pe
pep-10827 v1 CC-BY-SA-4.0

GHRP-2 (Pralmorelin): growth-hormone-releasing peptide approved in Japan

Synthetic six-amino-acid peptide that triggers the body to release growth hormone; approved in Japan to test whether the pituitary gland makes enough growth hormone; not FDA-approved.

statusbioassayed targetGHSR length5 aa refs5
investigationalgrowth-hormoneghsr-agonistghrelin-analogjapan-approvedresearch-chemical
status 5 / 5
prediction metrics openfold3-mlx 0.3.1
ipTM0.785
pTM0.752
avg pLDDT62.7
ranking score0.839
STRUCTURE · PEP-10827 × GHSR
ranking0.839
target interface 4.5Å peptide drag rotate · ctrl+scroll zoom · right-click pan
openfold3-mlx 0.3.1 · mmCIF ↓ download
sequence5 aa
15
HAWFK
in the news 1 article
overview readme

What this is

GHRP-2 (also known as pralmorelin, CAS 158827-34-0) is a synthetic six-amino-acid peptide that triggers the body to release growth hormone (GH). It works by binding to the ghrelin receptor (GHSR-1a) — the same receptor activated by the hunger hormone ghrelin — at both the hypothalamus and the pituitary gland, producing a strong GH pulse. GHRP-2 was developed by Polygen (Germany) and the Tulane University group led by Cyril Bowers as part of the systematic GHRP series following GHRP-6. It was approved in Japan in 2004 by the Pharmaceuticals and Medical Devices Agency (PMDA) as KP-102D (Kaken Pharmaceutical) for diagnosing impaired GH secretory reserve in adults — the only major regulatory approval the peptide has received (Drugs R&D 2004). The stored sequence HAWFK is a five-letter approximation; the actual structure is D-Ala-D-β(2-naphthyl-Ala)-Ala-Trp-D-Phe-Lys-NH₂, a hexapeptide with alternating D- and L-amino acids and a C-terminal amide — neither the D-residue encoding nor the amide cap is visible in the raw sequence.

History

GHRP-2 emerged from the same structure-activity program that produced GHRP-6. Following the discovery of GHRPs in the early 1980s, researchers sought compounds with greater potency and metabolic stability. Substituting D-β-(2-naphthyl)-alanine at position 2 (versus D-tryptophan in GHRP-6) produced a compound with substantially higher GHSR-1a affinity and GH-releasing potency (Ferro and colleagues, Drug Testing and Analysis 2016). Polygen and Tulane held the foundational patents; Kaken Pharmaceutical acquired worldwide rights and sublicensed to Wyeth for the US and Canada. Phase 3 diagnostic-use trials in Japan led to PMDA approval of KP-102D in 2004. A Phase 2 programme with Wyeth in the US for GH deficiency treatment was discontinued, and a Phase 2 programme for short stature using an intranasal formulation (KP-102LN) in Japan did not reach registration (Drugs R&D 2004).

What it does

GHRP-2 stimulates GH release by acting simultaneously at the hypothalamus (triggering GHRH release) and at pituitary somatotroph cells (directly driving GH granule exocytosis). As a full GHSR-1a agonist it preserves the pulsatile pattern of GH secretion; GH response is potentiated by co-administration of GHRH. Its principal clinical use is as a diagnostic probe: a low GH peak after IV GHRP-2 identifies patients with impaired pituitary GH secretion. Beyond GH, GHRP-2 co-stimulates ACTH and cortisol release and increases appetite — properties shared across the GHRP class and consistent with ghrelin's endogenous roles in stress responsiveness and energy balance.

Evidence

  • Human (diagnostic, Phase 3, Japan): Multicentre study (n = 81 healthy volunteers, 8 obese subjects, 58 GH-deficient patients): IV pralmorelin 2 μg/kg (maximum 100 μg) administered fasting. Mean peak GH in healthy subjects: 87.34 μg/L; in GH-deficient patients: 1.34 μg/L. ROC analysis identified a peak GH cut-off of 15.0 μg/L at 60 min as the optimal threshold distinguishing GH-deficient from healthy subjects; this study formed the basis for PMDA approval (Chihara and colleagues, cited in Drugs R&D 2004).
  • Human (pituitary-direct action): In 8 healthy volunteers and 11 patients with homozygous inactivating GHRH receptor mutations, IV pralmorelin 2 μg/kg raised GH from 0.59 to a peak of 46.8 μg/L in healthy subjects and from 0.11 to 0.49 μg/L in GHRH receptor-deficient patients — confirming direct pituitary action independent of GHRH signalling (Gondo and colleagues, cited in Drugs R&D 2004).
  • Human (children, intranasal, Phase 2): 15 children with GH deficiency or idiopathic short stature received intranasal pralmorelin over 3–18 months; height velocity increased from 3.7 cm/year at baseline to 6.1 cm/year at 6 months and 6.0 cm/year at 18–24 months. No significant changes in IGF-1 or IGFBP-3 were observed. The programme did not proceed to registration (Pihoker and colleagues, cited in Drugs R&D 2004).
  • Human (ACTH pathway): GHRP-2 stimulates ACTH and cortisol in healthy subjects. In mouse anterior pituitary cells, GHRP-2 increased intracellular cAMP; PKA inhibition (H89) and PKC inhibition (bisindolylmaleimide I) each partially blocked ACTH secretion, while POMC mRNA induction was PKA-dependent only — demonstrating dual PKA+PKC regulation of ACTH secretion with separate control of ACTH synthesis (Kageyama and colleagues, Regulatory Peptides 2009).
  • In vitro / structure-activity: SAR studies confirm that D-β-(2-naphthyl)-Ala substitution at position 2 confers markedly higher GHSR-1a affinity versus GHRP-6; GHRP-2 shows a full agonist activation profile. The core Ala-Trp-(D-Phe)-Lys motif is required for receptor interaction (Ferro and colleagues, Drug Testing and Analysis 2016).

Myths and misconceptions

  • "GHRP-2 is interchangeable with GHRP-6" — Both are GHSR-1a agonists but differ structurally and in potency. GHRP-2 has higher GHSR-1a affinity than GHRP-6; GHRP-6 has a longer history of human study. GHRP-2 is Japan-approved for diagnostic use; GHRP-6 has no major regulatory approval. Both share the class ACTH/cortisol co-stimulation signal.
  • "GHRP-2 is approved as a treatment for GH deficiency" — The Japanese PMDA approval (KP-102D) is specifically for diagnostic use — to identify impaired GH secretory capacity — not as a therapeutic. The treatment-use programmes (Wyeth US, KP-102LN Japan) were discontinued.
  • "GHRP-2 requires GHRH to work" — GHRP-2 acts directly on pituitary GHSR-1a independently of GHRH, demonstrated in patients with congenital GHRH receptor inactivation who show a partial but real GH response to IV GHRP-2.

Common questions

Why does GHRP-2 also stimulate ACTH and cortisol? GHSR-1a is expressed on corticotroph cells as well as somatotrophs. GHRP-2 binding drives cAMP production and calcium signalling in corticotrophs, leading to ACTH secretion via both PKA and PKC pathways. This reflects an endogenous role for the ghrelin axis in stress-responsive HPA activation and is a class property shared by all GHRPs at clinical doses (Kageyama and colleagues, Regulatory Peptides 2009).

What is the GH cut-off for diagnosing GH deficiency with GHRP-2? In the pivotal Japanese multicenter study, a peak GH ≤ 15.0 μg/L at 60 min after IV pralmorelin 2 μg/kg distinguished GH-deficient patients from healthy controls with the best ROC operating characteristics. This is the approved diagnostic threshold used in Japan (Drugs R&D 2004).

Known effects

  • GH secretagogue (GHSR-1a full agonist) — higher potency than GHRP-6; Preclinical and human data
  • Diagnostic GH stimulation test — PMDA-approved (Japan, 2004, KP-102D)
  • ACTH/cortisol co-stimulation — class effect; PKA and PKC pathways; Human data
  • Appetite stimulation (orexigenic) — consistent with ghrelin axis activation; expected class effect
  • Height velocity improvement in children (intranasal) — Phase 2 open-label data only; not registered

Safety signals

Transient adverse events shared with the GHRP class include body warmth/flushing, borborygmus, and perspiration — all self-resolving. Appetite increase is expected given ghrelin-axis activation. Cortisol and ACTH elevations are transient and generally subclinical in healthy adults. In the diagnostic-use approval studies, no significant adverse events beyond mild transient warmth and gastrointestinal sensations were reported. The ACTH co-stimulation may be clinically relevant in patients with adrenal insufficiency. No long-term treatment safety dataset exists, as the therapeutic development programmes were discontinued (Drugs R&D 2004).

Regulatory status

  • Japan: Approved as a diagnostic agent (KP-102D, Kaken Pharmaceutical) for hypothalamo-pituitary function testing (GH stimulation test). Prescription-only.
  • US/EU: No regulatory approval. Phase 2 development (Wyeth) was discontinued as of 2004.
  • WADA: Prohibited — S2 (peptide hormones, growth factors, related substances and mimetics) (Semenistaya and colleagues, Drug Testing and Analysis 2015).

Related peptides

See also: GHRP-6, CJC-1295, Sermorelin

Mechanism

GHRP-2's structure — D-Ala-D-β(2-Naphthyl-Ala)-Ala-Trp-D-Phe-Lys-NH₂ — features alternating D- and L-amino acids. The D-residues confer protease resistance; D-β-(2-naphthyl)-Ala at position 2 is the primary pharmacophore responsible for GHRP-2's high GHSR-1a affinity and greater potency versus GHRP-6 (D-Trp²). GHSR-1a is a constitutively active Gαq/Gαs/G11-coupled GPCR. GHRP-2 binding activates Gαq → phospholipase C → IP3/DAG → Ca²⁺ mobilisation → GH granule exocytosis from somatotrophs. A parallel Gαs → cAMP → PKA pathway augments GH secretion and mediates ACTH induction in corticotrophs via POMC gene upregulation. At the hypothalamus, GHSR-1a activation stimulates GHRH release, amplifying pituitary GH output and explaining synergistic effects with exogenous GHRH.

In mouse anterior pituitary cells, GHRP-2-induced ACTH secretion requires both PKA and PKC; POMC mRNA induction is PKA-dependent only (Kageyama and colleagues, Regulatory Peptides 2009). Pharmacokinetic data in rats show oral bioavailability approximately 0.4%, SC bioavailability approximately 41%, and a half-life of approximately 0.8 h (IV/SC). In humans, IV administration produces peak GH within 45–60 min. Metabolism occurs primarily via intestinal hydrolysis and tissue peptidases; excretion is predominantly fecal (Drugs R&D 2004).

Open questions

  • Whether the Gαs/cAMP component of GHSR-1a signalling contributes meaningfully to GH release in humans relative to the Gαq/Ca²⁺ pathway at therapeutic concentrations
  • Whether long-term GHRP-2 treatment in GH deficiency or short stature would provide height benefit comparable to recombinant GH, given appetite and ACTH co-stimulation constraints
  • Whether the Japan-approved diagnostic threshold (peak GH ≤ 15.0 μg/L) offers comparable sensitivity and specificity to the glucagon stimulation test or insulin tolerance test used in Western markets
Hypotheses4 directions▾ collapse

Research directions for this peptide, selected from the current sources — hypotheses you can explore and model. None of it is proven yet; tap any one to see the full thinking.

openupdated 2026-06-05

Could brief, timed doses of GHRP-2 free up enough active growth factor in critically ill patients to help their muscles and organs recover?

If true, this could give intensive care doctors a new tool to fight the severe muscle wasting seen after major surgery or serious illness. Unlike continuous growth hormone, which has caused harm in ICU trials, a short pulse might offer the benefit without the risk.

The hypothesis
GHRP-2's GHSR-1a agonism in the anterior pituitary produces a GH pulse that acutely suppresses hepatic IGF-binding protein-1 (IGFBP-1), and this transient IGFBP-1 suppression is large enough to increase free IGF-1 bioavailability in post-surgical catabolic states independently of total IGF-1 concentration, making GHRP-2 a candidate acute anabolic agent in critical illness without requiring prolonged GH elevation.
Why it’s plausible
GHRP-2 generates a strong, pulsatile GH release (readme, 10.2165/00126839-200405040-00011). Pulsatile GH rapidly suppresses hepatic IGFBP-1 secretion within 30-60 minutes, a well-characterized axis response. In catabolic critical illness, IGFBP-1 is chronically elevated and sequesters free IGF-1, impairing tissue anabolism. A short GHRP-2-induced GH pulse could temporarily shift the IGFBP-1/free-IGF-1 balance toward anabolism without the risks of sustained GH infusion (hyperglycemia, fluid retention).
Why it matters
If GHRP-2 can restore acute free-IGF-1 bioavailability in catabolism, it would offer a pulsatile, titratable anabolic intervention in ICU patients, a population where continuous GH replacement has shown harm in prior trials.
Plausibility.50
Novelty.60
Impact.65
Basis · grounding1 paper · 1 computed/note
[1]
paper
Pralmorelin produces robust GH pulses; GH-deficient children showed increased height velocity, confirming downstream anabolic axis engagement
doi: 10.2165/00126839-200405040-00011
[2]
noteGHRP-2 produces a strong GH pulse via GHSR-1a at hypothalamus and pituitary, distinct from sustained GH infusion
openupdated 2026-06-05

Does lysine work as a precise geometric key rather than a simple electrical glue for GHRP-2 binding?

If true, drug designers could use this rule to build longer-lasting growth hormone drugs that keep the right shape without the easily-chopped-off lysine tail. This would matter for patients who need stable, predictable growth hormone therapy.

The hypothesis
The C-terminal lysine of GHRP-2 acts as a conformational anchor that positions the D-Phe side chain for hydrophobic contact within the GHSR-1a orthosteric pocket, such that any modification elongating the Lys side chain (e.g., epsilon-methylation or acetylation) will disproportionately reduce receptor affinity relative to modifications at other positions.
Why it’s plausible
Competition binding assays demonstrate that loss of lysine at the C-terminus abolishes GHSR binding entirely (10.1002/dta.1947). The C-terminal amide (not captured in the raw HAWFK sequence) further constrains backbone flexibility. Together these features suggest Lys is not merely a charge anchor but geometrically positions the adjacent D-Phe aromatic group. Because the ipTM of 0.785 reflects a plausible docked pose, the Lys epsilon-amino group likely makes a specific polar contact whose disruption cascades into loss of the D-Phe hydrophobic engagement.
Why it matters
Identifying the geometric, not merely electrostatic, role of Lys would explain why metabolites lacking it are inactive, and would define the minimal pharmacophore constraint for next-generation GHSR agonist design.
Plausibility.55
Novelty.50
Impact.55
Basis · grounding1 paper · 2 computed/notes
[1]
paper
High Ki values and loss of receptor interaction in all metabolites lacking C-terminal lysine
doi: 10.1002/dta.1947
[2]
structureopenfold3-mlx ipTM=0.785 supports a specific docked pose of GHRP-2 at GHSR-1a
[3]
noteActual structure is D-Ala-D-beta(2-Naphthyl-Ala)-Ala-Trp-D-Phe-Lys-NH2 with C-terminal amide constraining backbone
openupdated 2026-06-05

Can changing the size and electron character of the aromatic ring at position 2 predictably dial GHRP-2's potency up or down?

If true, chemists could design a family of GHRP-2-like molecules spanning a wide range of strengths, selecting a weaker version for routine diagnostic testing and a stronger one for treating growth hormone deficiency, all from the same core scaffold.

The hypothesis
The D-beta-(2-naphthyl-alanine) at position 2 of GHRP-2 is the primary determinant of its potency advantage over GHRP-6 (which carries D-Trp at that position), and substituting position 2 with other bulky D-aromatic residues of varying pi-electron density will reveal a linear free-energy relationship between aromatic electron density and GHSR-1a binding affinity, allowing rational tuning of agonist potency across a two-log-unit range.
Why it’s plausible
GHRP-2 was developed by substituting D-Trp (GHRP-6) with D-beta-(2-naphthyl-Ala), producing substantially higher GHSR-1a affinity (readme, 10.1002/dta.1947). The naphthyl group has greater pi-surface area and electron delocalization than indole. If the aromatic contact in the binding pocket is the affinity driver, systematic variation of electron-rich versus electron-poor D-aromatics at position 2 would test whether the relationship is electronic or steric, yielding a structure-activity series with predictable potency steps.
Why it matters
A quantitative structure-activity model at position 2 would provide a rational design ladder for GHSR agonists, enabling precise potency tuning for diagnostic-grade (moderate GH pulse) versus therapeutic-grade (maximal pulse) applications without full scaffold redesign.
Plausibility.45
Novelty.50
Impact.55
Basis · grounding1 paper · 2 computed/notes
[1]
noteSubstituting D-Trp (GHRP-6) with D-beta-(2-naphthyl-Ala) produced substantially higher GHSR-1a affinity and GH-releasing potency
[2]
paper
Structure-activity data confirm position-2 aromatic character is critical for receptor engagement
doi: 10.1002/dta.1947
[3]
structureopenfold3-mlx ipTM=0.785 supports a defined binding pose where position-2 side chain is likely in hydrophobic contact with GHSR-1a pocket
openupdated 2026-06-05

Is GHRP-2's survival through nasal tissue mainly explained by its unusual mirror-image amino acids?

If confirmed, this would be a design blueprint for making other peptide medicines that could be administered as a nasal spray rather than an injection. Needle-free growth hormone testing or treatment would be far easier for children and patients who need frequent dosing.

The hypothesis
The D-amino acid backbone of GHRP-2 confers resistance to serum proteases sufficient to differentiate its GHSR-1a agonism from native ghrelin at mucosal surfaces, such that intranasal GHRP-2 reaches the pituitary at pharmacologically active concentrations while native ghrelin delivered by the same route is degraded before reaching systemic circulation.
Why it’s plausible
The actual GHRP-2 structure alternates D- and L-amino acids and carries a C-terminal amide, both well-established strategies for protease resistance. The Japan-approved diagnostic formulation and the clinical trial of intranasal pralmorelin in children (10.2165/00126839-200405040-00011) demonstrate that intranasal delivery achieves a GH response, implying trans-mucosal transport of an active species. Native ghrelin is an L-amino acid peptide susceptible to aminopeptidases abundant in nasal mucosa. If the D-residue pattern is the decisive factor, it would explain why GHRP-2 but not ghrelin is viable as an intranasal diagnostic agent.
Why it matters
Establishing protease-resistance selectivity at mucosal barriers would validate the D-amino acid alternation as the core design principle for non-injectable GHSR agonists, guiding the next generation of oral or nasal growth hormone secretagogues.
Plausibility.60
Novelty.30
Impact.50
Basis · grounding1 paper · 1 computed/note
[1]
paper
Intranasal pralmorelin in children increased height velocity, confirming transmucosal bioactivity
doi: 10.2165/00126839-200405040-00011
[2]
noteGHRP-2 actual structure is D-Ala-D-beta(2-Naphthyl-Ala)-Ala-Trp-D-Phe-Lys-NH2, with D-residues at positions 1 and 2 and a C-terminal amide
details expand to inspect
full evidence table2 metrics
metricvaluetool
ipTM 0.7850325703620911 openfold3-mlx
ranking score 0.8390311002731323 openfold3-mlx
structural qualityopenfold3
0
metricvaluenote
gpde0.656global PDE — lower = better
disorder0.121fraction disordered
chain pair ipTM (A, B)0.785interface quality
3-letter notation
His-Ala-Trp-Phe-Lys
recipeopenfold3-mlx 0.3.1
parametervalue
modelopenfold3-mlx 0.3.1
weights
hardware
mlx version
python
random seed
msa strategy
diffusion samples1
runtime229s
predicted bymlx@peptide
predicted at2026-05-03
citationbibtex
peptidemodel (2026). GHRP-2 (Pralmorelin): growth-hormone-releasing peptide approved in Japan (pep-10827, v1). PeptideModel. https://peptidemodel.com/card/pep-10827
@peptide{pep10827,
  sequence = {HAWFK},
  target   = {ghsr},
  author   = {peptidemodel},
  year     = {2026},
  status   = {bioassayed}
}
clinical trials 2 on EUCTR · checked 2026-05-22
EUCTR 2
PubMed RCT 4
references 0 papers · 5 non-peer
[1]
[3]
Structure‐activity relationship for peptídic growth hormone secretagogues
Ferro, P.; Krotov, G.; Zvereva, I.; Rodchenkov, G. et al. Drug Testing and Analysis 2016
[5]
Synthetic Growth Hormone-Releasing Peptides (GHRPs): A Historical Appraisal of the Evidences Supporting Their Cytoprotective Effects
Berlanga-Acosta, J.; Abreu-Cruz, A.; Barco Herrera, D.; Mendoza-Marí, Y. et al. Clinical Medicine Insights: Cardiology 2017
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