AOD-9604 - Frequently Asked Questions

AOD-9604 is a synthetic 16-residue peptide, classed as an analogue of the C-terminal lipolytic domain of human growth hormone (residues 176-191) with an added N-terminal tyrosine. It is studied in adipocyte and rodent models as a tool for examining that fragment's metabolic signaling. All description here is in-vitro and preclinical; no therapeutic or human claim is made.

The sequence is Tyr-Leu-Arg-Ile-Val-Gln-Cys-Arg-Ser-Val-Glu-Gly-Ser-Cys-Gly-Phe, sixteen residues. Fifteen correspond to the hGH 176-191 C-terminal lipolytic domain, with an added N-terminal tyrosine.

The molecular weight is 1815.06 g/mol and the molecular formula is C78H123N23O23S2. The two sulfur atoms correspond to the two cysteine residues that form a single intramolecular disulfide bond.

The CAS registry number is 221231-10-3, the unique identifier used to confirm the identity of AOD-9604 reference material.

In adipocyte and rodent models it reproduces lipolytic (fat-mobilizing) signaling associated with the parent hormone's C-terminal fragment without engaging the growth-hormone receptor. Mechanistic work associates its lipolytic readout with up-regulation of beta-3 adrenergic receptor signaling rather than direct GH-receptor agonism.

No. A defining feature noted in the dataset is that it produces a lipolytic signaling readout without stimulating IGF-1 production in models, which is what separates the fragment's metabolic signaling from the IGF-1 output of classical GH-receptor activation.

Because it is modeled only on the C-terminal lipolytic domain of growth hormone (residues 176-191) rather than the full hormone, it lacks the structural surfaces required for classical GH-receptor agonism, so in the cited models its metabolic signaling is GH-receptor-independent.

The two cysteines form an intramolecular disulfide bond that constrains the fragment's conformation, locking the peptide into a defined three-dimensional shape rather than a freely flexible chain. This conformational constraint is the key structural feature in its structure-activity description.

Three areas are specified: adipocyte lipolysis-signaling models focused on the beta-3 adrenergic pathway; GH-receptor-independent metabolic-fragment studies; and structure-activity work on the hGH 176-191 domain it is modeled on.

The primary citation is Heffernan, M. A., et al. (2001), 'The effects of human GH and its lipolytic fragment (AOD9604) on lipid metabolism following chronic treatment in obese mice and beta(3)-AR knock-out mice,' Endocrinology (DOI 10.1210/endo.142.12.8522; PMID 11713213). It is a rodent lipid-metabolism study that connects the lipolytic readout to the beta3-AR pathway.

Lyophilized reference material is dissolved by adding a defined volume of solvent (commonly bacteriostatic water) to a vial of known peptide mass; the resulting stock concentration equals mass divided by volume. For example, 2 mL added to a 5 mg vial gives 2.5 mg/mL. The solution should be added gently down the vial wall, not shaken, then stored cold and light-protected. This is laboratory preparation only, not a human dosing protocol.

No compound-specific half-life, clearance, or degradation figure is provided in this dataset. The only documented stability-relevant feature is the conformation-constraining intramolecular disulfide. General small-peptide-class handling principles (cold storage, light protection, minimized freeze-thaw) are stated as conventions, not as AOD-9604-specific measurements.