If you have been reading about WADA prohibited list and want a single page that covers the useful parts, this is it: definitions, context, how it is studied, and the questions that come up repeatedly.
Last reviewed on 2025-10-07. Where a claim depends on a specific study, the study is described rather than over-claimed.
Clinical development of AOD-9604 included trials in people with obesity. Reports from early-phase and mid-phase studies described modest or inconsistent changes in body weight. A phase IIb program did not meet its primary endpoint, and the compound was not approved for medical use. Differences in formulation, delivery route, and participant characteristics may explain some of the variation. Later investigations explored whether the peptide might have effects in other tissues, including cartilage.
Regulatory treatment of AOD-9604 is shaped by its classification as a peptide hormone. The World Anti-Doping Agency lists it as a prohibited substance, and many national anti-doping organizations adopt that list. It does not hold approval as a prescription medicine in the United States, the European Union, or other major markets. Products sold online are frequently labeled for research use only and may not undergo independent quality testing. Import and possession rules differ by country, so legal status depends on local law.
Proposed mechanisms for AOD-9604 focus on fat cells. Laboratory studies suggest the peptide can increase lipolysis, the breakdown of stored fat, and reduce lipogenesis, the formation of new fat. Unlike full human growth hormone, it does not appear to stimulate substantial IGF-1 production in the studies reported so far. Some evidence points to beta-adrenergic signaling, but the precise receptor targets and downstream pathways remain unresolved. The fragment is not thought to act through the classical growth hormone receptor.
Proposed mechanism focuses on lipolysis, the breakdown of stored triglycerides into free fatty acids and glycerol. AOD-9604 is thought to act on adipose tissue without stimulating appetite or affecting blood sugar in the same way as growth hormone. Laboratory studies report increased fat oxidation in some models. The precise receptor interactions and signaling pathways remain incompletely characterized. Researchers have proposed that the peptide may influence fat mobilization through pathways distinct from the full hormone.
Research has examined whether the peptide affects fat mass independently of growth hormone's other actions. Early animal studies suggested reductions in body fat, but species differences and small sample sizes limit interpretation. Human studies have generally been short and have not consistently shown large effects. Some trials measured body composition, lipid profiles, and safety parameters, but the overall picture is one of suggestive yet inconclusive metabolic activity. Findings vary across study populations and protocols.
| Property | Value | Notes |
|---|---|---|
| Typical storage temperature | -20 °C | Lyophilized peptide; protect from moisture and light. |
| Typical analytical method | HPLC and mass spectrometry | Used to confirm identity and estimate purity. |
| Common synonyms | AOD9604; hGH 176-191 | Naming varies by supplier and publication. |
| Disulfide bonds | One | Affects folded structure and stability. |
| Typical research purity | ≥95% | Value depends on supplier and analytical method. |
AOD-9604 is a synthetic peptide whose structure corresponds to a C-terminal segment of human growth hormone. It is often described as hGH fragment 176-191, a 16-amino-acid sequence. The peptide was designed to isolate a region of hGH associated with fat metabolism while avoiding the full hormone's growth-promoting actions. Laboratory and commercial materials typically present it as a lyophilized powder for research use. Its identity is defined by amino acid sequence, not by a single brand.
The fragment includes residues that can form an internal disulfide bond between two cysteine positions. This structural feature can influence how the peptide folds and how stable it is in solution. AOD-9604 differs from full-length hGH in size and receptor interactions; it does not contain the entire growth hormone sequence. Published descriptions sometimes use slightly different residue numbering, so sequence information should be checked against primary sources. The molecule is small compared with intact hGH, which affects analytical detection and purification approaches.
Interest in AOD-9604 arose from attempts to separate metabolic effects from growth effects attributed to hGH. Early work explored whether the fragment could influence lipolysis or fat oxidation without promoting growth. Those questions remain partly unresolved because human data are limited and results have varied across studies. The peptide is not a hormone replacement for hGH and is not equivalent to hGH in clinical use. Its research history includes both laboratory studies and commercial marketing claims that are not the same as regulatory approval.
AOD-9604 is typically supplied as a lyophilized white to off-white powder. In this form, it is relatively stable when kept cool, dry, and protected from light. Common storage recommendations place it at −20 °C or below for long-term retention. Reconstituted solutions are less stable and are often kept at 2–8 °C for short periods. Freeze-thaw cycles should be minimized because they can promote aggregation or loss of peptide content. Vials are usually sealed under inert gas to reduce oxidation.
Identity and purity are commonly checked with reversed-phase high-performance liquid chromatography and mass spectrometry. RP-HPLC separates the peptide from related impurities and can estimate purity by peak area. Mass spectrometry confirms molecular mass and helps detect sequence variants or truncations. Some laboratories use amino acid analysis or peptide mapping for additional characterization. No single method proves biological activity; these techniques establish chemical identity and purity only. They also require suitable reference standards for confident comparison.
Identity and purity are usually assessed with reversed-phase high-performance liquid chromatography and mass spectrometry. Reversed-phase HPLC separates the peptide from related impurities and can estimate purity by ultraviolet absorbance, while mass spectrometry confirms the molecular mass and detects modifications. Peptide mapping, amino acid analysis, and disulfide mapping may be used when the sequence or disulfide arrangement must be verified. Because AOD9604 contains cysteine residues, oxidation and disulfide isomers are possible quality concerns in synthetic batches.
Quality varies among research-grade suppliers, so certificates of analysis and independent testing are important for verification. A typical certificate reports purity by HPLC, identity by mass spectrometry, appearance, and sometimes residual solvents or water content. AOD9604 is often sold as a research chemical not intended for human consumption, and labels can be inaccurate. Common misconceptions include treating the peptide as a form of growth hormone, assuming supplement status, or expecting approved-drug quality from unregulated products.
Regulatory interest in AOD-9604 increased after high-profile anti-doping cases involving peptide products. In some cases, the substance was supplied under alternative names or in compounded preparations, complicating traceability. Sports tribunals and anti-doping panels have discussed whether the peptide was explicitly banned at the time of use, leading to clarifications by the World Anti-Doping Agency. For consumers and researchers, the legal status can vary by jurisdiction, and products marketed as research chemicals may lack independent quality verification.
AOD-9604 is listed as a prohibited substance in sport by the World Anti-Doping Agency. It falls under the peptide hormones, growth factors, related substances, and mimetics class on the prohibited list. Anti-doping organizations treat its presence in an athlete's sample as an adverse finding unless a therapeutic use exemption applies. The prohibition reflects concerns about performance enhancement in competitive settings and the difficulty of distinguishing exogenous peptide use from endogenous hormone fragments.
Detection of AOD-9604 in biological samples relies on analytical techniques capable of distinguishing a small synthetic peptide from related endogenous sequences. Liquid chromatography coupled with tandem mass spectrometry is commonly used for confirmatory analysis. Sample preparation may involve immunoaffinity enrichment or solid-phase extraction to concentrate the peptide. Because the molecule is small and may be present at low concentrations, assay sensitivity and specificity are ongoing analytical challenges. Laboratories also validate methods against reference materials when available.
== Bedeutung == Thiersch war einer der bedeutendsten Chirurgen des 19. Jahrhunderts in Deutschland. Seine erste wissenschaftliche Arbeit, die von der Pariser Akademie preisgekrönt wurde, beschäftigte sich mit der Übertragbarkeit der Cholera, wobei er während der Choleraepidemie in München 1854 getrocknete Choleradärme an Mäuse verfütterte und somit die Kontagiosität des Cholerastuhls nachwies. Seine 1865 erschienene Arbeit über den von ihm erstmals als „Epithelkrebs“ benannten Hautkrebs wies entgegen der Auffassung von Rudolf Virchow (1821–1902) nach, dass die bösartige Erkrankung aus Haut-, Schleimhaut- und Drüsenepithel entstehen kann, und schlug die Exzision der Krebsgeschwüre mit deutlichem Abstand vom sichtbaren kanzerösen Infiltrat vor. Im Jahr 1875 hatte er bereits eine Sigmaresektion zur Behandlung einer durch adenoides Gewebe verursachten Darmstenose durchgeführt. Mit Hilfe experimenteller Untersuchungen demonstrierte Thiersch grundlegende Vorgänge der Wundheilung („plasmatische Circulation“). Er führte als einer der ersten die Antisepsis nach Joseph Lister (1827–1912) in Deutschland ein und verwendete seit 1874 zu diesem Zweck statt Karbolsäure (Phenol) die ungiftigere Salicylsäure. Bahnbrechende chirurgische Behandlungsverfahren bei Missbildungen des Urogenitalapparates (Epi-, Hypospadie, Blasenektopie) stammen gleichfalls von Thiersch. Im Gegensatz zu Jacques Louis Reverdin (1842–1929), der dicke Hautstücke auf granulierende Flächen aufbrachte, erzielte Thiersch 1886 mit sehr dünnen Hauttransplantaten große Behandlungserfolge.
== Veröffentlichungen == Infektionsversuche an Tieren mit dem Inhalt des Choleradarmes. München 1865. Der Epithelialkrebs, namentlich der Haut. Eine anatomische-klinische Untersuchung. Leipzig 1865. Die feineren anatomischen Veränderungen nach Verwundung der Weichteile. In: Theodor Billroth, Franz von Pitha (Hrsg.): Handbuch der allgemeinen und speciellen Chirurgie., Bd. 1/2. 1867. Klinische Ergebnisse der Listerschen Wundbehandlung und über den Ersatz der Karbolsäure durch Salizylsäure. Sammlung klinischer Vorträge. 1875, S. 84–85. Über Hautverpflanzung. XV. Chirurgischer Kongress. Bd. 1. 17, 1886; XVII. Chirurgischer Kongress. Band 1. 66, 1888. Über Nervenextraktion, mit Vorzeigung von Instrumenten und ausgezogenen Nerven. XVIII. Chirurgischer Kongress. Bd. 1. 44, 1889.
== Literatur == Justus Thiersch: Thiersch, Karl. In: Allgemeine Deutsche Biographie (ADB). Band 55, Duncker & Humblot, Leipzig 1910, S. 255–263. Julius Pagel (Hrsg.): Biographisches Lexikon hervorragender Ärzte des 19. Jahrhunderts. Berlin 1901, S. 1704–1705. August Hirsch (Hrsg.): Biographisches Lexikon der hervorragenden Ärzte aller Zeiten und Völker. Band 5. Berlin 1929–1934, S. 556. H. Tillmanns: Zur Erinnerung an Carl Thiersch. In: Berliner Klinische Wochenschrift 32 (1895), S. 421–423. A. v. Bardeleben: Karl Thiersch. In: Deutsche Medizinische Wochenschrift 21 (1895), S. 311–312. A. Landerer: Carl Thiersch. In: Münchner Medizinische Wochenschrift 42 (1895), S. 472–475. Heinrich Helferich: Karl Thiersch. In: Deutsche Zeitschrift für Chirurgie 41 (1895), S. 617. Wilhelm His: Karl Ludwig und Karl Thiersch. Akademische Gedächtnisrede. Leipzig 1895. o. V.: Nekrolog Karl Thiersch. In: Virchows Archiv. Band 143, 1896, S. 679. Justus Thiersch: Carl Thiersch. Sein Leben. Leipzig 1922. Christian Schwokowski: Erinnerungen an Carl Thiersch – zum 100. Todestag. In: Zentralblatt für Chirurgie. Band 121, 1996, S. 426–429. Beatrice Hesse: Lebenssituationen und wissenschaftliches Werk von Carl Thiersch. Dissertation. Leipzig 1998. G. Dohm: Geschichte der Histopathologie. 2001, S. 555–561. Barbara I. Tshisuaka: Thiersch, Karl. In: Werner E. Gerabek u. a. (Hrsg.): Enzyklopädie Medizingeschichte. De Gruyter, Berlin / New York 2005, ISBN 3-11-015714-4, S. 1395. Dietrich von Engelhardt (Hrsg.): Biographische Enzyklopädie deutschsprachiger Mediziner. Band 2. 2002, S. 626. Eberhard J.
Sources: de.wikipedia.org
Literatur von und über Carl Thiersch im Katalog der Deutschen Nationalbibliothek Übersicht der Lehrveranstaltungen von Carl Thiersch an der Universität Leipzig (Wintersemester 1867 bis Sommersemester 1895) Carl Thiersch im Professorenkatalog der Universität Leipzig Carl Thiersch auf Google Books Eva Haberkorn: FAMILIENARCHIV CARRIÈRE - LIEBIG (= Repertorien Hessisches Staatsarchiv Darmstadt) Bestand O 12 (PDF; 914 kB). In: Archivinformationssystem Hessen (Arcinsys Hessen), Stand: Januar 2010, abgerufen am 16. September 2016. Der Nachlass befindet sich in der Bayerischen Staatsbibliothek Thiersch, Johanna. Hessische Biografie. In: Landesgeschichtliches Informationssystem Hessen (LAGIS). Edda Dammmüller: 20.04.1822 - Geburtstag des Chirurgen Carl Thiersch WDR ZeitZeichen vom 20. April 2017. (Podcast)
Sources: de.wikipedia.org
No. Major drug regulators have not approved AOD-9604 for weight loss or any other therapeutic indication. It remains an investigational compound studied in research settings.
The World Anti-Doping Agency classifies it as a prohibited peptide hormone. Athletes under anti-doping rules are not permitted to use it. Its presence can trigger a doping violation.
It is a fragment of growth hormone rather than a substance that signals the pituitary to release more hormone. Studies have not shown a consistent rise in IGF-1 or full growth hormone. Its metabolic effects, if any, appear separate from those of the complete hormone.
It is proposed to promote lipolysis in fat tissue, the breakdown of stored fat into fatty acids and glycerol. The detailed receptor and signaling mechanisms are not fully established.