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Molecular Weight
Purity
Storage
Appearance
Solubility
01
Adipotide, also known as FTPP (fat-targeted proapoptotic peptide), prohibitin-targeting peptide-1 or TP01, is a synthetic two-part peptide. A short, disulfide-cyclised homing sequence, CKGGRAKDC, is joined through a Gly-Gly spacer to a membrane-active sequence built entirely from D-amino acids, D(KLAKLAK)₂.
In the published literature, the homing sequence was identified for its binding to prohibitin (and annexin A2) on the blood vessels of white adipose tissue, while the D(KLAKLAK)₂ portion disrupts mitochondrial membranes once inside the cell. The compound was studied as an experimental agent in animal models; its clinical development has been discontinued. It is supplied here as a lyophilized reference material for in vitro research on targeted peptide design, disulfide-cyclised motifs and D-amino-acid peptide analysis.
02
Adipotide is made of two functional modules joined by a short linker, which gives it analytical features that single-domain peptides lack.
Cyclic homing domain, CKGGRAKDC
Residues 1–9 contain two cysteines that form an intramolecular disulfide, closing the segment into a loop. This ring accounts for the two sulfur atoms in the formula and gives the homing motif its defined shape.
Gly-Gly spacer
A flexible two-residue linker separates the homing loop from the effector so that each can work without blocking the other.
D(KLAKLAK)₂ effector
A 14-residue repeat of Lys-Leu-Ala-Lys-Leu-Ala-Lys, all in the D-configuration. It is amphipathic and strongly cationic, and the D-stereochemistry makes it resistant to proteases.
Overall charge
With eight lysines and one arginine, the peptide carries a high positive charge, which affects its chromatography and makes it prone to sticking to surfaces.
Across all 25 residues, the cyclic form is about 2 Da lighter than the reduced (open) form, because forming the disulfide removes two hydrogens.
03
The mechanism described for Adipotide comes from published cell-based and animal studies.
Vascular homing
The cyclic CKGGRAKDC motif, originally found by phage display, is reported to bind prohibitin, and in some studies annexin A2, on the endothelium of white adipose tissue blood vessels.
Mitochondrial disruption
After uptake, the D(KLAKLAK)₂ domain is described as inserting into mitochondrial membranes, releasing cytochrome c and triggering apoptosis of the targeted endothelial cells.
Published models
The peptide was first characterised in obese mouse models (Nature Medicine, 2004) and later in obese non-human primates (Science Translational Medicine, 2011). These studies are cited only as scientific background, not as claims about this material.
Characterisation of the reference material itself is limited to in vitro physicochemical analysis.
04
Disulfide characterisation
The single intramolecular disulfide of the homing loop is a model for reduced-versus-non-reduced mass comparison and reduction/alkylation workflows.
D-amino-acid analysis
The all-D effector domain is a reference for chiral analysis and protease-resistance studies, distinguishing D-configured motifs from L-versions.
Cationic peptide chromatography
Its strong positive charge makes it a useful test analyte for ion-pairing reversed-phase and cation-exchange method development.
Targeted-peptide design
A well-known example of a homing-plus-effector design, used for comparison in studies of other bipartite peptides.
05
Storage
Store the lyophilized powder at −20 °C, sealed, desiccated and protected from light. Long-term storage in solution is not recommended.
Disulfide integrity
The main structural risk is reduction or scrambling of the homing-loop disulfide. Avoid reducing agents (DTT, TCEP, free thiols) and prolonged exposure to basic pH.
Reconstitution
Soluble in water and dilute acetic acid. Add solvent slowly down the side of the vial and swirl rather than shake, as the peptide is surface-active and can foam.
Surface adsorption
The highly cationic effector domain sticks to glass and ordinary plastics at low concentrations. Use low-binding polypropylene tubes and tips.
Solutions
Prepare fresh or freeze single-use aliquots, and avoid repeated freeze–thaw cycles.
06
Adipotide combines the analytical needs of a disulfide-containing peptide with those of a strongly cationic, D-amino-acid sequence.
HPLC
Reversed-phase separation with 0.1% TFA as ion-pairing agent controls peak shape; 0.1% formic acid is used instead for LC-MS. Cation-exchange chromatography gives an independent check for charge variants.
Mass spectrometry
ESI-MS in positive mode gives a series of highly charged ions. The cyclic form matches about 2555.2 Da, and reduction adds about 2 Da, which confirms the disulfide.
Disulfide confirmation
Comparing reduced and non-reduced spectra, or reducing and alkylating the cysteines (about +57 Da each), verifies correct ring formation and rules out scrambled or dimeric species.
Impurity profile
Typical checks include reduced and mis-paired forms, deletion sequences from the repetitive KLAK units, and L-epimers in the effector domain.
07
They form a disulfide bond that closes the CKGGRAKDC homing sequence into a loop. This cyclic shape is what the literature links to its binding to adipose blood vessels, and it must be kept intact during handling and analysis.
D-amino acids are not recognised by most proteases, so the effector domain resists enzymatic breakdown. Its amphipathic, cationic sequence is what allows it to interact with membranes.
2557.2 g/mol is the reduced (open) form, which many suppliers quote. Forming the disulfide removes two hydrogens, giving about 2555.2 g/mol for the cyclic form. Check which form a certificate of analysis refers to.
By accurate mass of the cyclic form, MS/MS sequence confirmation, comparison of reduced and non-reduced spectra to verify the disulfide, and chiral analysis of the D-configured effector domain.
Dissolve in water or dilute acetic acid, adding the solvent slowly down the vial wall and swirling gently. Use low-binding polypropylene labware to limit adsorption of this highly cationic peptide.
Keeping the disulfide intact: avoid reducing agents, free thiols and basic pH, which can open or scramble the loop and destroy its defined structure.
No. It is supplied strictly as a reference compound for laboratory and analytical research and is not for human or animal use.
Adipotide Research Reference. (2026). Pure Peptides Labs Research Catalogue. Retrieved from https://purepeptideslabs.net/research-catalogue/metabolic-research-peptides/adipotide/
Materials listed on this platform are supported by independent testing and published documentation for laboratory research contexts.
