Compound monograph

Teriparatide

Teriparatide is the linear 34-residue peptide corresponding to residues 1-34 of human parathyroid hormone, with a free amino terminus and a free C-terminal carboxyl group. This record describes the peptide without counterion.

Published: 2026-10-15Last updated: 2026-10-16Literature/identifier verification: 2026-10-16

Also known asHuman parathyroid hormone (1-34)

Identity & nomenclature

PTH(1-34) without a species prefix, and PTH alone, do not identify this molecule: other species' fragments differ in sequence, and the intact hormone has 84 residues. Acetate-containing preparations are separate species. Brewer et al. (PMID 4509319) reported a 1972 human sequence with glutamine at position 22, lysine at 28 and leucine at 30; Niall et al. (PMID 4521809) reported a sequence differing at those three positions and concluded theirs was correct. This record follows the sequence in the 2000 crystal structure and current regulatory disclosures, with glutamate at 22, leucine at 28 and aspartate at 30. PubChem CIDs 16133850 and 16132393 encode this structure with different histidine tautomer representations; 16133850 is used here.

Declared aliases and development codes: Human parathyroid hormone (1-34).

Molecular properties

Molecular formula	C181H291N55O51S2
Molecular mass	4117.773 Da
CAS Registry Number	52232-67-4
PubChem CID	16133850
UNII	10T9CSU89I
One-letter sequence	SVSEIQLMHNLGKHLNSMERVEWLRKKLQDVHNF
Three-letter sequence	Ser–Val–Ser–Glu–Ile–Gln–Leu–Met–His–Asn–Leu–Gly–Lys–His–Leu–Asn–Ser–Met–Glu–Arg–Val–Glu–Trp–Leu–Arg–Lys–Lys–Leu–Gln–Asp–Val–His–Asn–Phe
Terminal groups	Free N-terminal amino group; Free C-terminal carboxyl group

Thirty-four residues numbered Ser1 to Phe34, corresponding to residues 1-34 of the mature human hormone. Every chiral residue is L; Gly12 is achiral.

Structural characteristics

Jin et al. (PMID 10837469) determined the crystal structure of human parathyroid hormone 1-34 at 0.9 Å resolution. Frolik et al. (PMID 9933468) measured binding of recombinant human PTH(1-34) at the human PTH/PTHrP receptor expressed in a human kidney cell line. The chain contains no cysteine and no covalent ring.

Terminal features: Free N-terminal amino group, Free C-terminal carboxyl group.

Molecular targets & mechanisms

Parathyroid hormone 1 receptor

PTH1R · PTH/PTHrP receptor

PTH1R is a class B G-protein-coupled receptor encoded by PTH1R and also called the PTH/PTHrP receptor. The record linked here cites a direct binding measurement made at the human receptor expressed in a human kidney cell line.

Analytical considerations

The molecular formula and the 4117.773 Da average mass are calculated from the sequence with CIAAW 2024 abridged atomic weights; the neutral monoisotopic mass calculated from the same formula is 4115.131 Da. Kovács et al. (PMID 31595483) reported a theoretical monoisotopic mass of 4115.1309 Da for the teriparatide molecule. The GSRS record for this UNII lists a non-defining estimated formula, C181H287N55O50S2, which lacks four hydrogens and one oxygen relative to this structure. Oxidized, deamidated and truncated forms are separate species; oxidation of one methionine adds 16 Da.

What the studies reported

Each finding describes one cited study in its stated model. These observations are specific to that study and do not establish effects in other settings.

Cell and tissue studies

Recombinant human PTH-R1 extracellular-domain fragment in a competitive ELISA
Kovács et al. observed teriparatide displacement of biotinylated PTH(1-34) from the recombinant human PTH-R1 extracellular-domain fragment spanning residues 23-189 in a competitive ELISA.
Reference [5]
Rat UMR-106 and human Saos-2 osteosarcoma cells in cAMP-release assays
Kovács et al. measured teriparatide-associated cAMP release in rat UMR-106 and human Saos-2 osteosarcoma cells using enzyme-fragment-complementation assays.
Reference [5]

Animal studies

Young male Fisher rats in bone-mass assays
Frolik et al. observed increased trabecular and cortical bone mass in young male Fisher rats receiving recombinant human PTH(1-34) in a study using bone densitometry and histomorphometry.
Reference [2]

Verified bibliography

Cited studies by type

The 5 papers this record cites, counted by the kind of work each reports. A count is the size of this record's selection, not of the research that exists, and says nothing about results, safety, effectiveness or approval.

A paper can report more than one kind of work. Each count opens those papers in the bibliography. Compare every record on the Evidence Map.

Reference 1
Crystal structure of human parathyroid hormone 1-34 at 0.9-A resolution.
Jin L, Briggs SL, Chandrasekhar S, Chirgadze NY, Clawson DK, Schevitz RW, Smiley DL, Tashjian AH, Zhang F
The Journal of biological chemistry · 2000-09-01 · Journal Article
current
PMID 10837469 DOI 10.1074/jbc.M001134200 Teriparatide
Reference 2
Comparison of recombinant human PTH(1-34) (LY333334) with a C-terminally substituted analog of human PTH-related protein(1-34) (RS-66271): In vitro activity and in vivo pharmacological effects in rats.
Frolik CA, Cain RL, Sato M, Harvey AK, Chandrasekhar S, Black EC, Tashjian AH Jr, Hock JM
Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 1999-02 · Journal Article
current
PMID 9933468 DOI 10.1359/jbmr.1999.14.2.163 Teriparatide PTH1R
Reference 3
Human parathyroid hormone: amino-acid sequence of the amino-terminal residues 1-34.
Brewer HB Jr, Fairwell T, Ronan R, Sizemore GW, Arnaud CD
Proceedings of the National Academy of Sciences of the United States of America · 1972-12 · Journal Article
current
PMID 4509319 PMC389826 DOI 10.1073/pnas.69.12.3585 Teriparatide
Reference 4
The amino-acid sequence of the amino-terminal 37 residues of human parathyroid hormone.
Niall HD, Sauer RT, Jacobs JW, Keutmann HT, Segre GV, O'Riordan JL, Aurbach GD, Potts JT Jr
Proceedings of the National Academy of Sciences of the United States of America · 1974-02 · Journal Article
current
PMID 4521809 PMC388010 DOI 10.1073/pnas.71.2.384 Teriparatide
Reference 5
Comparative Physicochemical and Biological Characterisation of the Similar Biological Medicinal Product Teriparatide and Its Reference Medicinal Product.
Kovács P, Schäfer T, Háda V, Hevér H, Klingelhöfer S, Nebel M, Stadie T, Kiss R, Urbányi Z
BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2020-02 · Comparative Study
current
PMID 31595483 PMC6985066 DOI 10.1007/s40259-019-00386-x Teriparatide PTH1R

Study models of these references

What kind of experiment each cited paper reports, taken from its abstract unless marked. Not a summary of results.

Reference	Study models
Jin L et al. 2000	Chemical, structural or analytical study; no biological model reported
Frolik CA et al. 1999	Study models reported: in vitro; animal (rat) · from the abstract
Brewer HB Jr et al. 1972	Chemical, structural or analytical study; no biological model reported
Niall HD et al. 1974	Chemical, structural or analytical study; no biological model reported
Kovács P et al. 2020	Study models reported: in vitro · from the abstract

Record history

Published 2026-10-15.

2026-10-16: Analytical notes, References

Each entry names the parts of this record that changed on that date. Changes to links between records and to catalogue links are not listed. This history covers the tracked record fields; study findings are not listed here.

Cite this record: Purely Peptides Research Library. Teriparatide. Published 2026-10-15; updated 2026-10-16. https://purelypeptides.org/research/compounds/teriparatide/

Methodology & citation verification

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