If you have been reading about secretagogue 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.
Updated 2025-12-08. Numbers and descriptions here follow the published literature rather than marketing material.
The molecule contains five residues, including alpha-aminoisobutyric acid, D-2-naphthylalanine, and D-phenylalanine, and it ends in a lysine amide. Non-natural and D-configured residues make the chain less susceptible to common peptidases, which helps explain its resistance to rapid breakdown. Its molecular formula is C38H49N9O5, corresponding to a free-base mass near 711.9 daltons. The C-terminal amide removes a negative charge and is a recurring feature in receptor-active peptides of this family. These structural choices are usually discussed as the basis for its selectivity profile.
Published animal and early human work describes growth hormone release that is separated from comparable rises in adrenocorticotropic hormone and cortisol. Prolactin changes are reported as small in the same studies. Selectivity is attributed to binding at the ghrelin receptor and to the downstream signaling that follows, rather than to differences in how quickly the peptide is cleared. Authors commonly label the compound selective rather than potent, because the same mass produces a smaller growth hormone response than some older secretagogues tested in parallel. Whether that profile holds across species and routes of administration remains an open question.
Identity and purity are assessed by complementary methods rather than a single test. Reversed-phase high-performance liquid chromatography separates the peptide from related impurities and reports a percentage purity. Mass spectrometry, most often with electrospray ionization, confirms the expected molecular mass and detects sequence-related variants. Amino acid analysis can verify composition, while water content and residual counterion measurements support the mass balance of a batch. Stability studies under accelerated conditions are used to estimate shelf life, though such estimates carry uncertainty for long-term storage.
Material supplied for research use is normally a white to off-white lyophilized powder. The solid is hygroscopic and is handled in a low-humidity environment to limit water uptake. Bulk quantities are frequently shipped in sealed vials under inert gas. Once reconstituted in water or a neutral buffer, the solution is less stable than the dry powder and is usually divided into single-use aliquots.
| Property | Value | Notes |
|---|---|---|
| Molecular formula | C38H49N9O5 | Value for the free base |
| Molar mass | 711.9 g/mol | Calculated from the formula |
| Appearance | White to off-white powder | Typical lyophilized form |
| Mechanism class | Ghrelin receptor agonist | Also described as a secretagogue |
| Half-life | About 2 hours | Reported for human circulation |
Activity is mediated mainly through the growth hormone secretagogue receptor, now generally called the ghrelin receptor or GHS-R1a. Binding at this G-protein-coupled receptor triggers phospholipase C signaling, calcium mobilization, and release of growth hormone from pituitary somatotrophs. Reports describe less pronounced stimulation of adrenocorticotropic hormone and prolactin compared with earlier secretagogues such as hexarelin or GHRP-6. Selectivity figures vary between assay systems, so the degree of separation from other secretagogues is an area of ongoing comparison rather than a fixed constant.
In animal and early human studies, ipamorelin produces pulsatile growth hormone release and a secondary rise in insulin-like growth factor 1. The magnitude and duration of that rise depend on route, sampling schedule, and the baseline endocrine state of the subject. Whether repeated exposure alters the response over time is not firmly settled, since some reports describe stable pulsatility while others note attenuation. Most published data come from small samples, which limits the strength of any general claim about long-term behavior.
Ipamorelin is a synthetic pentapeptide that belongs to the growth hormone secretagogue class of compounds. Its sequence is Aib-His-D-2-Nal-D-Phe-Lys-NH2, a structure that differs from natural ghrelin in length and in the presence of non-natural amino acid residues. Early laboratory work described it as a comparatively selective agent that stimulates growth hormone release with limited effect on other pituitary hormones. The compound is supplied as a lyophilized solid for research use and has no identified natural source in the body.
Structural features distinguish the molecule from earlier secretagogues. An alpha-aminoisobutyric acid residue near the N-terminus and a D-naphthylalanine substitution increase receptor affinity, while C-terminal amidation improves resistance to exopeptidases. These modifications are associated with reduced stimulation of appetite and of the hypothalamic-pituitary-adrenal axis compared with hexarelin or growth hormone releasing peptide-6. Whether the same profile applies at every dose level studied is a matter of ongoing investigation rather than settled consensus.
Ipamorelin is a synthetic pentapeptide that acts as an agonist at the ghrelin receptor, also called the growth hormone secretagogue receptor type 1a. Its sequence incorporates non-natural residues, which slows enzymatic breakdown relative to short native peptides. In laboratory and early clinical work the compound is described as a selective growth hormone secretagogue because it raises growth hormone with comparatively little effect on other pituitary outputs. The degree to which that selectivity holds across species and dosing regimens remains an open question in the published literature.
At the molecular level, ipamorelin acts as an agonist at the growth hormone secretagogue receptor, also called the ghrelin receptor or GHS-R1a. Binding to this receptor on pituitary somatotroph cells triggers a signaling cascade that leads to growth hormone release. The effect is mediated through phospholipase C and calcium mobilization rather than through the cyclic AMP pathway used by growth hormone releasing hormone. The two pathways are complementary, and combined stimulation produces a larger response than either alone.
Compared with other secretagogues such as GHRP-2, GHRP-6, and hexarelin, ipamorelin is described as more selective. Published animal work reports little or no increase in adrenocorticotropic hormone, cortisol, or prolactin at doses that release growth hormone. This selectivity is the property most often cited in the research literature. Whether the same profile holds across species and dosing schedules remains an open question, since human data are limited and come largely from small studies.
Ipamorelin is a synthetic pentapeptide that acts on the growth hormone secretagogue receptor, also known as the ghrelin receptor. Its sequence contains five amino acid residues, including a non-natural residue that increases stability against enzymatic breakdown. The compound was developed in the 1990s as part of research into small peptides that stimulate pituitary hormone release. Unlike larger protein hormones, it can be produced by solid-phase peptide synthesis and characterized by standard analytical methods.
At the receptor level, ipamorelin binds GHS-R1a and triggers signaling through Gq-coupled pathways. Activation leads to calcium release and downstream effects in pituitary somatotroph cells. These events promote the release of growth hormone into circulation. The response depends on the presence of the receptor and on the physiological state of the animal or tissue studied. Because the receptor is also found in other tissues, effects beyond the pituitary have been examined in laboratory models, though the extent of those effects remains an area of ongoing study.
The variation in the 14C/12C ratio in different parts of the carbon exchange reservoir means that a straightforward calculation of the age of a sample based on the amount of 14C it contains will often give an incorrect result. There are several other possible sources of error that need to be considered. The errors are of four general types:
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Nitrate reductase (NADPH) (EC 1.7.1.3, assimilatory nitrate reductase, assimilatory reduced nicotinamide adenine dinucleotide phosphate-nitrate reductase, NADPH-nitrate reductase, assimilatory NADPH-nitrate reductase, triphosphopyridine nucleotide-nitrate reductase, NADPH:nitrate reductase, nitrate reductase (NADPH2), NADPH2:nitrate oxidoreductase) is an enzyme with systematic name nitrite:NADP+ oxidoreductase. This enzyme catalises the following chemical reaction
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Sources: en.wikipedia.org
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== Selected publications == Góngora-Benítez M, Tulla-Puche J, Albericio F (2014). Multifaceted roles of disulfide bonds. Peptides as therapeutics. Chemical Reviews. doi:10.1021/Cr400031Z Subirós-Funosas R, Prohens R, Barbas R, El-Faham A, Albericio F (2010). Oxyma: an efficient additive for peptide synthesis to replace the benzotriazole-based HOBt and HOAt with a lower risk of explosion. Chemistry (Weinheim An Der Bergstrasse, Germany). doi:10.1002/Chem.200900614 Ruiz-Sanchis P, Savina SA, Albericio F, Álvarez M. Structure, bioactivity and synthesis of natural products with hexahydropyrrolo[2,3-b]indole. Chemistry (Weinheim An Der Bergstrasse, Germany). doi:10.1002/Chem.201001451 El-Faham A, Albericio F (2011). Peptide coupling reagents, more than a letter soup. Chemical Reviews. 111: 6557-602. doi:10.1021/Cr100048W Isidro-Llobet A, Alvarez M, Albericio F (2009). Amino acid-protecting groups. Chemical Reviews. doi:10.1021/Cr800323S Bruckdorfer T, Marder O, Albericio F (2004). From production of peptides in milligram amounts for research to multi-tons quantities for drugs of the future. Current Pharmaceutical Biotechnology. doi:10.2174/1389201043489620
Sources: en.wikipedia.org
It has not been approved as a therapeutic by major regulators, and the human trial record is small and dated. Material available today is mostly sold as a research chemical for laboratory use. Approval and restriction status varies by country.
It binds the ghrelin receptor, known as the growth hormone secretagogue receptor type 1a. Activation of that receptor triggers signaling that leads to growth hormone release. Selectivity for growth hormone over cortisol and prolactin is the property most often cited for this compound.
Published estimates place the circulating half-life at roughly two hours in humans. Clearance involves peptidase activity and renal handling. Because the peptide is short-lived, release patterns after administration are usually described as pulsatile rather than sustained.
Dry powder is held at minus twenty degrees Celsius or colder, away from light and moisture. Sealed vials under inert gas limit degradation during storage.