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Abaloparatide (Tymlos) / Studies
Synthetic analog · 34 amino acids · 3,961 Da

Abaloparatide (Tymlos) studies and research data

PepBank has 157 abaloparatide studies with results. 121 of them gave abaloparatide, with 878 results, grouped by what the studies measured. In each group, results from studies in people come first. Data as of 2026-10-30.

Searches 878 results and 405 papers. Newer studies from Europe PMC

Results in people
381
43% of 878 results
Results in animals
414
47% of 878 results
Results in lab cells
79
9% of 878 results
From computer models
4
under 1% of 878 results
The molecule

Abaloparatide identity

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

Abaloparatide is a 34-residue PTHrP analog and PTH1 receptor agonist. It contains alpha-aminoisobutyric acid at position 29 and a C-terminal amide. Head-to-head trials can test both abaloparatide and teriparatide.

Kind
Synthetic analog · 34 residues
Identifiers
UniProtP12272 (opens in a new tab)PubChem CID76943386 (opens in a new tab)UNIIAVK0I6HY2U (opens in a new tab)DrugBankDB05084 (opens in a new tab)CAS247062-33-5
Parent
Analog of Human parathyroid hormone-related protein · residues 37-70The label identifies a PTHrP(1-34) analog. UniProt P12272 starts mature PTHrP at residue 37. Mature residues 1-34 map to precursor residues 37-70. Substitution positions use mature PTHrP numbering. No parent seed reference is assigned.
Development
Approved in the US and EU (Tymlos)Radius Health, Inc.An 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)Agonistofficial prescribing informationSource (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 · 2 modifications

H-
Residues 1 to 10:
AVSEHQLLHD
Residues 11 to 20:
KGKSIQDLRR
Residues 21 to 30:
RELLEKLLK
Residues 31 to 34:
LHTA
  • HydrophobicA V I L M
  • PositiveK R H
  • NegativeD E
  • PolarS T N Q
  • SpecialC G P
  • Non-canonicalX
  • Modified residue

Modifications

34
C-terminal amide
C-terminal carboxamide.
29
Non-canonical residue
Alpha-aminoisobutyric acid. X denotes this non-canonical residue.

Parent: Human parathyroid hormone-related protein

No sequence is listed for the parent, so no alignment is shown.The label identifies a PTHrP(1-34) analog. UniProt P12272 starts mature PTHrP at residue 37. Mature residues 1-34 map to precursor residues 37-70. Substitution positions use mature PTHrP numbering. No parent seed reference is assigned.

Properties

From identity sources

Formula
C174H300N56O49
Molecular weight
3,961 g/mol
Monoisotopic mass
3,958.2705 Da

Calculated from the sequence

Some values cannot be calculated. The sequence has a non-canonical residue (X). Residue tables cover only the 20 standard amino acids.

Average mass
Not calculated
Monoisotopic mass
Not calculated
Isoelectric point (pI)
Not calculated
Net charge at pH 7.4
Not calculated
GRAVY (hydropathy)
Not calculated
Extinction coefficient, 280 nm (Cys reduced)
0 M⁻¹ cm⁻¹
5500 x Trp + 1490 x Tyr · Pace et al. 1995 (ExPASy ProtParam)
No Trp or Tyr: absorbance at 280 nm cannot measure this peptide.
Instability index
Not calculated
Aliphatic index
Not calculated
Boman index
Not calculated
Hydrophobic moment (μH)
Not calculated
  • 1 non-canonical residue (X) is not included in calculated 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

The sequence has a non-canonical residue (X). Residue tables cover only the 20 standard amino acids.

Composition

  • Hydrophobic35% (12)
  • Positive29% (10)
  • Negative15% (5)
  • Polar15% (5)
  • Special3% (1)
  • Non-canonical3% (1)

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

A Ala2 · 6%
I Ile1 · 3%
L Leu8 · 24%
M Met0 · 0%
V Val1 · 3%
F Phe0 · 0%
W Trp0 · 0%
Y Tyr0 · 0%
H His3 · 9%
K Lys4 · 12%
R Arg3 · 9%
D Asp2 · 6%
E Glu3 · 9%
N Asn0 · 0%
Q Gln2 · 6%
S Ser2 · 6%
T Thr1 · 3%
C Cys0 · 0%
G Gly1 · 3%
P Pro0 · 0%
X Xaa1 · 3%

3D structure

PredictedAlphaFold DB · P12272

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 P12272, not an experimental structure of Abaloparatide (Tymlos). Abaloparatide (Tymlos) = residues 37–70.

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

2D structure

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

SMILES fromPubChem CID 76943386(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(=O)O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)NC(C)(C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC1=CN=CN1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C)C(=O)N)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)CNC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CC2=CN=CN2)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(=O)N)NC(=O)[C@H](CC3=CN=CN3)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CO)NC(=O)[C@H](C(C)C)NC(=O)[C@H](C)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 Abaloparatide (Tymlos), 34 residues at 100 degrees per residue. Hydrophobic moment 0.03 pointing at 33 degrees.Ala 1, Eisenberg consensus (normalized) 0.62A1Val 2, Eisenberg consensus (normalized) 1.08V2Ser 3, Eisenberg consensus (normalized) -0.18S3Glu 4, Eisenberg consensus (normalized) -0.74E−4His 5, Eisenberg consensus (normalized) -0.40H5Gln 6, Eisenberg consensus (normalized) -0.85Q6Leu 7, Eisenberg consensus (normalized) 1.06L7Leu 8, Eisenberg consensus (normalized) 1.06L8His 9, Eisenberg consensus (normalized) -0.40H9Asp 10, Eisenberg consensus (normalized) -0.90D−10Lys 11, Eisenberg consensus (normalized) -1.50K+11Gly 12, Eisenberg consensus (normalized) 0.48G12Lys 13, Eisenberg consensus (normalized) -1.50K+13Ser 14, Eisenberg consensus (normalized) -0.18S14Ile 15, Eisenberg consensus (normalized) 1.38I15Gln 16, Eisenberg consensus (normalized) -0.85Q16Asp 17, Eisenberg consensus (normalized) -0.90D−17Leu 18, Eisenberg consensus (normalized) 1.06L18Arg 19, Eisenberg consensus (normalized) -2.53R+19Arg 20, Eisenberg consensus (normalized) -2.53R+20Arg 21, Eisenberg consensus (normalized) -2.53R+21Glu 22, Eisenberg consensus (normalized) -0.74E−22Leu 23, Eisenberg consensus (normalized) 1.06L23Leu 24, Eisenberg consensus (normalized) 1.06L24Glu 25, Eisenberg consensus (normalized) -0.74E−25Lys 26, Eisenberg consensus (normalized) -1.50K+26Leu 27, Eisenberg consensus (normalized) 1.06L27Leu 28, Eisenberg consensus (normalized) 1.06L28Non-canonical 29X29Lys 30, Eisenberg consensus (normalized) -1.50K+30Leu 31, Eisenberg consensus (normalized) 1.06L31His 32, Eisenberg consensus (normalized) -0.40H32Thr 33, Eisenberg consensus (normalized) -0.05T33Ala 34, Eisenberg consensus (normalized) 0.62A34
μH, residues shown
0.032
μH, best 11-residue window
—
Arrow direction
33°
Residues
34 · 2 rings of 18 · 1 X not scored
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)
1A0°0.62
2V100°1.08
3S200°-0.18
4E300°-0.74
5H40°-0.40
6Q140°-0.85
7L240°1.06
8L340°1.06
9H80°-0.40
10D180°-0.90
11K280°-1.50
12G20°0.48
13K120°-1.50
14S220°-0.18
15I320°1.38
16Q60°-0.85
17D160°-0.90
18L260°1.06
19R0°-2.53
20R100°-2.53
21R200°-2.53
22E300°-0.74
23L40°1.06
24L140°1.06
25E240°-0.74
26K340°-1.50
27L80°1.06
28L180°1.06
29X280°not scored
30K20°-1.50
31L120°1.06
32H220°-0.40
33T320°-0.05
34A60°0.62
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