The short version of peptide research fits in a sentence. The long version — which is the one that helps — is below.
This page was last updated on 2026-03-15 and is reviewed periodically as new material appears.
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 corresponds to residues 176-191 of the 191-amino-acid hGH sequence. The fragment is not the full hormone and lacks the receptor-binding region associated with growth and metabolic effects of hGH. Researchers developed it to isolate a specific portion of hGH for study. Its exact sequence and length are often stated in peptide catalogs and patents.
The peptide is frequently described as a growth hormone fragment, although it is chemically distinct from full-length hGH. AOD-9604 contains 16 amino acids and includes two cysteine residues that can form an intramolecular disulfide bond. In solution, this structural feature can influence folding, aggregation, and stability. Published descriptions sometimes call it hGH 176-191 or AOD9604, with spacing and capitalization varying. Such naming differences can complicate literature searches, database entries, and product verification.
| Property | Value | Notes |
|---|---|---|
| Molecular class | Synthetic peptide | Fragment analog of human growth hormone |
| Sequence basis | hGH 176–191 region | Modified C-terminal fragment |
| Common synonyms | AOD-9604; AOD9604; hGH fragment | Research and trade names vary |
| Regulatory status | Not approved as a drug | Prohibited in competitive sport |
| Research code | AOD9604 | Used in scientific and patent literature |
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.
Clinical development of AOD9604 included trials in people with obesity, but the results did not lead to approval as a prescription medicine in major markets. Interest later shifted to research settings and to unapproved products marketed for body composition. Regulatory agencies have questioned whether the peptide qualifies as a dietary ingredient, and some have issued warnings about its presence in supplements. Long-term human safety data are limited, and questions about efficacy, dosing, and target populations remain unresolved.
AOD9604 is a synthetic peptide modeled on the C-terminal region of human growth hormone. It corresponds to a short sequence near the end of the 191-amino-acid hormone, often described as residues 176–191 or a related fragment. Researchers designed it to separate metabolic effects from the growth-promoting actions of full-length growth hormone. Early work in the 1990s explored it as a candidate for weight and lipid disorders. It is not a naturally circulating hormone fragment produced in large amounts.
Laboratory studies have reported that AOD9604 can increase lipolysis and reduce lipid accumulation in fat cells. The precise molecular target remains uncertain, and the compound does not appear to activate the growth hormone receptor in the same way as full-length hGH. Proposed mechanisms include effects on beta-adrenergic signaling and enzymes involved in fatty acid synthesis, but these pathways are not firmly established. Because most evidence comes from cell and animal models, whether the same effects occur in humans is an open question.
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.
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.
== Function == Exercise causes increased expression in muscle of peroxisome proliferator-activated receptor gamma coactivator 1 alpha (PGC-1alpha), which is involved in adaptation to exercise. In mice, this causes production of the FNDC5 protein which is cleaved to give a new product irisin. Due to its production through a mechanism initiated by muscular contraction, irisin has been classified as a myokine.
One of the major switches for neuronal activity is the activation of PKs and PPs by elevated intracellular calcium. The degree of activation of the various isoforms of PKs and PPs is controlled by their individual sensitivities to calcium. Furthermore, a wide range of specific inhibitors and targeting partners such as scaffolding, anchoring, and adaptor proteins also contribute to the control of PKs and PPs and recruit them into signalling complexes in neuronal cells. Such signalling complexes typically act to bring PKs and PPs in close proximity with target substrates and signalling molecules as well as enhance their selectivity by restricting accessibility to these substrate proteins. Phosphorylation events, therefore, are controlled not only by the balanced activity of PKs and PPs but also by their restricted localisation. Regulatory subunits and domains serve to restrict specific proteins to particular subcellular compartments and to modulate protein specificity. These regulators are essential for maintaining the coordinated action of signalling cascades, which in neuronal cells include short-term (synaptic) and long-term (nuclear) signalling. These functions are, in part, controlled by allosteric modification by secondary messengers and reversible protein phosphorylation. It is thought that around 30% of known PPs are present in all tissues, with the rest showing some level of tissue restriction.
=== Post-mastectomy procedures === Surgical post-mastectomy breast reconstruction requires general anaesthesia, cuts the chest muscles, produces new scars, and requires a long post-surgical recovery for the patient. The surgical emplacement of breast implant devices (saline or silicone) introduces a foreign object to the patient's body (see capsular contracture). The TRAM flap (Transverse Rectus Abdominis Myocutaneous flap) procedure reconstructs the breast using an autologous flap of abdominal, cutaneous, and muscle tissues. The latissimus myocutaneous flap employs skin fat and muscle harvested from the back, and a breast implant. The DIEP flap (Deep Inferior Epigastric Perforators) procedure uses an autologous flap of abdominal skin and fat tissue.
Sources: en.wikipedia.org
G6PD is generally found as a dimer of two identical monomers (see main thumbnail). Depending on conditions, such as pH, these dimers can themselves dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold. For some higher organisms, such as humans, G6PD contains an additional NADP+ binding site, called the NADP+ structural site, that does not seem to participate directly in the reaction catalyzed by G6PD. The evolutionary purpose of the NADP+ structural site is unknown. As for size, each monomer is approximately 500 amino acids long (514 amino acids for humans). Functional and structural conservation between human G6PD and Leuconostoc mesenteroides G6PD points to three widely conserved regions on the enzyme: a nine-residue peptide in the substrate binding site, RIDHYLGKE (residues 198–206 on human G6PD), a nucleotide-binding fingerprint, GxxGDLA (residues 38–44 on human G6PD), and a partially conserved sequence EKPxG near the substrate binding site (residues 170–174 on human G6PD), where we have use "x" to denote a variable amino acid. The crystal structure of G6PD reveals an extensive network of electrostatic interactions and hydrogen bonding involving G6P, three water molecules, three lysine residues, one arginine, two histidines, two glutamic acids, and other polar amino acids. The proline at position 172 is thought to play a crucial role in positioning Lys171 correctly with respect to the substrate, G6P.
National Commission on Terrorist Attacks Upon the United States—Official commission website List of victims September 11, 2001, Documentary Project from the U.S. Library of Congress, Memory.loc.gov September 11, 2001, Web Archive from the U.S. Library of Congress The September 11th Sourcebooks at The National Security Archive September 11 Digital Archive: Saving the Histories of September 11, 2001, from the Center for History and New Media and the American Social History Project/Center for Media and Learning The 9/11 Legacies Project, Oriental Institute, Czech Academy of Sciences, Prague 9/11 at 20: A Week of Reflection; Archived April 16, 2022, at the Wayback Machine, Quincy Institute for Responsible Statecraft September 11, 2001 collection at the Smithsonian National Museum of American History Multimedia
== Early life and education == Born in Thuine, Lower Saxony, he studied mathematics and physics at the University of Göttingen. He received his Ph.D. in 1988 at Yale University where he worked in the group of John Fenn, who was later awarded the Nobel Prize in Chemistry.
=== Pharmacokinetics === When inhaled, dimethocaine starts working in 10–30 minutes, with highest effects at 60–120 minutes and until 4–6 hours there is a period of action with the 'after-effects'. The after effects include fatigue and slight mental impairment.
Sources: en.wikipedia.org
No. It is a synthetic peptide fragment modeled on part of human growth hormone, not the full hormone. It does not contain the complete sequence or receptor-binding regions of hGH.
It was investigated in clinical trials for obesity, but it did not receive approval for that use in major markets. Results were generally modest or mixed, and it remains an experimental compound.
WADA lists it as a prohibited peptide hormone. Its use can be detected by laboratory methods, and athletes are subject to sanctions if it is found in samples.
No, it is a synthetic peptide fragment corresponding to a small portion of hGH. It is not the full 191-amino-acid hormone and does not reproduce all of hGH's effects.