Compound monograph
AOD-9604
AOD-9604 is a synthetic, sixteen-residue human GH1 fragment analog specified with an N-terminal tyrosine, free termini and one intramolecular disulfide. AOD-9604 is used here as a provisional development-code name; an INN or USAN has not been established for this record.
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Identity & nomenclature
AOD-9604 is a synthetic, sixteen-residue human GH1 fragment analog specified with an N-terminal tyrosine, free termini and one intramolecular disulfide. AOD-9604 is used here as a provisional development-code name; an INN or USAN has not been established for this record.
AOD-9604 is specified as the tyrosine-extended human GH1 fragment Tyr-hGH(177-191), using the canonical mature-chain numbering. This is equivalent to replacing Phe176 with Tyr in hGH(176-191); the unqualified name “hGH fragment 176-191” can instead denote the distinct native phenylalanine-starting peptide and is not used here as an interchangeable identity.
Declared aliases and development codes: Tyr-hGH(177-191), AOD9604.
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Molecular properties
| Molecular formula | C78H123N23O23S2 |
|---|---|
| Molecular mass | 1815.1 Da |
| CAS Registry Number | 221231-10-3 |
| PubChem CID | 71300630 |
| UNII | 7UP768IP4M |
| One-letter sequence | YLRIVQCRSVEGSCGF |
| Three-letter sequence | Tyr–Leu–Arg–Ile–Val–Gln–Cys–Arg–Ser–Val–Glu–Gly–Ser–Cys–Gly–Phe |
| Terminal groups | Free N-terminus; Free C-terminal carboxyl |
Sixteen residues, using peptide positions 1-16. Two source conflicts remain unresolved. The 1993 native-fragment abstract (PMID 8358331) gives LRIVQCRVSEGSCGF, transposing Val and Ser at canonical mature GH1 positions 184-185 relative to LRIVQCRSVEGSCGF; these correspond to peptide positions 9-10 after the added Tyr. That paper describes the native fragment, not an independently established alternative AOD-9604 sequence. The FDA December 2024 briefing places the added Tyr at the N-terminus in its chemistry description and Figure 4, but its narrative on printed page 24 says C-terminus. The sequence here retains the specified N-terminal Tyr without resolving either conflict.
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Structural characteristics
The specified free peptide has a Cys7-Cys14 disulfide, a free N-terminal amino group and a free C-terminal carboxyl group. Spengler et al. (PMID 29953237) prepared this sixteen-residue chain, an N-terminal tyrosine followed by the fifteen C-terminal residues of human growth hormone, with a Cys7-Cys14 disulfide and free termini. The last fifteen residues correspond to positions 177-191 of the canonical mature human GH1 chain, with the historical sequence conflict retained in the sequence notes. The formula and identifiers describe the oxidized free peptide without a counterion; they do not describe its acetate species.
- Cys7-Cys14 disulfide
Ring closures: covalent bonds between residues, by position counted from the first residue of the chain.
- Disulfide Cys7–Cys14: thiol sulfur (Sγ) to thiol sulfur (Sγ). Source numbering: Cys182–Cys189 in mature human growth hormone (GH1) numbering. Source: PMID 29953237.
Terminal features: Free N-terminus, Free C-terminal carboxyl.
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Molecular targets & mechanisms
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Analytical considerations
Calculated average molecular mass is 1815.100 Da using CIAAW 2024 abridged atomic weights; calculated neutral monoisotopic mass is 1813.860360 Da using the specified isotope masses. These are distinct conventions. Formula and intact mass cannot distinguish Leu from Ile, D from L configuration, or residue order, including the Ser/Val transposition. Elemental composition alone also does not establish disulfide connectivity. The attached Cox reference documents analytical detection work on the named AOD9604 analyte; the accessible abstract is not used to certify every structural field.
Disagreements and mix-ups
Points where sources disagree about this compound's identity, or where a name or form is easily confused with another, as noted in this record. The discrepancy register quotes the passage for each one.
Sources disagree · unresolved · Sequence
Order of Val and Ser at peptide positions 9 and 10Sources disagree · unresolved · One source, two statements
Position of the added tyrosine within one FDA briefingOften mixed up · Name or substance
AOD-9604 is not the same as "hGH fragment 176-191"
What the studies reported
Each finding describes one cited study in its stated model. These observations are specific to that study and do not establish effects in other settings.
Cell and tissue studies
Serum and urine incubations
Cox et al. identified six potential AOD9604 metabolites after incubation in serum and urine in vitro.
Reference [1]Serum incubations
Cox et al. identified CRSVEGSCG as a stable AOD9604 metabolite in serum incubations in vitro.
Reference [1]
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Verified bibliography
Cited studies by type
The 2 papers this record cites, counted by the kind of work each reports. A count is the size of this record's selection, not of the research that exists, and says nothing about results, safety, effectiveness or approval.
A paper can report more than one kind of work. Each count opens those papers in the bibliography. Compare every record on the Evidence Map.
Reference 1
Detection and in vitro metabolism of AOD9604.Cox HD, Smeal SJ, Hughes CM, Cox JE, Eichner D
Drug testing and analysis · 2014-09-10 · Journal Article
currentReference 2
One-Pot Peptide Ligation-Oxidative Cyclization Protocol for the Preparation of Short-/Medium-Size Disulfide Cyclopeptides.Spengler J, Blanco-Canosa JB, Forni L, Albericio F
Organic letters · 2018-06-28 · Journal Article
current
Study models of these references
What kind of experiment each cited paper reports, taken from its abstract unless marked. Not a summary of results.
| Reference | Study models |
|---|---|
| Cox HD et al. 2014 | Study models reported: in vitro · from the abstract |
| Spengler J et al. 2018 | Chemical, structural or analytical study; no biological model reported |
Record history
Published 2026-09-27.
- : Sequence and structure, References
Each entry names the parts of this record that changed on that date. Changes to links between records and to catalogue links are not listed. This history covers the tracked record fields; study findings are not listed here.
Cite this record: Purely Peptides Research Library. AOD-9604. Published 2026-09-27; updated 2026-10-12. https://purelypeptides.org/research/compounds/aod-9604/
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Methodology & citation verification
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