database / metabolic

AOD-9604

also known as hGH fragment 177-191 analogue

research compound metabolic metabolic modified — mass check n/a

126 heavy atoms · 251 bonds · drag to pan, scroll to zoom C78O23N23S2

Skeletal structure drawn from the computed atomic coordinates in PubChem CID 71300630. Carbons are implicit vertices; hydrogens on carbon are suppressed, as in any structural formula. Nothing here is estimated — every atom sits where PubChem placed it.

Research reference only. The observations below are recorded in the cited literature. Nothing here is advice or a recommendation, and no dosing information is published on this site.

Sequence

YLRIVQCRSVEGSCGF

Tyr-Leu-Arg-Ile-Val-Gln-Cys-Arg-Ser-Val-Glu-Gly-Ser-Cys-Gly-Phe

hydrophobic
positive
negative
polar
aromatic
glycine
proline
cysteine

Modified molecule. C-terminal fragment of human growth hormone (177-191) with an added N-terminal tyrosine; carries a disulfide bond.

Backbone carries modifications, so computed backbone mass is not comparable to the reported mass of the complete molecule.

Molecular data

Chemical fields come from the PubChem compound record; computed values are derived from the sequence shown above.
molecular formula	C78H123N23O23S2
molecular weight	1815.1 Da (PubChem)
computed backbone mass	1817.11 Da
length	16 residues
net charge (pH 7.4)	+1
mean hydropathy	0.3
half-life	not characterised
delivery route	not characterised
PubChem CID	71300630
PDB	not characterised
UniProt parent	P01241

Mechanism

Growth-hormone C-terminal fragment studied for lipolytic activity without the full GH receptor profile.

Reported targets: not established

Experimental structure

No experimental structure of this peptide is deposited in the PDB. Nothing is rendered here — a predicted fold would not be a structure, and this site does not draw one.

Parent protein

Derived from the C-terminal region of human growth hormone. UniProt P01241 · 217 aa

Reported effects

Each row is an outcome described in the literature indexed for this peptide. Reported in the cited work — not a claim, not a recommendation.

Reported observations and the corpus they are drawn from.
reported outcome	where it appears
lipolysis	Therapeutic Peptides in Orthopaedics: Applications, Challenges, and Future D… Journal of the American Academy of Orthopaedic Surgeons. Global research & reviews 2026
fat metabolism	Safety and Efficacy of Approved and Unapproved Peptide Therapies for Musculo… Sports medicine (Auckland, N.Z.) 2026

Literature (8)

Therapeutic Peptides in Orthopaedics: Applications, Challenges, and Future Directions — Journal of the American Academy of Orthopaedic Surgeons. Global research & reviews 2026

Therapeutic peptides are emerging as promising adjuncts in the management of orthopaedic injuries, grounded in their ability to modulate molecular signaling networks central to cellular medicine. By acting on key pathways such as PI3K/Akt, mTOR, MAPK, TGF-β, and AMPK, peptides exert influence over tissue regeneration, inflammation resolution, and neuromuscular recovery. Wound-healing peptides such as BPC-157, TB-500, and GHK-Cu promote angiogenesis, integrin-mediated extracellular matrix remodeling, and fibroblast activation, whereas growth hormone secretagogues like ipamorelin, CJC-1295, tesamorelin, sermorelin, and AOD-9604 activate IGF-1 signaling and satellite cell repair. Recovery-enhancing agents such as epithalon, delta sleep-inducing peptide, and pinealon target circadian and mitochondrial regulators, and neuroactive peptides like selank, semax, and dihexa enhance brain-derived n…

open access ↗ · PMID 41490200 · DOI 10.5435/jaaosglobal-d-25-00236

Safety and Efficacy of Approved and Unapproved Peptide Therapies for Musculoskeletal Injuries and Athletic Performance — Sports medicine (Auckland, N.Z.) 2026