A practical reference on AOD-9604: what it is, how it behaves, what the literature reports, and where the honest uncertainties sit.
This page was last updated on 2025-12-13 and is reviewed periodically as new material appears.
AOD-9604 is a synthetic peptide whose sequence matches the C-terminal fragment of human growth hormone, specifically residues 176 through 191. This region differs from the full hormone in its receptor interactions. The peptide is not a growth hormone secretagogue and does not bind the growth hormone receptor in the same manner. Researchers have examined it for effects on lipid metabolism, but its exact pharmacological profile remains an active area of study.
Development of AOD-9604 began in the 1990s as scientists sought to isolate metabolic effects of growth hormone without its growth-promoting actions. Early laboratory work focused on fat cells and animal models. Several human trials followed, examining changes in body composition and fat mass. Results have been mixed, and the peptide has not progressed to widespread clinical approval. Interest continues in research settings, particularly regarding its mechanism and potential metabolic targets.
Regulatory status varies by country. In the United States, AOD-9604 is not approved as a prescription drug. It is sometimes sold as a research chemical or dietary supplement, though such marketing may fall outside legal frameworks. The World Anti-Doping Agency prohibits its use in sport. Researchers must obtain it through legitimate suppliers and follow institutional rules. Its legal classification continues to evolve as authorities increasingly assess peptide products more broadly.
Regulatory bodies have taken different approaches to AOD-9604. It is not approved as a prescription medicine by major agencies such as the U.S. Food and Drug Administration or the European Medicines Agency. In sport, the World Anti-Doping Agency prohibits peptide hormones, growth factors, and related substances, and AOD-9604 has been treated as a prohibited substance. These regulatory decisions reflect concerns about safety, efficacy, and potential misuse rather than proof of benefit.
Research on AOD-9604 also examines how the peptide is measured in biological samples. Analytical methods may include liquid chromatography coupled with mass spectrometry, immunoassays, or both. Detection can be challenging because the peptide is small and may be present at low concentrations. Published methods vary in sensitivity and specificity, so comparative interpretation requires attention to validation details. The presence of related hGH fragments can complicate identification in some matrices.
| Property | Value | Notes |
|---|---|---|
| Molecular class | Peptide fragment | Corresponds to hGH residues 176-191 |
| Common synonyms | AOD9604, hGH 176-191 | Also written as AOD-9604 |
| Typical form | Lyophilized powder | Often supplied in sealed vials |
| Solubility | Water-soluble | Dissolves in aqueous buffers |
| Regulatory status | Not approved as drug | Banned in sport; varies by country |
AOD-9604 is a synthetic peptide whose sequence is modeled on the C-terminal region of human growth hormone. Published descriptions commonly place it as a modified fragment corresponding to hGH amino acids 176–191, with a tyrosine residue added or retained at the N-terminus to support detection and handling. It is not intact growth hormone and lacks the full receptor-binding architecture of the parent protein. The molecule was developed as a research candidate for metabolic studies rather than as a replacement for growth hormone therapy. Its identity is defined by its amino acid sequence rather than by any single commercial preparation.
AOD-9604 drew attention in the 1990s and 2000s as a potential anti-obesity agent. Early work explored both injectable and oral routes, which is unusual for a peptide of this size. Animal studies reported changes in fat metabolism without the growth-promoting or insulin-like effects associated with full-length growth hormone. Subsequent human trials produced mixed or modest results, and the compound did not obtain regulatory approval for weight management in major markets. It remains known mainly through research literature, sports anti-doping listings, and non-approved supplement advertising.
AOD-9604 is prohibited in sport by the World Anti-Doping Agency under the peptide hormone class. Its presence in a sample can be detected through mass spectrometry-based methods, although the exact assay depends on the laboratory. In research settings, material is often supplied as a lyophilized powder for reconstitution. Buyers and researchers should note that products labeled AOD-9604 may vary in purity and actual peptide content. Analytical certificates and independent testing are common ways to verify identity, but no global harmonized standard exists for all commercial lots.
AOD-9604 is a synthetic peptide modeled on the C-terminal region of human growth hormone. It is often described as hGH fragment 176-191. Research interest arose because it was designed to isolate possible effects on fat metabolism from other actions of growth hormone. It is not a full growth hormone molecule. Its development history includes early laboratory and animal studies followed by human trials. The peptide has been examined in laboratory, animal, and limited human studies.
The compound has been studied as a potential treatment for obesity and related metabolic conditions. Published trials have examined changes in body weight, fat mass, and safety markers over limited durations. Results have been mixed or modest, and no large-scale outcome trials are established. Regulatory agencies in several countries have not approved it as a therapeutic drug. Some commercial products have been marketed outside regulated pharmaceutical channels, which raises questions about quality and claims.
In the scientific literature, AOD-9604 appears in reviews of growth hormone fragments and in discussions of peptide-based metabolic research. Some sources distinguish it from growth hormone itself, while others group it with compounds marketed for weight management. The evidence base is small compared with approved obesity medications. Questions about long-term efficacy and clinical relevance remain open, and independent replication of key findings is limited. Most published reports are early-stage and exploratory.
=== Resistance === Three mechanisms of resistance to chloramphenicol are known: reduced membrane permeability, mutation of the 50S ribosomal subunit, and elaboration of chloramphenicol acetyltransferase. It is easy to select for reduced membrane permeability to chloramphenicol in vitro by serial passage of bacteria, and this is the most common mechanism of low-level chloramphenicol resistance. High-level resistance is conferred by the cat-gene; this gene codes for an enzyme called chloramphenicol acetyltransferase, which inactivates chloramphenicol by covalently linking one or two acetyl groups, derived from acetyl-S-coenzyme A, to the hydroxyl groups on the chloramphenicol molecule. The acetylation prevents chloramphenicol from binding to the ribosome. Resistance-conferring mutations of the 50S ribosomal subunit are rare. Chloramphenicol resistance may be carried on a plasmid that also codes for resistance to other drugs. One example is the ACCoT plasmid (A=ampicillin, C=chloramphenicol, Co=co-trimoxazole, T=tetracycline), which mediates multiple drug resistance in typhoid (also called R factors). As of 2014 some Enterococcus faecium and Pseudomonas aeruginosa strains are resistant to chloramphenicol. Some Veillonella spp. and Staphylococcus capitis strains have also developed resistance to chloramphenicol to varying degrees. Some other resistance genes beyond cat are known, such as chloramphenicol hydrolase, and chloramphenicol phosphotransferase.
S-adenosyl-L-homocysteine + [myelin basic protein]-Nomega-methyl-arginine Thus, the two substrates of this enzyme are S-adenosyl methionine and myelin basic protein-arginine, whereas its two products are S-adenosylhomocysteine and myelin basic protein-Nomega-methyl-arginine. This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:[myelin-basic-protein]-arginine Nomega-methyltransferase. Other names in common use include myelin basic protein methylase I, protein methylase I, S-adenosyl-L-methionine:[myelin-basic-protein]-arginine, and omega-N-methyltransferase.
dipole moment See electric dipole moment, magnetic dipole moment, molecular dipole moment, bond dipole moment, electron electric dipole moment, electron magnetic dipole moment, and nuclear magnetic moment.
=== As an antibiotic target === The sortases are thought to be good targets for new antibiotics as they are important proteins for pathogenic bacteria and some limited commercial interest has been noted by at least one company.
Sources: en.wikipedia.org
=== Direct === Antibodies that are specific for a particular protein (or group of proteins) are immobilized on a solid-phase substrate such as superparamagnetic microbeads or on microscopic agarose (non-magnetic) beads. The beads with bound antibodies are then added to the protein mixture, and the proteins that are targeted by the antibodies are captured onto the beads via the antibodies; in other words, they become immunoprecipitated.
A summary of the atomic-scale molecular dynamics simulations is then provided which contains important information as follows: 1) a system number that corresponds to a particular phospholipid simulation 2) the concentration of ethanol mol% used in a particular simulation 3) the concentration of ethanol (v/v%) used for the simulation 3) the ethanol/lipid ratio that is derived from the simulation 4) the area (nm2) of the phospholipid membrane which details the expansion of the membranes as the concentration of ethanol is increased 5) the thickness of the membrane which is based on the distance between the average positions of the phosphorus atoms on opposite sides of the phospholipid membrane and 6) the tilt of the head group of the POPC lipid based on changes in the angle towards the interior region of the phospholipid membrane which was surprisingly not very significant.
== Recent extraditions == On 29 April 2024, prominent El Mencho associate Juan Manuel Abouzaid El Bayeh, also known as "El Escorpion," was arrested in Mexico and then immediately extradited to the United States. On 27 February 2025, Antonio Oseguera was among 29 suspected Mexican drug trafficking figures who were extradited to the United States. In August 2025, Mexico extradited 26 individuals accused of involvement in major drug-trafficking organizations, including the CJNG and the Sinaloa Cartel, to the United States. The extraditions were conducted under U.S. pressure, with assurances that the death penalty would not be pursued. This marked the second large-scale extradition of alleged cartel members in 2025, following a similar transfer in February. These actions reflect ongoing cooperation between Mexico and U.S. authorities in combating transnational organized crime. Among those extradited included the imprisoned head of CJNG's Los Cuinis fraction, Abigael González Valencia.
Sources: en.wikipedia.org
AOD-9604 is a synthetic peptide fragment of human growth hormone, corresponding to amino acids 176-191. It is studied for potential effects on fat metabolism, but it is not approved as a drug in most countries. Its exact mechanism remains under investigation.
No, it is a small fragment of the full growth hormone protein. It does not appear to stimulate growth or increase growth hormone levels in the same way. Its actions are thought to be more limited to metabolic pathways.
Regulatory status varies. It is not approved for medical use in the United States or many other countries. It is banned in sport by WADA, and its sale as a supplement or research chemical may be subject to legal restrictions.
No. It is not approved as a therapeutic drug by major regulators. It is sold for research purposes in many settings, which is not the same as clinical approval.