CompletedPhase 4Results postedNCT01701973
Effect of DPP4 Inhibition on Growth Hormone Secretion
Vanderbilt Universityn = 44Jan 2013 to May 2017
Obesity
Pegvisomant / Studies
Conjugate · 191 amino acids
Pegvisomant studies and research data
PepBank has 52 pegvisomant studies with results. All of them gave pegvisomant, with 299 results, grouped by what the studies measured. In each group, results from studies in people come first. Data as of 2026-10-30.
Searches 299 results and 419 papers. Newer studies from Europe PMC
Results in people
224
75% of 299 results
Results in animals
60
20% of 299 results
Results in lab cells
15
5% of 299 results
From computer models
0
0% of 299 results
The molecule
Pegvisomant identity
Identifiers, parent molecule, targets and development stage, from curated data.
Pegvisomant is a PEG-conjugated growth hormone analog that antagonizes growth hormone receptors. Its protein has nine substitutions. PEG chains create a distribution of molecular masses.
- Kind
- Conjugate · 191 residues
- Identifiers
- ChEMBLCHEMBL1201515 (opens in a new tab)UNIIN824AOU5XV (opens in a new tab)DrugBankDB00082 (opens in a new tab)CAS218620-50-9
- Parent
- Analog of Human growth hormoneGSRS pegvisomant sequence differs from UniProt P01241 mature human GH at H18D, H21N, G120K, R167N, K168A, D171S, K172R, E174S, and I179T. The US label substitution table reports Ala21 instead of His21. This conflicts with the UniProt parent sequence. UniProt residues 27-217 encode the 191-residue mature parent chain. Pegvisomant adds heterogeneous PEG conjugation. The parent slug remains somatotropin.
- Development
- Approved in the US and EU (Somavert)An approved medicinal product exists. Availability and other indications can differ. Source (opens in a new tab)
Targets
| Target | Action | Evidence |
|---|---|---|
| Growth hormone receptorGHRP10912 (opens in a new tab) | Antagonist | Official prescribing information, mechanism of actionSource (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 · 1 modification
Residues 1 to 10:
FPTIPLSRLF
Residues 11 to 20:
DNAMLRADRL
Residues 21 to 30:
NQLAFDTYQE
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:
YDLLKDLEEK
Residues 121 to 130:
IQTLMGRLED
Residues 131 to 140:
GSPRTGQIFK
Residues 141 to 150:
QTYSKFDTNS
Residues 151 to 160:
HNDDALLKNY
Residues 161 to 170:
GLLYCFNADM
Residues 171 to 180:
SRVSTFLRTV
Residues 181 to 190:
QCRSVEGSCG
Residues 191 to 191:
F
Alignment to Human growth hormone
Calculated from the two sequences. Curated notes are shown as given.
182 of 191 aligned residues identical (95%) · 9 substitutions · Human growth hormone 1–191
- Top row: Human growth hormone (parent)
- Bottom row: Pegvisomant
FPTIPLSRLF
DNAMLRARL
QLAFDTYQE
FEEAYIPKEQ
KYSFLQNPQT
SLCFSESIPT
PSNREETQQK
SNLELLRISL
LLIQSWLEPV
QFLRSVFANS
LVYGASDSNV
YDLLKDLEE
IQTLMGRLED
GSPRTGQIFK
QTYSKFDTNS
HNDDALLKNY
GLLYCFDM
VTFLRV
QCRSVEGSCG
F
- Same as parent
- Substituted
- Non-canonical or D-form
- Added
- Gap
- Modified side chain or end
Differences from the parent
- 1Parent 18 · analog 18His → Asp · Substitution
- 2Parent 21 · analog 21His → Asn · Substitution
- 3Parent 120 · analog 120Gly → Lys · Substitution
- 4Parent 167 · analog 167Arg → Asn · Substitution
- 5Parent 168 · analog 168Lys → Ala · Substitution
- 6Parent 171 · analog 171Asp → Ser · Substitution
- 7Parent 172 · analog 172Lys → Arg · Substitution
- 8Parent 174 · analog 174Glu → Ser · Substitution
- 9Parent 179 · analog 179Ile → Thr · Substitution
Basis: GSRS pegvisomant sequence differs from UniProt P01241 mature human GH at H18D, H21N, G120K, R167N, K168A, D171S, K172R, E174S, and I179T. The US label substitution table reports Ala21 instead of His21. This conflicts with the UniProt parent sequence. UniProt residues 27-217 encode the 191-residue mature parent chain. Pegvisomant adds heterogeneous PEG conjugation. The parent slug remains somatotropin.
Calculated from the two sequences with @pepdb/chem alignToParent (ungapped unless a gap scores higher). The record’s curated notes are shown as given.
Properties
From identity sources
No formula or molecular weight is listed for Pegvisomant.
Calculated from the sequence
Some values cannot be calculated. A modification changes this value and is not modeled here (for example a lipid, metal or linker).
- Average mass
- Not calculated
- Monoisotopic mass
- Not calculated
- Isoelectric point (pI)
- Not calculated
- Net charge at pH 7.4
- Not calculated
- GRAVY (hydropathy)
- −0.399
- 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
- 44.17
- Dipeptide instability weights (DIWV) · Guruprasad et al. 1990
- Above 40: classed as possibly unstable (ExPASy).
- Aliphatic index
- 82.2
- Mole % A + 2.9 V + 3.9 (I + L) · Ikai 1980
- Boman index
- 1.96 kcal/mol
- Mean solubility value (negated) · Boman 2003
- 2.48 or below: lower protein-binding potential (Boman).
- Hydrophobic moment (μH)
- 0.623
- Eisenberg scale, 100° per residue, best 11-residue window · Eisenberg et al. 1982, 1984
- Not included: PEG chain. Mass, charge and pI are not calculated; use the identity-source values.
- 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
No charge curve
A modification changes this value and is not modeled here (for example a lipid, metal or linker).
Composition
- Hydrophobic27% (51)A I L M V
- Aromatic12% (22)F W Y
- Positive10% (20)H K R
- Negative13% (24)D E
- Polar29% (55)N Q S T
- Special10% (19)C G P
191 residues. Each residue counts in one class; F and W count as aromatic.
A Ala8 · 4%
I Ile7 · 4%
L Leu26 · 14%
M Met3 · 2%
V Val7 · 4%
F Phe13 · 7%
W Trp1 · 1%
Y Tyr8 · 4%
H His1 · 1%
K Lys8 · 4%
R Arg11 · 6%
D Asp11 · 6%
E Glu13 · 7%
N Asn11 · 6%
Q Gln13 · 7%
S Ser20 · 10%
T Thr11 · 6%
C Cys4 · 2%
G Gly7 · 4%
P Pro8 · 4%
3D structure
PredictedAlphaFold DB · P01241
Loads the 3D viewer (3Dmol.js, about 150 KB) and the model file from AlphaFold DB (EMBL-EBI).
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
- 0.173
- μH, best 11-residue window
- 0.623
- Arrow direction
- 151°
- 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 | D | 260° | -0.90 |
| 19 | R | 0° | -2.53 |
| 20 | L | 100° | 1.06 |
| 21 | N | 200° | -0.78 |
| 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