CompletedPhase 4NCT05353192
A Study to Evaluate the Efficacy and Safety of Recombinant Human Growth Hormone in Children With Achondroplasia
Changchun GeneScience Pharmaceutical Co., Ltd.n = 3920 Aug 2022 to 12 Dec 2025
Achondroplasia
HGH (somatotropin) / Studies
Natural peptide · 191 amino acids · 22,124.8 Da
HGH (somatotropin) studies and research data
PepBank has 140 HGH studies with results. 137 of them gave HGH, with 1,108 results, grouped by what the studies measured. In each group, results from studies in people come first. Data as of 2026-10-30.
Searches 1,108 results and 2,834 papers. Newer studies from Europe PMC
Results in people
1,034
93% of 1,108 results
Results in animals
74
7% of 1,108 results
Results in lab cells
0
0% of 1,108 results
From computer models
0
0% of 1,108 results
The molecule
HGH identity
Identifiers, parent molecule, targets and development stage, from curated data.
Somatropin is recombinant human growth hormone with the mature 191-residue human sequence. This existing record covers the hormone and its medicinal products. Long-acting analogs have separate records.
- Kind
- Natural peptide · 191 residues
- Identifiers
- UniProtP01241 (opens in a new tab)ChEMBLCHEMBL1201621 (opens in a new tab)UNIINQX9KB6PCL (opens in a new tab)DrugBankDB00052 (opens in a new tab)CAS12629-01-5PDB1HWG (opens in a new tab)3HHR (opens in a new tab)KEGGD02691 (opens in a new tab)IUPHAR4943 (opens in a new tab)
- Development
- Approved in the US and EU (Genotropin)Multiple (Eli Lilly, Pfizer, Novo Nordisk, Sandoz, Ferring and others)Approved reference hormone. Multiple manufacturers have somatropin products. This list does not establish current availability of every trade name. Source (opens in a new tab)
Targets
| Target | Action | Evidence |
|---|---|---|
| Growth hormone receptorGHRP10912 (opens in a new tab) | Agonist | ChEMBL mechanism annotation, supported by the approved-drug labelSource (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
191 amino acids · 2 modifications · 2 disulfide bonds
H-
Residues 1 to 10:
FPTIPLSRLF
Residues 11 to 20:
DNAMLRAHRL
Residues 21 to 30:
HQLAFDTYQE
Residues 31 to 40:
FEEAYIPKEQ
Residues 41 to 50:
KYSFLQNPQT
Residues 51 to 60:
SLCFSESIPT
Residues 61 to 70:
PSNREETQQK
Residues 71 to 80:
SNLELLRISL
Residues 81 to 90:
LLIQSWLEPV
Residues 91 to 100:
QFLRSVFANS
Residues 101 to 110:
LVYGASDSNV
Residues 111 to 120:
YDLLKDLEEG
Residues 121 to 130:
IQTLMGRLED
Residues 131 to 140:
GSPRTGQIFK
Residues 141 to 150:
QTYSKFDTNS
Residues 151 to 160:
HNDDALLKNY
Residues 161 to 170:
GLLYCFRKDM
Residues 171 to 180:
DKVETFLRIV
Residues 181 to 190:
QCRSVEGSCG
Residues 191 to 191:
-OHF
Properties
From identity sources
- Formula
- C990H1528N262O300S7
- Molecular weight
- 22,124.77 g/mol
- Monoisotopic mass
- 22,111.0409 Da
- UniProt P01241(opens in a new tab)retrieved 2026-10-27
- GSRS UNII NQX9KB6PCL(opens in a new tab)retrieved 2026-10-27
- ChEMBL CHEMBL1201621(opens in a new tab)retrieved 2026-10-27
- Curated KEGG D02691(opens in a new tab)retrieved 2026-10-27
Calculated from the sequence
- Average mass
- 22,125.02 Da
- Sum of ExPASy residue masses + water + 2 disulfides · ExPASy Compute pI/Mw; FindMod
- Monoisotopic mass
- 22,111.0406 Da
- Sum of ExPASy residue masses + water + 2 disulfides · ExPASy FindMod
- Isoelectric point (pI)
- 5.06
- pH of zero net charge, EMBOSS pKa set · EMBOSS iep, Epk.dat
- Net charge at pH 7.4
- −4.73
- Henderson-Hasselbalch, EMBOSS pKa set · EMBOSS iep, Epk.dat
- GRAVY (hydropathy)
- −0.411
- Mean Kyte-Doolittle hydropathy · Kyte and Doolittle 1982
- Negative: hydrophilic on average.
- Extinction coefficient, 280 nm (Cys reduced)
- 17,420 M⁻¹ cm⁻¹
- 5500 x Trp + 1490 x Tyr · Pace et al. 1995 (ExPASy ProtParam)
- Extinction coefficient, 280 nm (all Cys as cystines)
- 17,670 M⁻¹ cm⁻¹
- 5500 x Trp + 1490 x Tyr + 125 x cystine · Pace et al. 1995 (ExPASy ProtParam)
- Instability index
- 40.76
- Dipeptide instability weights (DIWV) · Guruprasad et al. 1990
- Above 40: classed as possibly unstable (ExPASy).
- Aliphatic index
- 83.7
- Mole % A + 2.9 V + 3.9 (I + L) · Ikai 1980
- Boman index
- 1.94 kcal/mol
- Mean solubility value (negated) · Boman 2003
- 2.48 or below: lower protein-binding potential (Boman).
- Hydrophobic moment (μH)
- 0.678
- Eisenberg scale, 100° per residue, best 11-residue window · Eisenberg et al. 1982, 1984
- pI with each pKa set
- EMBOSS 5.06Bjellqvist (ExPASy) 5.27IPC peptide 5.15IPC protein 5.15
- 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 5.06 · Net charge at pH 7.4: −4.73
Point or use arrow keys
Henderson-Hasselbalch, EMBOSS pKa set, 2 disulfide. Calculated, not measured.
Show as table
| pH | Net charge |
|---|---|
| 0 | 24.00 |
| 1 | 23.97 |
| 2 | 23.73 |
| 3 | 21.54 |
| 4 | 10.95 |
| 5 | 0.32 |
| 6 | −2.46 |
| 7 | −4.28 |
| 8 | −5.18 |
| 9 | −6.44 |
| 10 | −10.77 |
| 11 | −18.96 |
| 12 | −25.01 |
| 13 | −31.29 |
| 14 | −33.66 |
Composition
- Hydrophobic27% (51)A I L M V
- Aromatic12% (22)F W Y
- Positive12% (23)H K R
- Negative13% (25)D E
- Polar26% (50)N Q S T
- Special10% (20)C G P
191 residues. Each residue counts in one class; F and W count as aromatic.
A Ala7 · 4%
I Ile8 · 4%
L Leu26 · 14%
M Met3 · 2%
V Val7 · 4%
F Phe13 · 7%
W Trp1 · 1%
Y Tyr8 · 4%
H His3 · 2%
K Lys9 · 5%
R Arg11 · 6%
D Asp11 · 6%
E Glu14 · 7%
N Asn9 · 5%
Q Gln13 · 7%
S Ser18 · 9%
T Thr10 · 5%
C Cys4 · 2%
G Gly8 · 4%
P Pro8 · 4%
3D structure
ExperimentalPDB 1HWG
Loads the 3D viewer (3Dmol.js, about 150 KB) and the model file from RCSB PDB.
Helical 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
- 0.175
- μH, best 11-residue window
- 0.678
- Arrow direction
- 156°
- Residues
- 1–54 of 191 · 3 rings of 18
HydrophilicHydrophobic
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 | F | 0° | 1.19 |
| 2 | P | 100° | 0.12 |
| 3 | T | 200° | -0.05 |
| 4 | I | 300° | 1.38 |
| 5 | P | 40° | 0.12 |
| 6 | L | 140° | 1.06 |
| 7 | S | 240° | -0.18 |
| 8 | R | 340° | -2.53 |
| 9 | L | 80° | 1.06 |
| 10 | F | 180° | 1.19 |
| 11 | D | 280° | -0.90 |
| 12 | N | 20° | -0.78 |
| 13 | A | 120° | 0.62 |
| 14 | M | 220° | 0.64 |
| 15 | L | 320° | 1.06 |
| 16 | R | 60° | -2.53 |
| 17 | A | 160° | 0.62 |
| 18 | H | 260° | -0.40 |
| 19 | R | 0° | -2.53 |
| 20 | L | 100° | 1.06 |
| 21 | H | 200° | -0.40 |
| 22 | Q | 300° | -0.85 |
| 23 | L | 40° | 1.06 |
| 24 | A | 140° | 0.62 |
| 25 | F | 240° | 1.19 |
| 26 | D | 340° | -0.90 |
| 27 | T | 80° | -0.05 |
| 28 | Y | 180° | 0.26 |
| 29 | Q | 280° | -0.85 |
| 30 | E | 20° | -0.74 |
| 31 | F | 120° | 1.19 |
| 32 | E | 220° | -0.74 |
| 33 | E | 320° | -0.74 |
| 34 | A | 60° | 0.62 |
| 35 | Y | 160° | 0.26 |
| 36 | I | 260° | 1.38 |
| 37 | P | 0° | 0.12 |
| 38 | K | 100° | -1.50 |
| 39 | E | 200° | -0.74 |
| 40 | Q | 300° | -0.85 |
| 41 | K | 40° | -1.50 |
| 42 | Y | 140° | 0.26 |
| 43 | S | 240° | -0.18 |
| 44 | F | 340° | 1.19 |
| 45 | L | 80° | 1.06 |
| 46 | Q | 180° | -0.85 |
| 47 | N | 280° | -0.78 |
| 48 | P | 20° | 0.12 |
| 49 | Q | 120° | -0.85 |
| 50 | T | 220° | -0.05 |
| 51 | S | 320° | -0.18 |
| 52 | L | 60° | 1.06 |
| 53 | C | 160° | 0.29 |
| 54 | F | 260° | 1.19 |
Results by area
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.
Trials and papers
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.
Status and safety
Data