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Palopegteriparatide / Studies
Conjugate · 34 amino acids

Palopegteriparatide studies and research data

PepBank has 25 palopegteriparatide studies with results. All of them gave palopegteriparatide, with 210 results, grouped by what the studies measured. In each group, results from studies in people come first. Data as of 2026-10-30.

Searches 210 results and 37 papers. Newer studies from Europe PMC

Results in people
193
92% of 210 results
Results in animals
17
8% of 210 results
Results in lab cells
0
0% of 210 results
From computer models
0
0% of 210 results
The molecule

Palopegteriparatide identity

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

Palopegteriparatide is a prodrug that releases PTH(1-34), or teriparatide. A cleavable linker joins the peptide to a methoxypolyethylene glycol carrier. Its label concerns adult hypoparathyroidism.

Kind
Conjugate · 34 residues
Identifiers
ChEMBLCHEMBL5095475 (opens in a new tab)UNIIG2N64C3385 (opens in a new tab)CAS2222514-07-8
Parent
Analog of TeriparatideTeriparatide is the released active peptide of this conjugated prodrug. It matches PTH(1-34), corresponding to UniProt P01270 precursor residues 32-65. The parent link does not identify the full conjugate as unconjugated teriparatide.
Development
Approved in the US and EU (Yorvipath, 2024)An approved medicinal product exists. Availability and other indications can differ. Source (opens in a new tab)

Targets

Molecular targets with action and evidence source
TargetActionEvidence
Parathyroid hormone 1 receptorPTH1RQ03431 (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

34 amino acids · 1 modification

Residues 1 to 10:
VSEIQLMHN
Residues 11 to 20:
LGKHLNSMER
Residues 21 to 30:
VEWLRKKLQD
Residues 31 to 34:
VHNF
-OH
  • HydrophobicA V I L M
  • AromaticF W Y
  • PositiveK R H
  • NegativeD E
  • PolarS T N Q
  • SpecialC G P
  • Modified residue

Modifications

N-terminal Ser1
PEGylation
The N-terminal amino group of PTH(1-34) connects through a cleavable TransCon linker to branched mPEG. It is not free in the prodrug.

Alignment to Teriparatide

Calculated from the two sequences. Curated notes are shown as given.

34 of 34 aligned residues identical (100%) · 1 modified residue · Teriparatide 1–34

  • Top row: Teriparatide (parent)
  • Bottom row: Palopegteriparatide
VSEIQLMHN
LGKHLNSMER
VEWLRKKLQD
VHNF
  • Same as parent
  • Substituted
  • Non-canonical or D-form
  • Added
  • Gap
  • Modified side chain or end

Differences from the parent

  1. 1Parent 1 · analog 1Ser, modified · PEGylationThe N-terminal amino group of PTH(1-34) connects through a cleavable TransCon linker to branched mPEG. It is not free in the prodrug.

Basis: Teriparatide is the released active peptide of this conjugated prodrug. It matches PTH(1-34), corresponding to UniProt P01270 precursor residues 32-65. The parent link does not identify the full conjugate as unconjugated teriparatide.

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 Palopegteriparatide.

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)
−0.671
Mean Kyte-Doolittle hydropathy · Kyte and Doolittle 1982
Negative: hydrophilic on average.
Extinction coefficient, 280 nm (Cys reduced)
5,500 M⁻¹ cm⁻¹
5500 x Trp + 1490 x Tyr · Pace et al. 1995 (ExPASy ProtParam)
Instability index
62.52
Dipeptide instability weights (DIWV) · Guruprasad et al. 1990
Above 40: classed as possibly unstable (ExPASy).
Aliphatic index
94.4
Mole % A + 2.9 V + 3.9 (I + L) · Ikai 1980
Boman index
2.30 kcal/mol
Mean solubility value (negated) · Boman 2003
2.48 or below: lower protein-binding potential (Boman).
Hydrophobic moment (μH)
0.635
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.
  • The N-terminal group is not modeled.
  • 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

  • Hydrophobic32% (11)
  • Aromatic6% (2)
  • Positive24% (8)
  • Negative12% (4)
  • Polar24% (8)
  • Special3% (1)

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

A Ala0 · 0%
I Ile1 · 3%
L Leu5 · 15%
M Met2 · 6%
V Val3 · 9%
F Phe1 · 3%
W Trp1 · 3%
Y Tyr0 · 0%
H His3 · 9%
K Lys3 · 9%
R Arg2 · 6%
D Asp1 · 3%
E Glu3 · 9%
N Asn3 · 9%
Q Gln2 · 6%
S Ser3 · 9%
T Thr0 · 0%
C Cys0 · 0%
G Gly1 · 3%
P Pro0 · 0%

3D structure

PredictedAlphaFold DB · P01270

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 P01270, not an experimental structure of Palopegteriparatide.

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

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 Palopegteriparatide, 34 residues at 100 degrees per residue. Hydrophobic moment 0.01 pointing at 172 degrees.Ser 1, Eisenberg consensus (normalized) -0.18S1Val 2, Eisenberg consensus (normalized) 1.08V2Ser 3, Eisenberg consensus (normalized) -0.18S3Glu 4, Eisenberg consensus (normalized) -0.74E−4Ile 5, Eisenberg consensus (normalized) 1.38I5Gln 6, Eisenberg consensus (normalized) -0.85Q6Leu 7, Eisenberg consensus (normalized) 1.06L7Met 8, Eisenberg consensus (normalized) 0.64M8His 9, Eisenberg consensus (normalized) -0.40H9Asn 10, Eisenberg consensus (normalized) -0.78N10Leu 11, Eisenberg consensus (normalized) 1.06L11Gly 12, Eisenberg consensus (normalized) 0.48G12Lys 13, Eisenberg consensus (normalized) -1.50K+13His 14, Eisenberg consensus (normalized) -0.40H14Leu 15, Eisenberg consensus (normalized) 1.06L15Asn 16, Eisenberg consensus (normalized) -0.78N16Ser 17, Eisenberg consensus (normalized) -0.18S17Met 18, Eisenberg consensus (normalized) 0.64M18Glu 19, Eisenberg consensus (normalized) -0.74E−19Arg 20, Eisenberg consensus (normalized) -2.53R+20Val 21, Eisenberg consensus (normalized) 1.08V21Glu 22, Eisenberg consensus (normalized) -0.74E−22Trp 23, Eisenberg consensus (normalized) 0.81W23Leu 24, Eisenberg consensus (normalized) 1.06L24Arg 25, Eisenberg consensus (normalized) -2.53R+25Lys 26, Eisenberg consensus (normalized) -1.50K+26Lys 27, Eisenberg consensus (normalized) -1.50K+27Leu 28, Eisenberg consensus (normalized) 1.06L28Gln 29, Eisenberg consensus (normalized) -0.85Q29Asp 30, Eisenberg consensus (normalized) -0.90D−30Val 31, Eisenberg consensus (normalized) 1.08V31His 32, Eisenberg consensus (normalized) -0.40H32Asn 33, Eisenberg consensus (normalized) -0.78N33Phe 34, Eisenberg consensus (normalized) 1.19F34
μH, residues shown
0.014
μH, best 11-residue window
0.635
Arrow direction
172°
Residues
34 · 2 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)
1S0°-0.18
2V100°1.08
3S200°-0.18
4E300°-0.74
5I40°1.38
6Q140°-0.85
7L240°1.06
8M340°0.64
9H80°-0.40
10N180°-0.78
11L280°1.06
12G20°0.48
13K120°-1.50
14H220°-0.40
15L320°1.06
16N60°-0.78
17S160°-0.18
18M260°0.64
19E0°-0.74
20R100°-2.53
21V200°1.08
22E300°-0.74
23W40°0.81
24L140°1.06
25R240°-2.53
26K340°-1.50
27K80°-1.50
28L180°1.06
29Q280°-0.85
30D20°-0.90
31V120°1.08
32H220°-0.40
33N320°-0.78
34F60°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
Status and safety
Data