{"id":71456,"date":"2026-05-20T12:05:00","date_gmt":"2026-05-20T12:05:00","guid":{"rendered":"https:\/\/medsbase.com\/adipotide-ftpp\/"},"modified":"2026-05-21T07:14:08","modified_gmt":"2026-05-21T07:14:08","slug":"adipotide-ftpp","status":"publish","type":"product","link":"https:\/\/medsbase.com\/nl\/adipotide-ftpp\/","title":{"rendered":"Adipotide (FTPP \u2014 Fat-Targeted Pro-apoptotic Peptide)"},"content":{"rendered":"

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Quick Answer \u2014 What is Adipotide (FTPP)?<\/h3>\n

Adipotide<\/strong> (also called FTPP<\/strong> \u2014 “Fat-Targeted Pro-apoptotic Peptide”) is a synthetic 25-amino-acid chimeric research peptide developed by Kolonin, Arap, and Pasqualini<\/strong> at MD Anderson Cancer Center. It fuses two functionally distinct domains: a cyclic homing peptide CKGGRAKDC<\/strong> that binds prohibitin-1 (and annexin A2) on the endothelium of white adipose tissue capillaries, and a D-stereoisomer pro-apoptotic \u03b1-helical peptide D(KLAKLAK)2<\/sub><\/strong> that disrupts mitochondrial membranes. The fused chimera selectively targets the vasculature feeding white adipose tissue and triggers endothelial apoptosis, starving adipocytes of blood supply and producing rapid fat-tissue mass loss. Published in obese rhesus monkeys (Barnhart et\u00a0al. 2011, Science Translational Medicine<\/em>) \u2014 ~11% body weight loss over 4 weeks. Caveat:<\/strong> documented nephrotoxicity in primate studies is the major translational limitation, and a Phase I human cancer trial (2014\u20132016) had limited published outcomes. For laboratory research use only.<\/p>\n<\/div>\n

Wat u krijgt bij MedsBase:<\/strong> Lyophilized \u226599% HPLC-verified powder \u00b7 COA available on request \u00b7 Discreet temperature-stable packaging \u00b7 Worldwide research-supply courier \u00b7 1,400+ verified klantbeoordelingen<\/a><\/div>\n

\ud83d\udce6 Elke bestelling is gedekt door onze Reshipment Assurance Policy<\/strong><\/a> \u2014 als uw pakket niet binnen 20 werkdagen arriveert, sturen wij het opnieuw.<\/p>\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n
Specificatie<\/th>\nDetail<\/th>\n<\/tr>\n<\/thead>\n
Compound Class<\/strong><\/td>\nSynthetic 25-amino-acid chimeric peptidomimetic; homing domain + pro-apoptotic domain joined by GG linker; fat-targeted pro-apoptotic peptide<\/em><\/td>\n<\/tr>\n
Chemical Name<\/strong><\/td>\nAdipotide \/ FTPP (Fat-Targeted Pro-apoptotic Peptide); synonyms: Prohibitin-targeting peptide-1 + D(KLAKLAK)2<\/sub> chimera; CKGGRAKDC-GG-D(KLAKLAK)2<\/sub><\/td>\n<\/tr>\n
CAS-nummer<\/strong><\/td>\nResearch-grade chimeric peptide \u2014 no single canonical CAS. Some supplier listings cite 1422956-49-3; identification primarily by published sequence (CKGGRAKDC-GG-D(KLAKLAK)2<\/sub>) rather than CAS. Consult COA for batch-specific identification.<\/td>\n<\/tr>\n
Sequentie<\/strong><\/td>\nCys-Lys-Gly-Gly-Arg-Ala-Lys-Asp-Cys (cyclised Cys1\u2013Cys9 disulfide, the “CKGGRAKDC” prohibitin-binding homing motif) \u2014 Gly-Gly linker \u2014 D-Lys-D-Leu-D-Ala-D-Lys-D-Leu-D-Ala-D-Lys-D-Lys-D-Leu-D-Ala-D-Lys-D-Leu-D-Ala-D-Lys (the D-stereoisomer pro-apoptotic \u03b1-helical peptide D(KLAKLAK)2<\/sub>). Total length: 25 amino acid residues (9 + 2 + 14).<\/td>\n<\/tr>\n
Moleculair gewicht<\/strong><\/td>\n~2,611 Da (calculated average; reported as 2,500\u20132,611 Da across published sources)<\/td>\n<\/tr>\n
Molecuulformule<\/strong><\/td>\nChimeric peptide \u2014 sequence CKGGRAKDC-GG-D(KLAKLAK)2<\/sub>; sequence-derived approximate MF ~C114<\/sub>H196<\/sub>N40<\/sub>O26<\/sub>S2<\/sub>; published MW ~2,611 Da (cyclic disulfide form). No single Sigma-canonical CAS; identification by sequence + COA.<\/td>\n<\/tr>\n
Werkingsmechanisme<\/strong><\/td>\nTwo-step targeted apoptosis<\/strong>. (1) The cyclic CKGGRAKDC homing domain binds prohibitin-1 \u2014 a mitochondrial chaperone-like protein that is unusually expressed on the surface<\/em> of capillary endothelial cells supplying white adipose tissue (identified by Kolonin et\u00a0al. 2004 in-vivo phage-display screen) \u2014 and also annexin A2 on the same vasculature. (2) Bound to the cell surface, the chimera is internalised, and the D(KLAKLAK)2<\/sub> \u03b1-helical pro-apoptotic domain disrupts the endothelial-cell mitochondrial membrane via direct membrane interaction. Mitochondrial collapse \u2192 caspase-mediated apoptosis of adipose vasculature \u2192 blood-supply starvation of adipocytes \u2192 adipose tissue mass loss over days to weeks.<\/td>\n<\/tr>\n
D-Amino-Acid Stereochemistry<\/strong><\/td>\nThe pro-apoptotic KLAKLAKKLAKLAK domain is synthesised exclusively in D-amino acid stereochemistry<\/strong> (mirror-image residues). The D-stereochemistry confers protease-resistance \u2014 host proteases recognise only L-amino acids \u2014 extending in-vivo half-life of the killer domain relative to the natural L-form. The homing domain (CKGGRAKDC) is in normal L-amino-acid stereochemistry because it needs to bind a host protein (prohibitin-1) in the canonical receptor-ligand geometry.<\/td>\n<\/tr>\n
Documented Toxicity (research-relevant)<\/strong><\/td>\nNefrotoxiciteit<\/strong> was documented in the obese-rhesus-monkey study (Barnhart et\u00a0al. 2011) and is the leading translational limitation. The kidney expresses prohibitin and is highly vascularised, so off-target homing of the chimera to renal vasculature produces dose-dependent renal injury. The MD Anderson group repositioned the compound for cancer rather than obesity precisely because the risk-benefit balance is more favourable in a cancer-treatment context than in an elective-fat-loss context. Researchers in any in-vivo protocol with Adipotide should include comprehensive renal-function monitoring (BUN, creatinine, urinalysis).<\/td>\n<\/tr>\n
Form<\/strong><\/td>\nLyophilized white-to-off-white amorphous powder; single-use research vials. Synthesis is technically demanding (D-amino-acid Fmoc-SPPS + cyclic disulfide closure of the homing domain) \u2014 purity grade matters more for this compound than for most.<\/td>\n<\/tr>\n
Zuiverheid<\/strong><\/td>\n\u226599% (HPLC verified); MALDI-TOF mass spectrometry confirms ~2,611 Da. Disulfide-bridge formation of the cyclic homing domain confirmed by reduced-vs-non-reduced mass comparison. COA available on request.<\/td>\n<\/tr>\n
Oplosbaarheid<\/strong><\/td>\nSoluble in bacteriostatic water, sterile water, and PBS at \u22652 mg\/mL; soluble in DMSO at \u226510 mg\/mL for in-vitro stock preparation. The amphipathic D(KLAKLAK)2<\/sub> domain has surfactant-like properties \u2014 solutions may show transient foaming on initial reconstitution; allow to settle before withdrawal.<\/td>\n<\/tr>\n
Opslag<\/strong><\/td>\nLyophilized: 2\u20138 \u00b0C unopened for short-term working stock; \u221220 \u00b0C for long-term storage (stable \u226536 months at \u221220 \u00b0C; \u226518 months at 2\u20138 \u00b0C). Reconstituted aqueous: 2\u20138 \u00b0C, use within ~30 days. Protect from light. Avoid repeated freeze\u2013thaw cycles \u2014 cumulative cycles risk Cys1\u2013Cys9 disulfide scrambling.<\/td>\n<\/tr>\n
Onderzoeksgebruik<\/strong><\/td>\nFor laboratory research use only. Not for human or veterinary diagnostic or therapeutic use. Adipotide is not on the current WADA Prohibited List under its specific name (its development arc went toward oncology rather than athletic-performance use). The compound has well-documented nephrotoxicity in primate studies and is not an FDA-approved therapeutic. Researchers in any in-vivo context must implement appropriate renal monitoring.<\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n

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What Is Adipotide \/ FTPP?<\/h2>\n

Adipotide<\/strong> (also called FTPP<\/strong> \u2014 “Fat-Targeted Pro-apoptotic Peptide”) is a synthetic 25-amino-acid chimeric peptidomimetic developed at the MD Anderson Cancer Center<\/strong> by Mikhail Kolonin, Wadih Arap, and Renata Pasqualini. The compound represents one of the cleanest examples of rational chimeric-peptide drug design<\/strong> in modern peptide pharmacology: a tissue-specific homing domain (identified by in-vivo phage display) is covalently fused to a generic killer domain (a pro-apoptotic mitochondrion-disrupting \u03b1-helical peptide), producing a chimera that delivers the killer activity selectively to the target tissue.<\/p>\n

The two functional domains and the design logic:<\/p>\n

1. CKGGRAKDC \u2014 the prohibitin-binding homing peptide.<\/strong> Kolonin et\u00a0al. (2004) used in-vivo phage-display screening in obese mice to identify a 9-residue cyclic peptide (sequence Cys-Lys-Gly-Gly-Arg-Ala-Lys-Asp-Cys, with a Cys1-Cys9 disulfide bridge that constrains the geometry) that selectively binds the vasculature of white adipose tissue. The binding target was subsequently identified as prohibitin-1<\/strong> (PHB1) \u2014 a normally mitochondrial-membrane-resident chaperone-like protein that, in white-adipose-tissue endothelium, is also expressed on the cell surface and accessible to circulating ligands. Annexin A2 has been identified as a secondary binding partner on the same vasculature. The CKGGRAKDC homing domain is the molecular zipcode that directs the chimera specifically to fat-tissue capillaries rather than to general systemic endothelium.<\/p>\n

2. D(KLAKLAK)2<\/sub> \u2014 the pro-apoptotic \u03b1-helical killer peptide.<\/strong> The 14-residue D-amino-acid \u03b1-helical peptide D-Lys-D-Leu-D-Ala-D-Lys-D-Leu-D-Ala-D-Lys-D-Lys-D-Leu-D-Ala-D-Lys-D-Leu-D-Ala-D-Lys is a synthetic membrane-disrupting peptide (originally developed in cancer-targeting research by Ellerby et\u00a0al. 1999). The amphipathic \u03b1-helical geometry causes the peptide to insert into membranes; the D-amino-acid stereochemistry confers protease-resistance in vivo. Crucially, the killer activity is niet<\/em> selective for any particular cell type \u2014 the peptide will disrupt mitochondrial membranes in essentially any cell it gets inside \u2014 which is why pairing it with a homing domain is necessary for therapeutic utility.<\/p>\n

3. GG linker.<\/strong> The two functional domains are joined by a simple di-glycine linker that provides flexible spacing and avoids steric interference between the homing and killer functions.<\/p>\n

The combined chimera (CKGGRAKDC-GG-D(KLAKLAK)2<\/sub>, ~2,611 Da) was characterised in obese rhesus monkeys in the landmark Barnhart et\u00a0al. (2011) paper in Science Translational Medicine<\/em> \u2014 animals lost approximately 11% body weight over 4 weeks of daily SC dosing, with concurrent improvements in insulin sensitivity. However, the same study and subsequent work documented dose-dependent nephrotoxicity<\/strong>: the kidney has high prohibitin expression and is densely vascularised, so off-target homing of the chimera to renal vasculature produces renal-cortex tubular damage. The MD Anderson group repositioned Adipotide for human oncology rather than obesity, and a Phase I clinical trial in patients with metastatic prostate cancer was conducted 2014\u20132016 with limited published outcomes. The compound remains a research tool today \u2014 extensively cited as a reference example of chimeric peptide drug design and the canonical pharmacological tool for studying targeted adipose-vascular apoptosis.<\/p>\n

Mechanism of Action \u2014 Tissue-Targeted Apoptosis of Adipose Vasculature<\/h2>\n

Adipotide’s mechanism is one of the most-characterised in chimeric-peptide pharmacology:<\/p>\n