Everything below concerns growth hormone secretagogue. We keep the language plain, cite what the science says, and separate well-supported claims from open questions.
Last reviewed on 2025-10-26. Where a claim depends on a specific study, the study is described rather than over-claimed.
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.
Selectivity is the property most often attached to this peptide. Published animal and early human studies record increases in growth hormone release after administration, with adrenocorticotropic hormone and cortisol responses remaining small by comparison. Effects on appetite-related pathways also appear weaker than those reported for several earlier secretagogues. Reviews that compare members of the growth hormone secretagogue family cite these findings frequently, though the receptor-level explanation for the selectivity continues to be debated rather than settled.
Ipamorelin is a synthetic pentapeptide classified as a growth hormone secretagogue. Its sequence, Aib-His-D-2-Nal-D-Phe-Lys-NH2, combines three non-proteinogenic residues with a C-terminal amide. The N-terminal aminoisobutyric acid unit and the two aromatic D-amino acids distinguish it from peptides assembled only from standard L-amino acids. Its formula is C38H49N9O5, corresponding to an average mass near 711.9 Da. At neutral pH the molecule carries a net positive charge, a property that shapes its behaviour in chromatographic and electrophoretic systems.
The compound was developed at Novo Nordisk during the 1990s as part of a programme seeking secretagogues with improved selectivity. It was described in the peer-reviewed literature in 1998 alongside related pentapeptides from the same series. Investigators advanced it because it raised growth hormone output in animal models while leaving other pituitary hormones comparatively unaffected. The development code NNC 26-0161 appears in earlier reports, and ipamorelin later became the common designation in published work.
| Property | Value | Notes |
|---|---|---|
| Molecular formula | C38H49N9O5 | Reported for the free peptide |
| Molecular mass | 711.85 Da | Monoisotopic value |
| Residue motif | Aib-His-D-2-Nal-D-Phe-Lys-NH2 | Non-natural residues at positions one and three |
| Primary target | GHSR-1a | Ghrelin receptor, G protein coupled |
| Reported plasma half-life | About two hours | Values vary with assay and subject group |
从用途定位看,ipamorelin 目前主要以研究用肽的身份被讨论,未见主要药品监管机构将其批准为治疗药物。市售材料通常标注仅供研究使用,不得用于人体或诊断程序。文献中它常与生长激素促分泌素、GHS-R1a 激动剂、胃饥饿素拟似物等表述并列出现。既有研究的样本量普遍偏小,因此对其效应强度与一致性的描述应保持谨慎。
Ipamorelin 是一种合成五肽,序列为 Aib-His-D-2-Nal-D-Phe-Lys-NH2,分子式 C38H49N9O5,游离碱分子量约 711.85 g/mol。它属于生长激素促分泌素(GHS)家族,作用靶点是胃饥饿素受体 GHS-R1a。该化合物由诺和诺德的研究团队在二十世纪九十年代末报道,设计目标是提高对生长激素释放的选择性。C 端酰胺化与 N 端 Aib 残基是两个用于抵抗肽酶降解的结构特征。
在 GHS 家族中,早期肽类如 GHRP-6 与 GHRP-2 会同时促进生长激素、皮质醇与催乳素的释放,并明显增加食欲。Ipamorelin 在动物与早期人体研究中表现出对生长激素释放的相对选择性,对上述其他激素的影响较小。这种差异通常归因于受体结合模式与下游信号偏向的不同,而完整的分子解释仍有待补充。需要区分的是,选择性是研究观察中的相对程度,并非绝对界限。
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.
Human data remain limited and come mainly from small, short-term studies conducted decades ago. The peptide has not received approval as a medicine from major regulators, so current availability is largely as a research chemical. Reported effects on growth hormone pulsatility, appetite, and body composition should be read as preliminary, since few independent groups have replicated the original findings. Analytical characterization of research-grade material varies between suppliers, which complicates comparison across studies. Regulatory status also differs by country, and some jurisdictions classify it as a prescription-only or otherwise restricted item.
Ipamorelin is a synthetic pentapeptide that belongs to the growth hormone secretagogue class. It acts as an agonist at the ghrelin receptor, also called the growth hormone secretagogue receptor type 1a. The compound was designed in the 1990s during a search for agents that release growth hormone with fewer off-target hormonal effects than earlier secretagogues. It appears in the research literature under several sequence-based names. Material supplied for laboratory work is normally a lyophilized solid, and it is not marketed as an approved therapeutic in major jurisdictions.
Compared with earlier growth hormone secretagogues such as GHRP-6 and hexarelin, ipamorelin has been reported to produce less stimulation of adrenocorticotropic hormone, cortisol, and prolactin in animal and early human studies. This selectivity is usually attributed to differences in receptor subtype interactions and to the tissue distribution of the receptor. Effects on appetite appear weaker than those of ghrelin itself, although the supporting evidence base is small. Whether these differences produce a distinct clinical profile remains an open question, since controlled human trials are limited.
Ipamorelin is a synthetic pentapeptide first described in the 1990s by researchers at Novo Nordisk during a program to develop selective growth hormone secretagogues. Its sequence is Aib-His-D-2-Nal-D-Phe-Lys-NH2, incorporating two non-natural residues, alpha-aminoisobutyric acid and D-2-naphthylalanine. The C-terminus is amidated, and the material is supplied as a white lyophilized powder. The molecular formula is C38H49N9O5 and the monoisotopic mass is approximately 711.85 daltons. The short chain and modified residues give it greater resistance to enzymatic degradation than many larger peptide hormones.
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Sources: en.wikipedia.org
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== History == Alazocine was one of the early members of the benzomorphan family of opioid analgesics to be investigated. It was first described in the scientific literature in 1961. Its development resulted from nalorphine (N-allylnormorphine), a potent analgesic and opioid antagonist with similar pharmacology which had been introduced in the mid-1950s. Alazocine was found to produce strong psychotomimetic effects in humans, and it was not further developed for clinical use. Subsequently, other benzomorphans, such as pentazocine (an N-dimethylallylbenzomorphan), cyclazocine (an N-cyclopropylmethylbenzomorphan), and phenazocine (an N-phenylethylbenzomorphan), were developed, and some have been marketed for use as analgesics. The sigma σ1 receptor was named in 1976 and (+)-alazocine was described as its prototypical ligand. The receptor was initially thought to be an opioid receptor, and then was confused with the NMDA receptor for a time, but was ultimately distinguished from them both. The psychotomimetic effects of alazocine and the other benzomorphans were initially attributed incorrectly to agonism of the σ1 receptor; subsequent research established that the effects are in fact caused by agonism of the κ-opioid receptor and/or antagonism of the NMDA receptor.
Sources: en.wikipedia.org
Both molecules activate the same receptor, GHSR-1a, but they share little sequence identity. Ghrelin is a 28-amino-acid hormone carrying a distinctive acyl modification, whereas ipamorelin is a short synthetic peptide. The shared target explains overlapping endocrine effects, while the different structures account for differences in metabolic stability and receptor selectivity.
Early animal and human studies reported growth hormone release at levels that produced small changes in cortisol, prolactin and adrenocorticotropic hormone. That contrast with older secretagogues gave rise to the selectivity label. The observation is consistent across several reports but rests on a limited number of small studies.
Plasma peptidases cleave the molecule into smaller fragments, and reported half-lives in human studies are on the order of a couple of hours. The identity and activity of individual breakdown products have not been fully mapped. Questions about tissue-level clearance remain open.
It is a synthetic five-amino-acid peptide that acts as a growth hormone secretagogue. Three of its residues are non-standard amino acids, and the chain ends in an amide rather than a free acid. The molecule is small enough that it can be characterised by routine peptide analytical techniques.