Lot certificates published
Plain, secure packaging

Compound monograph

Triptorelin

Triptorelin is a synthetic ten-residue peptide with an L-pyroglutamyl residue at position 1, D-tryptophan at position 6 and a C-terminal glycinamide. This record describes the parent peptide without counterion.

Published: 2026-10-15Literature/identifier verification: 2026-10-15
Also known asTriptorelinum

01

Identity & nomenclature

Triptorelin is a synthetic ten-residue peptide with an L-pyroglutamyl residue at position 1, D-tryptophan at position 6 and a C-terminal glycinamide. This record describes the parent peptide without counterion.

Triptorelin is the WHO international nonproprietary name (Latin triptorelinum). Triptorelin acetate and triptorelin pamoate (embonate) are salt forms with their own registry entries and are not aliases of this record. Bracketed substitution names of the D-Trp6 type, development codes and trade names are not listed because no two independent sources tie each of them to this exact species.

Declared aliases and development codes: Triptorelinum.

02

Molecular properties

Molecular formulaC64H82N18O13
Molecular mass1311.473 Da
CAS Registry Number57773-63-4
PubChem CID25074470
UNII9081Y98W2V
Three-letter sequencepGlu–His–Trp–Ser–Tyr–D-Trp–Leu–Arg–Pro–Gly
Terminal groupsN-terminal pyroglutamate; C-terminal amide at Gly10

Ten residues numbered pGlu1 to Gly10. pGlu is L-pyroglutamyl (5-oxo-L-prolyl), not open-chain glutamate or glutamine. Position 6 is D-tryptophan and every other chiral residue is L; Gly10 is achiral and carries the C-terminal amide. No one-letter string is published because the chain contains a nonstandard residue and a D residue.

03

Structural characteristics

Li et al. (PMID 40726784) synthesized triptorelin and report its full stereochemical structure with chromatographic and mass-spectrometric characterization. Sanz-Nebot et al. (PMID 11404838) characterized a synthesis crude and its side products by liquid chromatography-mass spectrometry. Hövelmann et al. (PMID 11802711) and Nederpelt et al. (PMID 26398856) measured triptorelin binding at the human GnRH receptor. The pyroglutamyl ring lies within residue 1; there is no ring closure between residues.

  • Pyroglutamate at position 1
  • D-tryptophan at position 6

Terminal features: N-terminal pyroglutamate, C-terminal amide at Gly10.

04

Molecular targets & mechanisms

05

Analytical considerations

The molecular formula and the 1311.473 Da average mass are calculated for the counterion-free parent from its structure with CIAAW 2024 abridged atomic weights, and the formula agrees with the WHO and FDA disclosures. The GSRS record for this UNII also lists a non-defining calculated weight of 1140 Da that does not correspond to this structure. The acetate and pamoate registry definitions each add one acid equivalent, so salt preparations differ in mass from the parent.

What the studies reported

No verified findings are published for this record under Content Policy v1.

06

Verified bibliography

Cited studies by type

The 4 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.

  1. Reference 1

    Design and Development of an Organocatalyst for Light Accelerated Amide and Peptide Synthesis.

    Li Y, Li J, Shen Z, Kuang H, Zuo Q, Bao G, Ni J, Sun W, Wang R

    ACS central science · 2025-06-30 · Journal Article

    current
  2. Reference 2

  3. Reference 3

    Impact of aromatic residues within transmembrane helix 6 of the human gonadotropin-releasing hormone receptor upon agonist and antagonist binding.

    Hövelmann S, Hoffmann SH, Kühne R, ter Laak T, Reiländer H, Beckers T

    Biochemistry · 2002-01-29 · Journal Article

    current
  4. Reference 4

    Characterization of 12 GnRH peptide agonists - a kinetic perspective.

    Nederpelt I, Georgi V, Schiele F, Nowak-Reppel K, Fernández-Montalván AE, IJzerman AP, Heitman LH

    British journal of pharmacology · 2015-11-04 · Journal Article

    current

Study models of these references

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

ReferenceStudy models
Li Y et al. 2025Chemical, structural or analytical study; no biological model reported
Sanz-Nebot V et al. 2001Chemical, structural or analytical study; no biological model reported
Hövelmann S et al. 2002Study models reported: in vitro · from the abstract
Nederpelt I et al. 2015Study models reported: in vitro · from the abstract

Record history

Published 2026-10-15.

No changes to this record's content have been recorded since publication.

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. Triptorelin. Published 2026-10-15. https://purelypeptides.org/research/compounds/triptorelin/

10

Methodology & citation verification

Reference identity is checked against official PubMed metadata. Local deterministic receipts bind each normalized title and canonical metadata record to its verification date. Scientific values remain absent when an authoritative source has not been verified.

Read the full methodology →