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Vosoritide / Studies
Synthetic analog · 39 amino acids · 4,103 Da

Vosoritide studies and research data

PepBank has 50 vosoritide studies with results. All of them gave vosoritide, with 306 results, grouped by what the studies measured. In each group, results from studies in people come first. Data as of 2026-10-30.

Searches 306 results and 90 papers. Newer studies from Europe PMC

Results in people
290
95% of 306 results
Results in animals
14
5% of 306 results
Results in lab cells
2
under 1% of 306 results
From computer models
0
0% of 306 results
The molecule

Vosoritide identity

Identifiers, parent molecule, targets and development stage, from curated data.

Vosoritide is a 39-residue C-type natriuretic peptide analog made with recombinant DNA technology in Escherichia coli. It adds Pro-Gly to the 37 C-terminal residues of CNP53. It activates natriuretic peptide receptor B.

Kind
Synthetic analog · 39 residues
Identifiers
ChEMBLCHEMBL3707276 (opens in a new tab)PubChem CID119058036 (opens in a new tab)UNII7SE5582Q2P (opens in a new tab)DrugBankDB11928 (opens in a new tab)CAS1480724-61-5
Parent
Analog of C-type natriuretic peptideVosoritide is a 39-residue C-type natriuretic peptide analog. It adds Pro-Gly to the 37 C-terminal residues of CNP53. It activates natriuretic peptide receptor B.
Development
Approved in the US and EU (Voxzogo)BioMarin Pharmaceutical Inc.Voxzogo is approved for pediatric achondroplasia with open epiphyses. Other indications remain separate. BioMarin manufactures the US product. Source (opens in a new tab)

Targets

Molecular targets with action and evidence source
TargetActionEvidence
Natriuretic peptide receptor BNPR2P20594 (opens in a new tab)AgonistOfficial 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

39 amino acids · 1 disulfide bond

H-
Residues 1 to 10:
PGQEHPNARK
Residues 11 to 20:
YKGANKKGLS
Residues 21 to 30:
KGCFGLKLDR
Residues 31 to 39:
IGSMSGLGC
-OH
  • HydrophobicA V I L M
  • AromaticF W Y
  • PositiveK R H
  • NegativeD E
  • PolarS T N Q
  • SpecialC G P
  • Disulfide partner

Modifications

Cys23–Cys39
Disulfide bond

Parent: C-type natriuretic peptide

No sequence is listed for the parent, so no alignment is shown.Vosoritide is a 39-residue C-type natriuretic peptide analog. It adds Pro-Gly to the 37 C-terminal residues of CNP53. It activates natriuretic peptide receptor B.

Properties

From identity sources

Formula
C176H290N56O51S3
Molecular weight
4,103 g/mol
Monoisotopic mass
4,100.0983 Da

Calculated from the sequence

Average mass
4,102.76 Da
Sum of ExPASy residue masses + water + 1 disulfide · ExPASy Compute pI/Mw; FindMod
Monoisotopic mass
4,100.0982 Da
Sum of ExPASy residue masses + water + 1 disulfide · ExPASy FindMod
Isoelectric point (pI)
11.11
pH of zero net charge, EMBOSS pKa set · EMBOSS iep, Epk.dat
Net charge at pH 7.4
6.05
Henderson-Hasselbalch, EMBOSS pKa set · EMBOSS iep, Epk.dat
GRAVY (hydropathy)
−0.774
Mean Kyte-Doolittle hydropathy · Kyte and Doolittle 1982
Negative: hydrophilic on average.
Extinction coefficient, 280 nm (Cys reduced)
1,490 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.
Extinction coefficient, 280 nm (all Cys as cystines)
1,615 M⁻¹ cm⁻¹
5500 x Trp + 1490 x Tyr + 125 x cystine · Pace et al. 1995 (ExPASy ProtParam)
Instability index
14.35
Dipeptide instability weights (DIWV) · Guruprasad et al. 1990
40 or below: classed as stable (ExPASy).
Aliphatic index
55.1
Mole % A + 2.9 V + 3.9 (I + L) · Ikai 1980
Boman index
1.77 kcal/mol
Mean solubility value (negated) · Boman 2003
2.48 or below: lower protein-binding potential (Boman).
Hydrophobic moment (μH)
0.478
Eisenberg scale, 100° per residue, best 11-residue window · Eisenberg et al. 1982, 1984
pI with each pKa set
EMBOSS 11.11Bjellqvist (ExPASy) 10.39IPC peptide 10.86IPC protein 9.79
  • 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 11.11 · Net charge at pH 7.4: 6.05

Point or use arrow keys

Net charge of Vosoritide from pH 0 to 14 (EMBOSS pKa set). Isoelectric point 11.11. Net charge at pH 7.4: 6.05.−50+5+1002468101214pHNet chargepH 7.4pI 11.11

Henderson-Hasselbalch, EMBOSS pKa set, 1 disulfide. Calculated, not measured.

Show as table
pHNet charge
010.00
110.00
29.96
39.61
48.28
57.19
66.78
76.22
85.81
95.12
103.77
110.38
12−2.11
13−3.48
14−3.93

Composition

  • Hydrophobic21% (8)
  • Aromatic5% (2)
  • Positive23% (9)
  • Negative5% (2)
  • Polar15% (6)
  • Special31% (12)

39 residues. Each residue counts in one class; F and W count as aromatic.

A Ala2 · 5%
I Ile1 · 3%
L Leu4 · 10%
M Met1 · 3%
V Val0 · 0%
F Phe1 · 3%
W Trp0 · 0%
Y Tyr1 · 3%
H His1 · 3%
K Lys6 · 15%
R Arg2 · 5%
D Asp1 · 3%
E Glu1 · 3%
N Asn2 · 5%
Q Gln1 · 3%
S Ser3 · 8%
T Thr0 · 0%
C Cys2 · 5%
G Gly8 · 21%
P Pro2 · 5%

3D structure

PredictedAlphaFold DB · P23582

Loads the 3D viewer (3Dmol.js, about 150 KB) and the model file from AlphaFold DB (EMBL-EBI).

  • Very high (pLDDT > 90)
  • Confident (90 > pLDDT > 70)
  • Low (70 > pLDDT > 50)
  • Very low (pLDDT < 50)

Predicted model of the whole UniProt entry P23582, not an experimental structure of Vosoritide.

AlphaFold DB, EMBL-EBI and Google DeepMind · CC BY 4.0

2D structure

Vosoritide has 39 residues. A full-atom drawing is hard to read at this size; the sequence view is the reference.

SMILES fromPubChem CID 119058036(opens in a new tab)

CC[C@H](C)[C@H]1C(=O)NCC(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)NCC(=O)N[C@H](C(=O)NCC(=O)N[C@@H](CSSC[C@@H](C(=O)N[C@H](C(=O)NCC(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N1)CCCNC(=N)N)CC(=O)O)CC(C)C)CCCCN)CC(C)C)CC2=CC=CC=C2)NC(=O)CNC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(=O)N)NC(=O)[C@H](C)NC(=O)CNC(=O)[C@H](CCCCN)NC(=O)[C@H](CC3=CC=C(C=C3)O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](C)NC(=O)[C@H](CC(=O)N)NC(=O)[C@@H]4CCCN4C(=O)[C@H](CC5=CN=CN5)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)N)NC(=O)CNC(=O)[C@@H]6CCCN6)C(=O)O)CC(C)C)CO)CCSC)CO

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.

Helical wheel of Vosoritide, 39 residues at 100 degrees per residue. Hydrophobic moment 0.09 pointing at 251 degrees.Pro 1, Eisenberg consensus (normalized) 0.12P1Gly 2, Eisenberg consensus (normalized) 0.48G2Gln 3, Eisenberg consensus (normalized) -0.85Q3Glu 4, Eisenberg consensus (normalized) -0.74E−4His 5, Eisenberg consensus (normalized) -0.40H5Pro 6, Eisenberg consensus (normalized) 0.12P6Asn 7, Eisenberg consensus (normalized) -0.78N7Ala 8, Eisenberg consensus (normalized) 0.62A8Arg 9, Eisenberg consensus (normalized) -2.53R+9Lys 10, Eisenberg consensus (normalized) -1.50K+10Tyr 11, Eisenberg consensus (normalized) 0.26Y11Lys 12, Eisenberg consensus (normalized) -1.50K+12Gly 13, Eisenberg consensus (normalized) 0.48G13Ala 14, Eisenberg consensus (normalized) 0.62A14Asn 15, Eisenberg consensus (normalized) -0.78N15Lys 16, Eisenberg consensus (normalized) -1.50K+16Lys 17, Eisenberg consensus (normalized) -1.50K+17Gly 18, Eisenberg consensus (normalized) 0.48G18Leu 19, Eisenberg consensus (normalized) 1.06L19Ser 20, Eisenberg consensus (normalized) -0.18S20Lys 21, Eisenberg consensus (normalized) -1.50K+21Gly 22, Eisenberg consensus (normalized) 0.48G22Cys 23, Eisenberg consensus (normalized) 0.29C23Phe 24, Eisenberg consensus (normalized) 1.19F24Gly 25, Eisenberg consensus (normalized) 0.48G25Leu 26, Eisenberg consensus (normalized) 1.06L26Lys 27, Eisenberg consensus (normalized) -1.50K+27Leu 28, Eisenberg consensus (normalized) 1.06L28Asp 29, Eisenberg consensus (normalized) -0.90D−29Arg 30, Eisenberg consensus (normalized) -2.53R+30Ile 31, Eisenberg consensus (normalized) 1.38I31Gly 32, Eisenberg consensus (normalized) 0.48G32Ser 33, Eisenberg consensus (normalized) -0.18S33Met 34, Eisenberg consensus (normalized) 0.64M34Ser 35, Eisenberg consensus (normalized) -0.18S35Gly 36, Eisenberg consensus (normalized) 0.48G36Leu 37, Eisenberg consensus (normalized) 1.06L37Gly 38, Eisenberg consensus (normalized) 0.48G38Cys 39, Eisenberg consensus (normalized) 0.29C39
μH, residues shown
0.090
μH, best 11-residue window
0.478
Arrow direction
251°
Residues
39 · 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
PositionResidueAngleEisenberg consensus (normalized)
1P0°0.12
2G100°0.48
3Q200°-0.85
4E300°-0.74
5H40°-0.40
6P140°0.12
7N240°-0.78
8A340°0.62
9R80°-2.53
10K180°-1.50
11Y280°0.26
12K20°-1.50
13G120°0.48
14A220°0.62
15N320°-0.78
16K60°-1.50
17K160°-1.50
18G260°0.48
19L0°1.06
20S100°-0.18
21K200°-1.50
22G300°0.48
23C40°0.29
24F140°1.19
25G240°0.48
26L340°1.06
27K80°-1.50
28L180°1.06
29D280°-0.90
30R20°-2.53
31I120°1.38
32G220°0.48
33S320°-0.18
34M60°0.64
35S160°-0.18
36G260°0.48
37L0°1.06
38G100°0.48
39C200°0.29
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
Status and safety
Data