Ipamorelin

Ipamorelin in brief

Ipamorelin is a synthetic pentapeptide amide, Aib-His-D-2-Nal-D-Phe-Lys-NH2 (711.9 g/mol), published in 1998 as NNC 26-0161 and an agonist at the growth hormone secretagogue receptor. Three of its five positions are non-proteinogenic, and it reaches the receptor without the fatty-acid group ghrelin requires. It released growth hormone from rat pituitary cells with a half-maximal concentration of 1.3 nmol/l and, unlike GHRP-6 and GHRP-2, did not raise corticotropin or cortisol in swine, which is the whole basis of its selectivity reputation. No affinity constant and no conformational measurement have been published. Development stopped at a phase 2 trial in postoperative ileus that reported no difference from placebo, and the FDA places it in category 2 of its bulk-substance safety list, citing serious adverse events including death identified in that same trial. Two laboratories have found a glycine-extended analogue in preparations sold under this name.^{[1,2,3,4,5,6,7]}

Ipamorelin regulatory status

No marketing authorisation for ipamorelin was found in Drugs@FDA (queried through openFDA), the EMA medicines database or the Health Canada Drug Product Database (searched November 2026), and the highest phase registered on ClinicalTrials.gov is phase 2, in postoperative ileus and gastrointestinal dysmotility; the postoperative ileus trial, NCT00672074, was sponsored by Helsinn Therapeutics (U.S.) and is recorded as completed. The 2026 WADA Prohibited List names ipamorelin among the growth hormone secretagogues in class S2.2.4, prohibited at all times. The FDA places ipamorelin acetate in category 2 under the 503B interim policy, its list of bulk substances that may present significant safety risks, citing possible immunogenicity from aggregation or peptide-related impurities, the added difficulty of characterising its unnatural amino acids, and serious adverse events including death identified in a published study of ipamorelin for gastric motility; the same page also lists it among nominations withdrawn by their nominators (page current as of 22 April 2026). The study the agency links to is that phase 2 trial, whose own abstract concludes the compound was well tolerated.^{[8,9,10,11,12,13,5,4]}

Ipamorelin at a glance

• A pentapeptide amide of 711.9 g/mol, C38H49N9O5, written Aib-His-D-2-Nal-D-Phe-Lys-NH2. Three of the five positions are outside the ordinary proteinogenic set: an achiral 2-aminoisobutyric acid cap, a D-naphthylalanine and a D-phenylalanine. No cysteine, no disulfide, no acyl chain, no metal.^[1,2]
• Reported in 1998 from a Novo Nordisk chemistry programme, as compound NNC 26-0161. It released growth hormone from primary rat pituitary cells with a half-maximal concentration of 1.3 nmol/l and a maximum 85 percent of that of GHRP-6, and the response was blocked by a secretagogue antagonist rather than by a growth hormone-releasing hormone antagonist.^[1]
• The one human kinetic dataset located is from 1999, in healthy male volunteers at five escalating exposure levels, eight men at each. It modelled dose-proportional kinetics with a terminal half-life of about 2 hours, a clearance of 0.078 L/h/kg and a steady-state volume of distribution of 0.22 L/kg, and a half-maximal stimulating concentration of 214 nmol/L, with growth hormone rising as a single episode peaking at 0.67 hours.^[14]
• The receptor it was profiled against was cloned in 1996 and its endogenous ligand was identified in 1999 as ghrelin, a 28-residue peptide whose activity requires an n-octanoyl group on serine 3. Ipamorelin reaches the same receptor with no acyl group at all, which is the structural question the molecule poses.^[15,3,1]
• It is a scaffold as much as a compound. Published chemistry names it as the lead that NN703, the 3-(aminomethyl)benzoyl tetrapeptides, the constrained-amine series and the NN703 hybrids were derived from, and two later groups built positron-emission tomography probes and boron-cluster conjugates on its backbone.^{[16,17,18,19,20,21]}
• Two laboratories independently identified Gly-ipamorelin, the same chain extended by one N-terminal glycine, in preparations labelled as growth hormone secretagogues. One confirmed the assignment against custom-synthesised material. A label naming this pentapeptide is a claim about a five-residue molecule and has been found to be wrong.^[6,22]
• Status and evidence base, in one place. There is no marketing authorisation anywhere, development stopped at a phase 2 trial that reported no difference from placebo, the compound is prohibited in sport at all times, and the FDA places it in category 2 of its bulk-substance safety list citing serious adverse events including death in that same trial. What exists as evidence: two human studies, a kinetic one and that trial; animal work in rats, mice, swine, ferret and fish; cell and cell-free work; and no receptor binding constant and no structure of any kind.^{[8,4,13,5,14,7]}

What is Ipamorelin?

Ipamorelin is a five-residue synthetic peptide that activates the growth hormone secretagogue receptor. The receptor came first: it was cloned from swine and human pituitary and hypothalamus in 1996 and shown to be the target of synthetic secretagogues, with its discoverers noting that its existence implied an undiscovered hormone. That hormone was purified from rat stomach three years later and named ghrelin, a 28-residue peptide carrying an n-octanoyl ester on serine 3 without which it does not act.^[15,3]

The compound was published in 1998 as the outcome of a chemistry programme, under the code NNC 26-0161. Its authors describe reaching it within a series of compounds from which the central Ala-Trp dipeptide of the earlier growth hormone-releasing peptides had been removed, which is why it carries five residues where GHRP-6 carries six and why it does not contain the Ala-Trp-(D-Phe)-Lys core that analytical work treats as this family common motif.^[1,16,23]

Its position in the literature is unusual for a peptide of this size. Four papers from the same programme describe it chiefly as a starting point: one series shrank it towards gastrointestinal absorption by replacing residues with a 3-(aminomethyl)benzoic acid fragment and N-methylating the backbone, another added constrained amines at the C-terminus after comparing it with NN703, and a third made hybrids of the two. Two unrelated groups later reused the backbone, for fluorine-18 imaging probes and for carborane conjugates. More published chemistry exists on molecules derived from ipamorelin than on ipamorelin itself.^{[17,16,18,19,20,21]}

Development reached a phase 2 trial in postoperative ileus, registered as NCT00672074 and reported in 2014, which stated no significant difference from placebo on its key or secondary efficacy analyses. That is cited here as the furthest point the molecule reached and for no other purpose. The names most often confused with it belong to a different receptor family: sermorelin, tesamorelin and the CJC-1295 forms act at the growth hormone-releasing hormone receptor, and in the 1998 work an antagonist of that receptor did not block what ipamorelin did to pituitary cells.^[4,1]

Its status is settled, and it is a stopped programme rather than an unexplored molecule. No marketing authorisation exists in Drugs@FDA, the European Medicines Agency medicines database or the Health Canada Drug Product Database. The furthest it reached was a phase 2 proof-of-concept trial in postoperative ileus after bowel resection, sponsored by Helsinn Therapeutics (U.S.) and registered as NCT00672074, which enrolled 117 patients between 2008 and 2009 and reported no significant difference from placebo on its key or secondary efficacy analyses. The 2026 World Anti-Doping Agency Prohibited List names it among the growth hormone secretagogues in class S2.2.4, prohibited at all times. And the FDA places ipamorelin acetate in category 2 of its list of bulk substances that may present significant safety risks, where the stated concern includes serious adverse events including death identified in that trial. The two readings of the same study do not agree and a reader should have both: the paper's own abstract concludes the compound was well tolerated and reports treatment-emergent adverse events in 87.5 percent of the ipamorelin group against 94.8 percent on placebo, while the agency, with the fuller record in front of it, names the harder finding.^{[8,9,10,11,4,13,5]}

Ipamorelin structure and sequence

The graph is short and almost every position in it is deliberate. Position 1 is 2-aminoisobutyric acid, an alpha carbon bearing two methyl groups, which makes the residue achiral and restricts the backbone angles available to it. Position 2 is L-histidine. Position 3 is D-alanine carrying a 2-naphthyl side chain, a fused bicyclic aromatic twice the size of a phenyl ring. Position 4 is D-phenylalanine. Position 5 is L-lysine whose C-terminal carboxylate has been replaced by a primary amide, leaving the side-chain amine free. Reading the registry stereodescriptors in order gives achiral, 2S, 2R, 2R, 2S.^[2,1]

Two of those features can be tied to measurements on neighbouring molecules rather than asserted. The adjacent D-residue pair at positions 3 and 4 is the arrangement that appeared when ghrelin was shortened from the other direction: replacing the third and fourth residues of a truncated ghrelin analogue with D-isomers was read by its authors as shaping the active geometry, with the N-terminal dipeptide acting as a spacer. The C-terminal end was tested by removal and restoration: a programme that stripped C-terminal pharmacophores out of this scaffold to improve gastrointestinal absorption found that putting a lysine mimetic and a naphthyl or biphenyl core back produced unexpectedly potent compounds, and a separate series added polar constrained amines there because comparing ipamorelin with NN703 suggested one was needed.^[24,19,18]

There is no three-dimensional view on this page and the reason is not a shortage of searching. The Protein Data Bank holds receptor-bound structures for ghrelin, GHRP-6, anamorelin, macimorelin and an orally active, non-peptide ghrelin-receptor agonist, and none for this molecule; PubChem holds no calculated conformer for it either, and no spectroscopic study of its solution shape was found. What the deposited structures establish bears on it only indirectly: they identify a pocket that accepts the octanoyl group of ghrelin and positions the peptide for activation, and they name a salt bridge and an aromatic cluster near the agonist site as recurring activation motifs. Ipamorelin has no acyl group to place in that pocket, and carries two bulky aromatic side chains in a four-bond span. How those are accommodated is an open structural question, not a described one.^{[7,2,25,26,3]}

Four of the five residues carry a defined configuration and the fifth has none. Reading the registry string residue by residue: the quaternary aminoisobutyric acid at position 1 is achiral, histidine 2 is 2S, the naphthylalanine at 3 is 2R, the phenylalanine at 4 is 2R, and lysine 5 is 2S. In the usual amino-acid convention that is L, D, D, L for positions 2 to 5. There is no cysteine, so no disulfide; no cyclisation, no lipid arm, no linker, no polyethylene glycol, no glycosylation and no metal coordination. The molecule carries no net charge in the registry record and has 19 rotatable bonds, which for a chain this short is a large fraction of its own skeleton.^[2,1]

What studies on Ipamorelin show

Each card names the experimental system and what was measured. A result in one system is not evidence about another.

What is established about ipamorelin at the growth hormone secretagogue receptor, and what is inferred from its neighbours

The receptor is a 366-residue class A G protein-coupled receptor, curated as coupling to Gq and producing diacylglycerol and inositol 1,4,5-trisphosphate, and as binding growth hormone releasing peptides including GHRP-6 as well as orally active non-peptide secretagogues. It is the receptor the 1998 work profiled ipamorelin against by antagonist exclusion, and the receptor whose antagonist abolished the measured responses to ipamorelin in the 2020 rat study. Those two experiments are the direct evidence that this molecule acts there; a radio-competitive binding assay at the same receptor did include ipamorelin, without an affinity figure in the accessible abstract.^[33,1,29,23]

What the structural work adds is a comparison rather than a picture. Cryo-electron microscopy of the receptor bound to ghrelin and to GHRP-6 identifies a pocket that receives the octanoyl group of ghrelin and guides the peptide into the activating position, and a second study with ghrelin and an orally active, non-peptide ghrelin-receptor agonist names a salt bridge and an aromatic cluster near the agonist site as motifs recurring across its agonists. Ghrelin loses activity without that acyl group. Ipamorelin never had one, and carries instead a naphthylalanine and a phenylalanine on adjacent D-residues, a plausible but untested candidate for engaging that aromatic cluster. No deposited structure contains this molecule, so the reading is inference from neighbours rather than a described binding mode.^[25,26,3,7]

Two observations complicate a single-site account, and both were made on relatives rather than on this compound. Radiolabelled NN703 and GHRP-6 accumulated substantially in the glandular stomach of the rat, and resecting the gastrointestinal tract reduced the growth hormone response to GHRP-6 by 60 to 70 percent while leaving the growth hormone-releasing hormone response intact, which the authors read as a second indirect route. Separately, an experiment in growth hormone-deficient mice found that part of what ipamorelin changed did not require growth hormone at all. The molecule has also been measured on tissue far from the pituitary: it reversed the inhibition of acetylcholine-induced and electrically stimulated contraction in isolated rat gastric fundus, and raised insulin release from isolated rat pancreatic fragments in a way reduced by calcium-channel and adrenergic blockers. Neither has been followed up structurally.^{[34,30,35,36,33]}

What is still unknown about Ipamorelin

There is no measured affinity for this molecule at its own receptor, which is the largest gap on the page. The 1998 half-maximal concentration of 1.3 nmol/l is a secretion potency in a pituitary cell preparation, and the same programme showed why the two must not be conflated: when NN703 was tested both ways, the inhibition constant from radioligand displacement at the human receptor did not match what its potency in rat pituitary cells predicted, and its potency on receptor-driven inositol phosphate turnover in those cells was lower than in rat pituitary cells. A radio-competitive assay at the receptor did include ipamorelin, without an itemised figure for it in the accessible abstract. So the compound best known for selectivity in this class has no published binding constant.^[1,37,23]

The selectivity claim is narrower than its reputation. What was measured was a panel of six pituitary hormones in conscious swine: follitropin, lutropin, prolactin and thyrotropin were unchanged by any secretagogue tested, and corticotropin and cortisol rose with GHRP-6 and GHRP-2 and not with ipamorelin at concentrations the authors describe as more than 200-fold above its half-maximal point for growth hormone release. That is a real negative result about six hormones in one species, and not a receptor screen. No broader off-target profiling was located, so the word selective in the original title describes the hormone panel rather than a surveyed receptorome.^[1]

Nothing experimental is known about the shape of the molecule. There is no deposited structure, no computed conformer in PubChem, and no circular dichroism or nuclear magnetic resonance study of the free peptide. Five residues with 19 rotatable bonds and a conformationally restricting aminoisobutyric acid cap is precisely the case where a measurement would decide something, and the structural literature on the receptor has accumulated instead around ghrelin, GHRP-6, anamorelin, macimorelin and an orally active, non-peptide ghrelin-receptor agonist.^[7,2,25,26]

Separately from that, much of the tissue-level work is unreplicated, and its most careful results are the negatives inside it. A bone study found mineral content raised by absorptiometry while volumetric density was unchanged by three independent methods. A rat pituitary culture study found secretion granule density raised with no change in the proportion of somatotroph cells. Neither has a second laboratory behind it, and in both the headline measurement and the controlling measurement point different ways, which is the pattern to look for when reading the rest of this literature.^[38,39]

The form in circulation is not fixed by the name. Three separate registry entries exist under acetate naming, with one, two and three acetates and masses of 771.9, 832.0 and 892.0 g/mol against 711.9 for the free peptide, and at least one published study specifies ipamorelin acetate as its material. Independently of salt form, two laboratories identified Gly-ipamorelin, a six-residue analogue, in preparations labelled as secretagogues. The analytical means to tell these apart exist: the intact pentapeptide is detectable in urine at 0.2 to 1 ng/mL by validated methods, and the fragment ipamorelin (1-4) free acid has been characterised. What does not exist is any study of what the glycine extension does at the receptor.^{[40,41,6,22,42,32]}

Key papers on Ipamorelin

1. Ipamorelin, the first selective growth hormone secretagogue.

   Raun K, Hansen BS, Johansen NL, Thøgersen H, Madsen K, Ankersen M, Andersen PH (1998), European Journal of Endocrinology · Primary study, cell-based secretion assay with antagonist profiling

   The discovery paper. It gives the sequence, the pituitary cell potency, the antagonist profiling that assigns the receptor, and the swine hormone panel that every later selectivity statement rests on. Read it for what it measured and for what it did not.

2. Ghrelin is a growth-hormone-releasing acylated peptide from stomach.

   Kojima M, Hosoda H, Date Y, Nakazato M, Matsuo H, Kangawa K (1999), Nature · Primary study, peptide purification and identification

   The endogenous ligand, and the reason the chemistry of this compound is interesting: ghrelin needs an n-octanoyl group on serine 3 to work, and ipamorelin has nothing of the kind.

3. Molecular recognition of an acyl-peptide hormone and activation of ghrelin receptor.

   Wang Y, Guo S, Zhuang Y, Yun Y, Xu P, He X, Guo J, Yin W, Xu HE, Xie X, Jiang Y (2021), Nature Communications · Structure paper, cryo-electron microscopy with mutagenesis

   The closest structural evidence available. Cryo-electron microscopy of the receptor with ghrelin and with the synthetic peptide GHRP-6, identifying the pocket that accepts the acyl group. It is the right paper to read precisely because it does not contain ipamorelin.

4. Pharmacological characterisation of a new oral GH secretagogue, NN703.

   Hansen BS, Raun K, Nielsen KK, Johansen PB, Hansen TK, Peschke B, Lau J, Andersen PH, Ankersen M (1999), European Journal of Endocrinology · Primary study, radioligand displacement and cell assays

   The clearest demonstration in this series that a secretion potency and a receptor affinity are different measurements, which is what makes the missing affinity figure for ipamorelin matter.

5. Analysis of new growth promoting black market products.

   Krug O, Thomas A, Malerød-Fjeld H, Dehnes Y, Laussmann T, Feldmann I, Sickmann A, Thevis M (2018), Growth Hormone & IGF Research · Primary study, structural characterisation by mass spectrometry

   Market-sourced material characterised by mass spectrometry, with Gly-ipamorelin confirmed against custom-synthesised reference. The practical identity paper for anything labelled with this name.

6. Metabolism of growth hormone releasing peptides.

   Thomas A, Delahaut P, Krug O, Schänzer W, Thevis M (2012), Analytical Chemistry · Primary study, metabolite identification by high-resolution mass spectrometry

   Where the molecule goes chemically. 28 metabolites across eight peptides of this class, all from exopeptidase, amidase or endopeptidase action, which makes the C-terminal amide an enzymatic target rather than a protective cap.

7. Growth hormone (GH)-independent stimulation of adiposity by GH secretagogues.

   Lall S, Tung LY, Ohlsson C, Jansson JO, Dickson SL (2001), Biochemical and Biophysical Research Communications · Primary study, genetic model with body composition measurement

   A clean experimental design: growth hormone-deficient mice separate what the receptor agonist does from what growth hormone does, and the two went in opposite directions on relative fat mass.

8. Prospective, randomized, controlled, proof-of-concept study of the Ghrelin mimetic ipamorelin for the management of postoperative ileus in bowel resection patients.

   Beck DE, Sweeney WB, McCarter MD; Ipamorelin 201 Study Group (2014), International Journal of Colorectal Disease · Randomised controlled trial

   The phase 2 trial, and it has to be read twice. Its own abstract reports no significant difference from placebo on the key and secondary efficacy analyses and concludes that the compound was well tolerated. The FDA cites this same study for serious adverse events including death, which the abstract does not report, and that pair of readings is the most important thing on this page.

9. Pharmacokinetic-pharmacodynamic modeling of ipamorelin, a growth hormone releasing peptide, in human volunteers.

   Gobburu JV, Agersø H, Jusko WJ, Ynddal L (1999), Pharmaceutical Research · Primary study, human pharmacokinetics and pharmacodynamics

   The only human kinetic data there is, and the figure worth carrying away from it: a modelled half-maximal stimulating concentration of 214 nmol/L against a 1.3 nmol/l potency in rat pituitary cells, which is the gap between a cell assay and a person.

References

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2. 2.PubChem. Compound Summary: CID 9831659, Ipamorelin. PubChem, National Center for Biotechnology Information. source · database record
3. 3.Kojima M, Hosoda H, Date Y, Nakazato M, Matsuo H, Kangawa K. (1999). Ghrelin is a growth-hormone-releasing acylated peptide from stomach. Nature. 402:656-660. doi:10.1038/45230 · abstract only
4. 4.Beck DE, Sweeney WB, McCarter MD; Ipamorelin 201 Study Group. (2014). Prospective, randomized, controlled, proof-of-concept study of the Ghrelin mimetic ipamorelin for the management of postoperative ileus in bowel resection patients. International Journal of Colorectal Disease. 29:1527-1534. doi:10.1007/s00384-014-2030-8 · abstract only
5. 5.U.S. Food and Drug Administration. (2026). Certain Bulk Drug Substances for Use in Compounding that May Present Significant Safety Risks (content current as of 22 April 2026). U.S. Food and Drug Administration, Human Drug Compounding. source · full text read
6. 6.Krug O, Thomas A, Malerød-Fjeld H, Dehnes Y, Laussmann T, Feldmann I, Sickmann A, Thevis M. (2018). Analysis of new growth promoting black market products. Growth Hormone & IGF Research. 41:1-6. doi:10.1016/j.ghir.2018.05.001 · abstract only
7. 7.RCSB Protein Data Bank. PDB entries 7F9Z (GHRP-6-bound ghrelin receptor in complex with Gq) and 7NA8 (Structures of human ghrelin receptor-Gi complexes with ghrelin and a synthetic agonist), with a full-text archive search for ipamorelin. RCSB Protein Data Bank. source · database record
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18. 18.Peschke B, Ankersen M, Bauer M, Hansen TK, Hansen BS, Nielsen KK, Raun K, Richter L, Westergaard L. (2002). The influence of conformational restriction in the C-terminus of growth hormone secretagogues on their potency. European Journal of Medicinal Chemistry. 37:487-501. doi:10.1016/s0223-5234(02)01370-3 · abstract only
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20. 20.Fowkes MM, Lalonde T, Yu L, Dhanvantari S, Kovacs MS, Luyt LG. (2018). Peptidomimetic growth hormone secretagogue derivatives for positron emission tomography imaging of the ghrelin receptor. European Journal of Medicinal Chemistry. 157:1500-1511. doi:10.1016/j.ejmech.2018.08.062 · abstract only
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23. 23.Ferro P, Krotov G, Zvereva I, Rodchenkov G, Segura J. (2017). Structure-activity relationship for peptídic growth hormone secretagogues. Drug Testing and Analysis. 9:87-95. doi:10.1002/dta.1947 · abstract only
24. 24.Matsumoto M, Kitajima Y, Iwanami T, Hayashi Y, Tanaka S, Minamitake Y, Hosoda H, Kojima M, Matsuo H, Kangawa K. (2001). Structural similarity of ghrelin derivatives to peptidyl growth hormone secretagogues. Biochemical and Biophysical Research Communications. 284:655-659. doi:10.1006/bbrc.2001.5014 · abstract only
25. 25.Wang Y, Guo S, Zhuang Y, Yun Y, Xu P, He X, Guo J, Yin W, Xu HE, Xie X, Jiang Y. (2021). Molecular recognition of an acyl-peptide hormone and activation of ghrelin receptor. Nature Communications. 12:5064. doi:10.1038/s41467-021-25364-2 · abstract only
26. 26.Liu H, Sun D, Myasnikov A, Damian M, Baneres JL, Sun J, Zhang C. (2021). Structural basis of human ghrelin receptor signaling by ghrelin and the synthetic agonist [an orally active, non-peptide ghrelin-receptor agonist]. Nature Communications. 12:6410. doi:10.1038/s41467-021-26735-5 · abstract only
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