus where it normally degrades p53. PNC-27 binds the surface-exposed HDM2, the MRP domain then disrupts the lipid bilayer, and cancer cells undergo rapid membrane lysis and necrotic cell death. Published in pancreatic, leukaemia, breast cancer, and other tumour models. For laboratory research use only. Tumour-targeted membrane-disrupting chimeric peptide.<\/em><\/p>\n<\/div>\n

Ce beneficii ofer\u0103 MedsBase:<\/strong> Lyophilized \u226599% HPLC-verified PNC-27 chimeric peptide \u00b7 COA available on request \u00b7 Discreet temperature-stable packaging \u00b7 Worldwide research-supply courier \u00b7 1,400+ verified ale clien\u021bilor<\/a><\/div>\n

\ud83d\udce6 Fiecare comand\u0103 este acoperit\u0103 de politica noastr\u0103 de Politica noastr\u0103 de Reexpediere Garantat\u0103<\/strong><\/a> \u2014 dac\u0103 coletul dumneavoastr\u0103 nu sose\u0219te \u00een 20 de zile lucr\u0103toare, \u00eel relivr\u0103m.<\/p>\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n
Specifica\u021bii<\/th>\nDetaliu<\/th>\n<\/tr>\n<\/thead>\n
Clas\u0103 de compu\u0219i<\/strong><\/td>\nSynthetic ~32-aa chimeric peptide; tumour-targeted membrane-disrupting therapeutic peptide; HDM2-binding helix + membrane-residency peptide (MRP) chimera<\/td>\n<\/tr>\n
Denumire chimic\u0103<\/strong><\/td>\nPNC-27 (Peptide Nuclear Construct 27; synonyms: p53-MRP chimera, p53(12-26)-MRP construct)<\/td>\n<\/tr>\n
Num\u0103r CAS<\/strong><\/td>\nResearch-grade chimeric peptide \u2014 no single canonical CAS; identification by published sequence and supplier COA<\/td>\n<\/tr>\n
Secven\u021b\u0103<\/strong><\/td>\nN-terminal HDM2-binding helix (p53 transactivation residues 12\u201326): PPLSQETFSDLWKLL<\/strong>; linker; C-terminal membrane-residency peptide (MRP, sequence varies slightly across published references \u2014 researchers should consult COA for exact batch sequence). Total ~32 amino acids.<\/td>\n<\/tr>\n
Greutate molecular\u0103<\/strong><\/td>\n~3,800 Da (depending on exact MRP sequence)<\/td>\n<\/tr>\n
Formula molecular\u0103<\/strong><\/td>\n~32-residue chimeric peptide \u2014 sequence-derived approximate MF C173<\/sub>H278<\/sub>N52<\/sub>O43<\/sub>S; published MW ~3,800 Da (depending on exact membrane-residency-peptide linker; consult batch COA).<\/td>\n<\/tr>\n
Mecanism de ac\u021biune<\/strong><\/td>\nTumour-cell-selective membrane lysis<\/strong>. (1) PNC-27 binds HDM2<\/strong> on the plasma membrane of cancer cells. Normal cells express HDM2 only in the nucleus (where it ubiquitinates and degrades p53 to control p53 levels); cancer cells anomalously express HDM2 on the cell surface \u2014 a tumour-specific marker. (2) Once bound, the membrane-residency peptide (MRP) domain inserts into the lipid bilayer. (3) Multimerisation of bound PNC-27 molecules creates membrane pores \u2192 rapid necrotic cell death within minutes to hours. The mechanism is necrotic-membrane-lysis (NOT classical apoptosis) \u2014 distinguishing PNC-27 from caspase-pathway anticancer peptides.<\/td>\n<\/tr>\n
Tumour-Cell Selectivity<\/strong><\/td>\nPublished research has demonstrated selective cancer-cell killing in pancreatic adenocarcinoma, AML and ALL leukaemia, breast cancer, prostate cancer, melanoma, and other tumour models \u2014 with sparing of matched normal-cell controls that lack surface HDM2 expression.<\/td>\n<\/tr>\n
Form\u0103<\/strong><\/td>\nLyophilized white-to-off-white powder; single-use research vials<\/td>\n<\/tr>\n
Puritate<\/strong><\/td>\n\u226599% (HPLC verified, COA on request); MALDI-TOF mass-confirmed at the chimera-specific MW<\/td>\n<\/tr>\n
Depozitare<\/strong><\/td>\nLyophilized: 2\u20138 \u00b0C short-term, \u221220 \u00b0C long-term. Reconstituted: 2\u20138 \u00b0C, use within 30 days. Avoid repeated freeze-thaw.<\/td>\n<\/tr>\n
Utilizare \u00een cercetare<\/strong><\/td>\nFor laboratory research use only. Not for human or veterinary diagnostic or therapeutic use. PNC-27 is a preclinical research tool that has not entered formal clinical development. Not on the WADA Prohibited List.<\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n

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Mechanism of Action \u2014 HDM2-Targeted Membrane Lysis<\/h2>\n

PNC-27 was developed by the Bowne \/ Pinto \/ Michl \/ Rauschmayer group at Albert Einstein College of Medicine as an example of chimeric peptide drug design<\/strong> applied to oncology \u2014 pairing a tumour-targeting domain (the p53-derived HDM2-binding helix) with a generic killer domain (the membrane-residency peptide). The design logic:<\/p>\n