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Sermorelin

Sermorelin (synthetic GHRH 1–29) is a 29-amino-acid fragment of human growth hormone-releasing hormone (GHRH) comprising the N-terminal bioactive core (residues 1–29). It acts as a full GHRH receptor agonist and is clinically approved as a diagnostic agent for growth hormone deficiency. In research settings, it is used to study the somatotropic axis, pituitary function, and GH dynamics.


Chemical Profile

Property Value
CAS Number 86168-78-7
IUPAC Name L-Tyrosyl-L-alanyl-L-α-aspartyl-L-alanyl-L-isoleucyl-L-phenylalanyl-L-threonyl-L-asparaginyl-L-seryl-L-tyrosyl-L-arginyl-L-lysyl-L-valyl-L-leucyl-L-glycyl-L-glutaminyl-L-leucyl-L-seryl-L-alanyl-L-arginyl-L-lysyl-L-leucyl-L-leucyl-L-glutaminyl-L-α-aspartyl-L-isoleucyl-L-methionyl-L-seryl-L-argininamide
Amino Acid Sequence Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly-Gln-Leu-Ser-Ala-Arg-Lys-Leu-Leu-Gln-Asp-Ile-Met-Ser-Arg-NH₂
Sequence (1-Letter) YADAIFTNSYRKVLGQLSARKLLQDIMSR-NH₂
Molecular Formula C₁₅₃H₂₅₃N₄₅O₄₂S
Molecular Weight 3357.86 g/mol
Purity (HPLC) ≥ 98%

Sermorelin at a Glance

  • Class: GHRH fragment (1–29) amide
  • Research Status: Investigated in GH research; formerly used in diagnostic testing
  • Route: Subcutaneous, intravenous
  • Half-life: ~12 minutes
  • CAS: 86168-78-7
  • MW: 3357.9 Da
  • Key Feature: Bioactive core of endogenous GHRH

Mechanism of Action

Sermorelin is the 1–29 N-terminal fragment of native human GHRH (1–44), containing the full bioactive sequence required for GHRH receptor activation.

Primary Signaling Pathways

Component Detail
Primary Target GHRH receptor (pituitary)
Receptor Class Class B GPCR (secretin family)
G-Protein Coupling Gαs → adenylyl cyclase → cAMP → PKA
GH Transcription PKA → CREB → GH gene transcription
GH Secretion Stimulates GH synthesis and release
Somatostatin Dependence Modulated by hypothalamic somatostatin tone
Pulsatility Preserves endogenous GH pulse pattern

Physiologic Effects

System Effect Mechanism
Pituitary GH synthesis and secretion GHRH-R → cAMP
Diagnostic GH deficiency testing Stimulated GH peak
Therapeutic GH pulse restoration Pulsatile GHRH signaling

Pharmacology

Parameter Value
Half-life (t½) ~12 minutes (IV); ~20 min (SC)
Bioavailability (SC) ~60–70%
Tmax ~15–30 minutes
Volume of Distribution (Vd) ~0.3 L/kg
Protein Binding ~70%
Metabolism Proteolytic degradation (rapid)
Route Subcutaneous, intravenous
Elimination Renal

Research Evidence

Study Model Findings Reference
Thorner et al. 1989 Clinical validation Diagnostic GH stimulation test DOI: 10.1210/jcem.68.6.2656709
Vance et al. 1985 GH-deficient adults Dose-dependent GH release DOI: 10.1210/jcem.61.2.289
Hindmarsh et al. 1991 Children with short stature Promoted linear growth in responders DOI: 10.1210/jcem.72.5.1048

Dosing Reference

Parameter Recommendation
Research Dose Range 200–500 μg daily
Dosing Timing Bedtime (mimics natural GH pulse)
Duration 12–24 weeks
Reconstitution 1–2 mL bacteriostatic water
Storage (Lyophilized) −20°C
Storage (Reconstituted) 2–8°C (7 days)

Safety Profile

Category Observations
Most Common Flushing, injection site reactions
Endocrine Transient GH elevation
Contraindications Research use only outside approved diagnostic indications
Immunogenicity Low

Physicochemical Properties

Property Value
Physical State White lyophilized powder
Solubility (Water) Soluble (> 20 mg/mL)
logP ~ −2.5
pI ~9.0
Stability (Lyophilized) ≥ 24 months at −20°C

Synthesis Pathway (SPPS — GHRH 1–29 Fragment)

Sermorelin (YADAIFTNSYRKVLGQLSARKLLQDIMSR-NH₂) is the 29-amino-acid N-terminal fragment of human GHRH (1–44) synthesized by SPPS, featuring a C-terminal amide for enhanced bioactivity.

🔬 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-Arg(Pbf)-OH loaded onto Rink amide MBHA resin (0.2–0.4 mmol/g)
2. Automated SPPS Fmoc/tBu strategy on automated synthesizer; 28 cycles using HBTU/HOBt/DIPEA (4 equiv) in NMP; 45 min coupling per residue
3. Double Coupling Double coupling at sterically hindered residues (Ile⁵, Val¹³, Ile²⁶) and after β-branched amino acids
4. Capping Ac₂O/pyridine/NMP (1:1:8) after each cycle
5. Cleavage TFA/TIS/H₂O/DODT (92.5:2.5:2.5:2.5, v/v/v/v), 3 h at room temperature
6. Precipitation Cold MTBE/hexane (1:1); crude pellet isolated by filtration
7. Purification Preparative RP-HPLC (C18, 20–55% MeCN in 0.1% TFA, 30 min gradient); purity >98%
8. Counter-Ion Exchange Acetate exchange via repeated lyophilization from 0.1% AcOH
9. Lyophilization Freeze-drying yields white, fluffy powder

Solid-Phase Support: Rink amide MBHA resin (100–200 mesh, substitution 0.35–0.45 mmol/g).

Side-Chain Protection: Arg(Pbf), Asp(OtBu), Asn(Trt), Gln(Trt), Lys(Boc), Ser(tBu), Thr(tBu), Tyr(tBu), Met (no protection — susceptible to oxidation).

Crude Purity: ~50–60% (29-mer); purified yield ~12–20%.

Identity Confirmation

Method Acceptance Criterion
Amino Acid Analysis Match theoretical composition; Met content verified (oxidation-sensitive)
MALDI-TOF MS [M+H]⁺ ~3358.9 Da; ±0.05% mass accuracy
Edman Sequencing First 15 residues confirmed (Tyr-Ala-Asp-Ala-Ile-Phe-Thr-Asn-Ser-Tyr-Arg-Lys-Val-Leu-Gly)
Peptide Mapping Trypsin digestion → 10 expected fragments confirmed by LC-MS/MS
UV Scan λmax 275 nm (Tyr); A₂₇₅/A₂₁₄ ratio 0.12–0.18

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 20–55% B over 30 min
Flow Rate 1.0 mL/min
Detection UV at 214 nm
Column Temperature 30°C
Injection Volume 20 μL
Retention Time ~15–17 min

LC-MS Analysis

Parameter Condition
Ionization Electrospray (ESI+), positive mode
Mass Range m/z 600–2000
Capillary Voltage 3.5 kV
Cone Voltage 60 V
Desolvation Temp 400°C
Source Temp 150°C
Detected Mass (M+H)+ ~3358.9 Da
Detected Charge States 3+ (m/z ~1120), 4+ (m/z ~840), 5+ (m/z ~673)

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 ≥ 96.0% White powder
25°C / 60% RH (accelerated) 3 months ≥ 92.0% Slight caking
40°C / 75% RH (stress) 1 month ≥ 85.0% Yellowing; Met oxidation ~4%, deamidation ~3%
Photostability (ICH Q1B) ≥ 93.0% Slight yellowing

Solution Stability (Reconstituted)

Solvent Concentration Temperature Stability Window
Bacteriostatic water (0.9% BA) 1 mg/mL 2–8°C 7 days
Bacteriostatic water (0.9% BA) 1 mg/mL 25°C 12 hours
Sterile saline (0.9% NaCl) 1 mg/mL 2–8°C 48 hours
PBS (pH 7.4) 1 mg/mL 37°C 2 hours

Degradation Pathways: Sermorelin is highly susceptible to Met²⁷ oxidation (Met sulfoxide), Asn⁸ deamidation, and Asp⁴–Ala⁵ peptide bond hydrolysis. Antioxidants (e.g., methionine 0.1% or ascorbic acid) are recommended in solution. The C-terminal amide enhances stability relative to the free-acid form.


References

  1. Thorner MO, et al. (1989). Sermorelin for GH deficiency testing. Journal of Clinical Endocrinology & Metabolism. DOI: 10.1210/jcem.68.6.2656709
  2. Vance ML, et al. (1985). Sermorelin in GH-deficient adults. Journal of Clinical Endocrinology & Metabolism. DOI: 10.1210/jcem.61.2.289
  3. Hindmarsh PC, et al. (1991). Sermorelin in short stature children. Journal of Clinical Endocrinology & Metabolism. DOI: 10.1210/jcem.72.5.1048
  4. Barinaga M, et al. (1985). GHRH mechanism of action. Endocrinology. DOI: 10.1210/endo-117-2-683
  5. Frohman LA, et al. (1999). GHRH physiology. Endocrine Reviews. DOI: 10.1210/edrv.20.3.0368

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