GHRH(1-44) (human), somatorelin studies and research data
PepBank has no study results for GHRH(1-44) (human), somatorelin yet. Data as of 2026-10-30.
Searches 0 results and 0 papers. Newer studies from Europe PMC
GHRH(1-44) (human), somatorelin identity
Identifiers, parent molecule, targets and development stage, from curated data.
Growth hormone-releasing hormone, also called growth hormone-releasing factor or somatoliberin, is the mature 44-residue peptide cut from the human GHRH precursor (UniProt P01286) and carrying a C-terminal leucinamide. It is released by the hypothalamus and acts on the GHRH receptor on pituitary somatotroph cells to drive growth hormone synthesis and pulsatile release. The INN for the synthetic peptide is somatorelin, and it has been used as a diagnostic agent (WHO ATC V04CD05). This record is a reference parent for sermorelin, tesamorelin, CJC-1295 and Mod GRF (1-29).
- Kind
- Natural peptide · 44 residues
- Identifiers
- UniProtP01286 (opens in a new tab)ChEMBLCHEMBL2108862 (opens in a new tab)PubChem CID16132353 (opens in a new tab)UNII4UR7N9Z9MM (opens in a new tab)DrugBankDB12656 (opens in a new tab)CAS83930-13-6PDB7CZ5 (opens in a new tab)7V9M (opens in a new tab)KEGGD08523 (opens in a new tab)D03326 (opens in a new tab)
- Development
- No known clinical developmentChEMBL lists max_phase 4 for CHEMBL2108862 (SOMATORELIN), but no FDA or EMA approval was found in this check, so the phase claim is not confirmed and is recorded as unknown here. GHRH is widely used as a research and diagnostic stimulus; 38 ClinicalTrials.gov records name it as an intervention (query.intr=EXPANSION[Term]"growth hormone-releasing hormone" OR EXPANSION[Term]GHRH OR EXPANSION[Term]somatorelin). Source (opens in a new tab)
Targets
| Target | Action | Evidence |
|---|---|---|
| Growth hormone-releasing hormone receptorGHRHRQ02643 (opens in a new tab) | Agonist | primary literatureSource (opens in a new tab) |
Sequence and structure
Residues, differences from the parent, calculated properties and 3D structure. Source values and calculated values are shown separately.
Sequence
44 amino acids · 1 modification
Properties
From identity sources
- Formula
- C215H358N72O66S
- Molecular weight
- 5,039.7 g/mol
- Monoisotopic mass
- 5,036.6591 Da
- UniProt P01286(opens in a new tab)retrieved 2026-10-09
- GSRS UNII 4UR7N9Z9MM(opens in a new tab)retrieved 2026-10-09
- PubChem CID 16132353(opens in a new tab)retrieved 2026-10-09
Calculated from the sequence
- Average mass
- 5,039.71 Da
- Sum of ExPASy residue masses + water + C-amide · ExPASy Compute pI/Mw; FindMod
- Monoisotopic mass
- 5,036.6591 Da
- Sum of ExPASy residue masses + water + C-amide · ExPASy FindMod
- Isoelectric point (pI)
- 11.43
- pH of zero net charge, EMBOSS pKa set · EMBOSS iep, Epk.dat
- Net charge at pH 7.4
- 4.94
- Henderson-Hasselbalch, EMBOSS pKa set · EMBOSS iep, Epk.dat
- GRAVY (hydropathy)
- −0.798
- Mean Kyte-Doolittle hydropathy · Kyte and Doolittle 1982
- Negative: hydrophilic on average.
- Extinction coefficient, 280 nm (Cys reduced)
- 2,980 M⁻¹ cm⁻¹
- 5500 x Trp + 1490 x Tyr · Pace et al. 1995 (ExPASy ProtParam)
- No Trp: ExPASy reports more than 10 % error without Trp.
- Instability index
- 38.48
- Dipeptide instability weights (DIWV) · Guruprasad et al. 1990
- 40 or below: classed as stable (ExPASy).
- Aliphatic index
- 80.0
- Mole % A + 2.9 V + 3.9 (I + L) · Ikai 1980
- Boman index
- 3.03 kcal/mol
- Mean solubility value (negated) · Boman 2003
- Above 2.48: high protein-binding potential (Boman).
- Hydrophobic moment (μH)
- 0.612
- Eisenberg scale, 100° per residue, best 11-residue window · Eisenberg et al. 1982, 1984
- pI with each pKa set
- EMBOSS 11.43Bjellqvist (ExPASy) 10.90IPC peptide 11.34IPC protein 11.04
- Defined and validated for proteins; use with care for short peptides.
- Assumes an ideal alpha helix. Many short peptides are not helical.
@pepdb/chem 0.2.0 · EMBOSS pKa set · ExPASy residue masses
Net charge by pH
pI 11.43 · Net charge at pH 7.4: 4.94
Point or use arrow keys
Henderson-Hasselbalch, EMBOSS pKa set, C-amide. Calculated, not measured.
Show as table
| pH | Net charge |
|---|---|
| 0 | 9.00 |
| 1 | 9.00 |
| 2 | 8.96 |
| 3 | 8.63 |
| 4 | 7.00 |
| 5 | 5.37 |
| 6 | 5.04 |
| 7 | 4.98 |
| 8 | 4.78 |
| 9 | 4.10 |
| 10 | 2.86 |
| 11 | 0.82 |
| 12 | −1.30 |
| 13 | −4.54 |
| 14 | −5.81 |
Composition
- Hydrophobic32% (14)A I L M V
- Aromatic7% (3)F Y
- Positive18% (8)K R
- Negative9% (4)D E
- Polar27% (12)N Q S T
- Special7% (3)G
44 residues. Each residue counts in one class; F and W count as aromatic.
3D structure
Loads the 3D viewer (3Dmol.js, about 150 KB) and the model file from RCSB PDB.
2D structure
GHRH(1-44) (human), somatorelin has 44 residues. A full-atom drawing is hard to read at this size; the sequence view is the reference.
SMILES fromPubChem CID 16132353(opens in a new tab)
CC[C@H](C)[C@@H](C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC2=CC=C(C=C2)O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CCC(=O)N)C(=O)NCC(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CC(C)C)C(=O)N)NC(=O)[C@H](C)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](C)NC(=O)[C@H](CC3=CC=C(C=C3)O)NHelical wheel
An ideal alpha-helix projection. It shows where the hydrophobic residues fall if the peptide folds as a helix. It does not show that it does.
- μH, residues shown
- 0.044
- μH, best 11-residue window
- 0.612
- Arrow direction
- 52°
- Residues
- 44 · 3 rings of 18
Eisenberg consensus (normalized) scale · + K, R · − D, E
Assumes an ideal α-helix: 100° per residue, 3.6 residues per turn. The arrow is the mean hydrophobic moment (Eisenberg et al. 1984) and points at the hydrophobic face.
Show as table
| Position | Residue | Angle | Eisenberg consensus (normalized) |
|---|---|---|---|
| 1 | Y | 0° | 0.26 |
| 2 | A | 100° | 0.62 |
| 3 | D | 200° | -0.90 |
| 4 | A | 300° | 0.62 |
| 5 | I | 40° | 1.38 |
| 6 | F | 140° | 1.19 |
| 7 | T | 240° | -0.05 |
| 8 | N | 340° | -0.78 |
| 9 | S | 80° | -0.18 |
| 10 | Y | 180° | 0.26 |
| 11 | R | 280° | -2.53 |
| 12 | K | 20° | -1.50 |
| 13 | V | 120° | 1.08 |
| 14 | L | 220° | 1.06 |
| 15 | G | 320° | 0.48 |
| 16 | Q | 60° | -0.85 |
| 17 | L | 160° | 1.06 |
| 18 | S | 260° | -0.18 |
| 19 | A | 0° | 0.62 |
| 20 | R | 100° | -2.53 |
| 21 | K | 200° | -1.50 |
| 22 | L | 300° | 1.06 |
| 23 | L | 40° | 1.06 |
| 24 | Q | 140° | -0.85 |
| 25 | D | 240° | -0.90 |
| 26 | I | 340° | 1.38 |
| 27 | M | 80° | 0.64 |
| 28 | S | 180° | -0.18 |
| 29 | R | 280° | -2.53 |
| 30 | Q | 20° | -0.85 |
| 31 | Q | 120° | -0.85 |
| 32 | G | 220° | 0.48 |
| 33 | E | 320° | -0.74 |
| 34 | S | 60° | -0.18 |
| 35 | N | 160° | -0.78 |
| 36 | Q | 260° | -0.85 |
| 37 | E | 0° | -0.74 |
| 38 | R | 100° | -2.53 |
| 39 | G | 200° | 0.48 |
| 40 | A | 300° | 0.62 |
| 41 | R | 40° | -2.53 |
| 42 | A | 140° | 0.62 |
| 43 | R | 240° | -2.53 |
| 44 | L | 340° | 1.06 |
What the studies measured
People first in each area, then animals, then lab cells. Counts are exact and come from studies that gave the peptide.
Newer studies
PepBank reads each paper before it shows the results. This search looks in Europe PMC for newer papers that PepBank has not read yet.
GHRH(1-44) (human), somatorelin studies: 0 papers with results
No paper with results is linked to this peptide.