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Teriparatide (PTH 1-34) / Studies
Natural fragment · 34 amino acids · 4,118 Da

Teriparatide (PTH 1-34) studies and research data

PepBank has 484 teriparatide studies with results. 430 of them gave teriparatide, with 2,709 results, grouped by what the studies measured. In each group, results from studies in people come first. Data as of 2026-10-30.

Searches 2,709 results and 1,327 papers. Newer studies from Europe PMC

Results in people
1,667
62% of 2,709 results
Results in animals
997
37% of 2,709 results
Results in lab cells
42
2% of 2,709 results
From computer models
3
under 1% of 2,709 results
The molecule

Teriparatide identity

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

Teriparatide matches residues 1 to 34 of mature human parathyroid hormone. It is a PTH1 receptor agonist. It differs from intact PTH and long-acting PTH prodrugs. The sequence is a natural fragment, irrespective of manufacturing method.

Kind
Natural fragment · 34 residues
Identifiers
UniProtP01270 (opens in a new tab)PubChem CID16133850 (opens in a new tab)UNII10T9CSU89I (opens in a new tab)DrugBankDB06285 (opens in a new tab)CAS52232-67-4
Parent
Fragment of Human parathyroid hormone · residues 32-65The 34-residue sequence matches UniProt P01270 residues 32-65 and mature hormone residues 1-34. This record does not link a parent seed record.
Development
Approved in the US and EU (Forteo)Eli Lilly and CompanyAn approved medicinal product exists. Investigational indications and formulations have separate development status. Source (opens in a new tab)

Targets

Molecular targets with action and evidence source
TargetActionEvidence
Parathyroid hormone 1 receptorPTH1RQ03431 (opens in a new tab)AgonistIUPHAR/BPS curated receptor assay dataSource (opens in a new tab)
Parathyroid hormone 2 receptorPTH2RP49190 (opens in a new tab)AgonistIUPHAR/BPS curated receptor assay dataSource (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

H-
Residues 1 to 10:
SVSEIQLMHN
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

Parent: Human parathyroid hormone

No sequence is listed for the parent, so no alignment is shown.The 34-residue sequence matches UniProt P01270 residues 32-65 and mature hormone residues 1-34. This record does not link a parent seed record.

Properties

From identity sources

Formula
C181H291N55O51S2
Molecular weight
4,118 g/mol
Monoisotopic mass
4,115.1309 Da

Calculated from the sequence

Average mass
4,117.76 Da
Sum of ExPASy residue masses + water · ExPASy Compute pI/Mw; FindMod
Monoisotopic mass
4,115.1309 Da
Sum of ExPASy residue masses + water · ExPASy FindMod
Isoelectric point (pI)
9.44
pH of zero net charge, EMBOSS pKa set · EMBOSS iep, Epk.dat
Net charge at pH 7.4
1.28
Henderson-Hasselbalch, EMBOSS pKa set · EMBOSS iep, Epk.dat
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
pI with each pKa set
EMBOSS 9.44Bjellqvist (ExPASy) 8.29IPC peptide 9.72IPC protein 8.59
  • 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 9.44 · Net charge at pH 7.4: 1.28

Point or use arrow keys

Net charge of Teriparatide (PTH 1-34) from pH 0 to 14 (EMBOSS pKa set). Isoelectric point 9.44. Net charge at pH 7.4: 1.28.−50+5+1002468101214pHNet chargepH 7.4pI 9.44

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

Show as table
pHNet charge
09.00
18.99
28.94
38.47
46.39
54.36
63.33
71.70
80.89
90.25
10−0.38
11−1.90
12−3.30
13−4.50
14−4.94

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 Teriparatide (PTH 1-34). Teriparatide (PTH 1-34) = residues 32–65.

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

2D structure

Teriparatide (PTH 1-34) has 34 residues. A full-atom drawing is hard to read at this size; the sequence view is the reference.

SMILES fromPubChem CID 16133850(opens in a new tab)

CC[C@H](C)[C@@H](C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC2=CNC=N2)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC3=CNC4=CC=CC=C43)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)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(C)C)C(=O)N[C@@H](CC5=CNC=N5)C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](CC6=CC=CC=C6)C(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CO)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CO)N

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 Teriparatide (PTH 1-34), 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