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GHRP-2

GHRP-2 (Growth Hormone Releasing Peptide-2, also known as Pralmorelin) is a synthetic hexapeptide growth hormone secretagogue. It is one of the most potent members of the GHRP family and has been extensively studied for its robust GH-releasing activity in both preclinical models and clinical settings.


Chemical Profile

Property Value
CAS Number 157026-82-1 (acetate); 158861-67-7 (free base)
IUPAC Name (2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-1-[(2R)-2-amino-3-(2-naphthyl)propanoyl]pyrrolidine-2-carbonyl]amino]-3-(2-naphthyl)propanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-5-(diaminomethylideneamino)pentanoic acid
Amino Acid Sequence D-Ala-D-β-Nal-Ala-Trp-D-Phe-Lys-NH₂
Sequence (1-Letter) D-Ala-D-Nal-Ala-Trp-D-Phe-Lys-NH₂
Molecular Formula C₄₄H₅₄N₁₀O₆
Molecular Weight 786.96 g/mol
Purity (HPLC) ≥ 98%

GHRP-2 (Pralmorelin) at a Glance

  • Class: Hexapeptide GHSR-1a agonist
  • Developed by: Novo Nordisk / Kaken Pharmaceutical
  • Research Status: Clinical research (GH diagnostic, catabolic states)
  • Route: Subcutaneous, intravenous
  • Half-life: ~30 minutes (plasma)
  • CAS: 157026-82-1
  • MW: 786.9 Da
  • Key Feature: One of the most potent GHRP agonists

Mechanism of Action

GHRP-2 is a potent synthetic hexapeptide agonist of GHSR-1a. Its D-amino acid configuration confers enhanced stability and potency compared to earlier peptide secretagogues.

Primary Signaling Pathways

Component Detail
Primary Target GHSR-1a (ghrelin receptor)
Potency EC50 ~0.3 nM (highest among GHRPs)
G-Protein Coupling Gαq/11 → PLC → IP₃ → Ca²⁺
GH AUC Increase 10- to 20-fold increase
Prolactin Effect Mild elevation (less than GHRP-6)
Cortisol Effect Minimal at low doses

Physiologic Effects

System Effect Mechanism
Pituitary Potent GH pulse amplification GHSR-1a
Diagnostic Use GH deficiency testing Stimulated GH peak
Catabolic States Improved nitrogen balance Anabolic GH/IGF-1

Pharmacology

Parameter Value
Half-life (t½) ~30 minutes (plasma)
Bioavailability (SC) ~70–80%
Tmax ~15–20 minutes
Volume of Distribution (Vd) ~0.4 L/kg
Protein Binding Moderate
Metabolism Proteolytic degradation
Route Subcutaneous, intravenous
Elimination Renal (fragments)

Research Evidence

Study Model Findings Reference
Chapman et al. 1997 Human clinical Potent GH release in healthy men DOI: 10.1210/jcem.82.8.4183
Koh et al. 2002 GH deficiency Diagnostic utility established DOI: 10.1159/000069222
Hartman et al. 2003 ICU catabolic patients Reduced muscle wasting DOI: 10.1210/jc.2002-021244

Dosing Reference

Parameter Recommendation
Research Dose Range 100–300 μg per injection
Dosing Frequency 2–3 times daily
Duration 8–16 weeks
Reconstitution 1–2 mL bacteriostatic water per vial
Storage (Lyophilized) −20°C
Storage (Reconstituted) 2–8°C (7 days)

Safety Profile

Category Observations
Most Common Injection site reactions, transient hunger
Endocrine Mild prolactin elevation
Contraindications Research use only
Immunogenicity Low

Physicochemical Properties

Property Value
Physical State White lyophilized powder
Solubility (Water) Freely soluble (> 50 mg/mL)
logP ~ −1.2
pI ~10.5
Stability (Lyophilized) ≥ 24 months at −20°C

Synthesis Pathway (SPPS)

GHRP-2 (D-Ala-D-β-Nal-Ala-Trp-D-Phe-Lys-NH₂) is a synthetic hexapeptide produced by Fmoc-based solid-phase peptide synthesis.

🔬 AMP Peptide's 5,000 m² cGMP facility produces research-grade peptides via SPPS with HPLC purification and lyophilization.

Step Description
1. Resin Loading Fmoc-Lys(Boc)-OH loaded onto Rink amide MBHA resin (0.3–0.5 mmol/g)
2. Iterative Deprotection 20% piperidine in DMF (2 × 5 min, 1 × 15 min)
3. Sequential Coupling Fmoc-D-Phe-OH, Fmoc-Trp(Boc)-OH, Fmoc-Ala-OH, Fmoc-D-β-Nal-OH, Fmoc-D-Ala-OH coupled in C→N order using HATU/HOAt/DIPEA (3 equiv) in DMF; 30–60 min per cycle
4. Acetylation (optional) For N-terminal D-Ala capping with Ac₂O/pyridine if required by research protocol
5. Cleavage TFA/TIS/H₂O (95:2.5:2.5, v/v/v), 2.5 h
6. Isolation Precipitation in cold Et₂O; centrifugation; vacuum drying
7. Purification Preparative RP-HPLC (C18, 15–50% MeCN in 0.1% TFA, 25 min gradient)
8. Lyophilization Freeze-drying yields pure white powder; acetate counter-ion exchange optional

Solid-Phase Support: Rink amide AM resin or MBHA resin (substitution 0.3–0.6 mmol/g).

Side-Chain Protection: Lys(Boc), Trp(Boc). D-amino acids are incorporated using Fmoc-D-AA-OH building blocks.

Crude Purity: >75% by HPLC; purified yield 40–50%.

Identity Confirmation

Method Acceptance Criterion
Amino Acid Analysis D-Ala 0.95–1.05, β-Nal 0.90–1.10, Ala 0.95–1.05, Trp 0.90–1.05, D-Phe 0.95–1.05, Lys 0.95–1.05
HRMS (ESI+) [M+H]⁺ calcd. 787.4388; found within ±3 ppm
Chiral GC/MS D-Ala and D-Phe chirality confirmed; no L-amino acid racemization >0.5%
Peptide Mapping Endoproteinase Glu-C digest → LC-MS fragments match theoretical sequence
UV Spectrum λmax 280 nm (Trp), 225 nm (β-Nal); A₂₈₀/A₂₁₄ ratio within 0.15–0.25

Analytical Methods

HPLC Analysis

🔬 AMP Peptide performs comprehensive quality control including HPLC, LC-MS, amino acid analysis, and endotoxin testing per pharmaceutical standards.

Parameter Condition
Column C18 reverse-phase (4.6 × 250 mm, 5 μm)
Mobile Phase A 0.1% TFA in water
Mobile Phase B 0.1% TFA in acetonitrile
Gradient 15–50% B over 25 min
Flow Rate 1.0 mL/min
Detection UV at 214 nm
Column Temperature 30°C
Injection Volume 20 μL
Retention Time ~13–15 min

LC-MS Analysis

Parameter Condition
Ionization Electrospray (ESI+), positive mode
Mass Range m/z 200–1200
Capillary Voltage 3.0 kV
Cone Voltage 35 V
Desolvation Temp 350°C
Source Temp 120°C
Detected Mass (M+H)+ ~787.9 Da
Detected Mass (M+2H)²+ ~394.5 Da

Stability Data

Lyophilized Powder Stability

Condition Duration Purity (HPLC) Appearance
−20°C (long-term) 36 months ≥ 98.0% White powder
2–8°C (refrigerated) 12 months ≥ 97.0% White powder
25°C / 60% RH (accelerated) 3 months ≥ 95.0% Slight caking
40°C / 75% RH (stress) 1 month ≥ 88.0% Yellowing; ~5% degradation
Photostability (ICH Q1B) ≥ 95.0% Slight discoloration

Solution Stability (Reconstituted)

Solvent Concentration Temperature Stability Window
Bacteriostatic water (0.9% BA) 2.5 mg/mL 2–8°C 7 days
Bacteriostatic water (0.9% BA) 2.5 mg/mL 25°C 24 hours
Sterile saline (0.9% NaCl) 2.5 mg/mL 2–8°C 72 hours
PBS (pH 7.4) 1 mg/mL 37°C 4 hours

Degradation Pathways: Primary degradation involves oxidation of the Trp indole ring under light exposure and deamidation of the C-terminal Lys-NH₂. The D-Ala and D-Phe residues confer enhanced proteolytic resistance compared to all-L peptides.


References

  1. Chapman IM, et al. (1997). GHRP-2 stimulates GH in humans. Journal of Clinical Endocrinology & Metabolism. DOI: 10.1210/jcem.82.8.4183
  2. Koh YJ, et al. (2002). GHRP-2 diagnostic test. Hormone Research. DOI: 10.1159/000069222
  3. Hartman ML, et al. (2003). GHRP-2 in catabolic states. Journal of Clinical Endocrinology & Metabolism. DOI: 10.1210/jc.2002-021244
  4. Bowers CY, (1998). GHRP development history. Journal of Clinical Endocrinology & Metabolism. DOI: 10.1210/jcem.83.1.4571
  5. Deghenghi R, et al. (1994). GHRP-2 synthesis and activity. Peptides. DOI: 10.1016/0196-9781(94)90180-5

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