CompletedPhase 4NCT02892942
NATural Ovarian Stimulation
Assistance Publique - Hôpitaux de Parisn = 12913 Jan 2017 to 8 Feb 2019
Infertility
Cetrorelix / Studies
Synthetic analog · 10 amino acids · 1,431 Da
Cetrorelix studies and research data
PepBank has 83 cetrorelix studies with results. 82 of them gave cetrorelix, with 486 results, grouped by what the studies measured. In each group, results from studies in people come first. Data as of 2026-10-30.
Searches 486 results and 523 papers. Newer studies from Europe PMC
Results in people
436
90% of 486 results
Results in animals
40
8% of 486 results
Results in lab cells
10
2% of 486 results
From computer models
0
0% of 486 results
The molecule
Cetrorelix identity
Identifiers, parent molecule, targets and development stage, from curated data.
Cetrorelix is a ten-residue GnRH receptor antagonist. It prevents premature luteinizing hormone surges during controlled ovarian stimulation.
- Kind
- Synthetic analog · 10 residues
- Identifiers
- ChEMBLCHEMBL1200490 (opens in a new tab)PubChem CID25074887 (opens in a new tab)UNIIOON1HFZ4BA (opens in a new tab)DrugBankDB00050 (opens in a new tab)CAS120287-85-6
- Parent
- Analog of GonadorelinThe US label identifies cetrorelix as a native GnRH analog with substitutions at residues 1, 2, 3, 6, and 10. UniProt P01148 identifies human gonadorelin within its precursor. No parent span is asserted.
- Development
- Approved in the US and EU (Cetrotide)An approved medicinal product exists. Availability and other indications can differ. Source (opens in a new tab)
Targets
| Target | Action | Evidence |
|---|---|---|
| Gonadotropin-releasing hormone receptorGNRHRP30968 (opens in a new tab) | Antagonist | Official 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
10 amino acids · 5 modifications
Residues 1 to 10:
SYLRP
Alignment to Gonadorelin
Calculated from the two sequences. Curated notes are shown as given.
5 of 10 aligned residues identical (50%) · 5 non-canonical residues · Gonadorelin 1–10
- Top row: Gonadorelin (parent)
- Bottom row: Cetrorelix
SYLRP
- Same as parent
- Substituted
- Non-canonical or D-form
- Added
- Gap
- Modified side chain or end
Differences from the parent
- 1Parent 1 · analog 1Xaa → D-2-Nal · Non-canonical residueD-2-Nal
- 2Parent 2 · analog 2His → D-4-Cl-Phe · Non-canonical residueD-4-Cl-Phe
- 3Parent 3 · analog 3Trp → D-3-Pal · Non-canonical residueD-3-Pal
- 4Parent 6 · analog 6Gly → D-Cit · Non-canonical residueD-Cit
- 5Parent 10 · analog 10Gly → D-Ala · D-amino acidD-Ala
Basis: The US label identifies cetrorelix as a native GnRH analog with substitutions at residues 1, 2, 3, 6, and 10. UniProt P01148 identifies human gonadorelin within its precursor. No parent span is asserted.
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
- Formula
- C70H92ClN17O14
- Molecular weight
- 1,431 g/mol
- Monoisotopic mass
- 1,429.6698 Da
- GSRS UNII OON1HFZ4BA(opens in a new tab)retrieved 2026-10-27
- PubChem CID 25074887(opens in a new tab)retrieved 2026-10-27
- Curated Cetrotide US label(opens in a new tab)retrieved 2026-10-27
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)
- 1,490 M⁻¹ cm⁻¹
- 5500 x Trp + 1490 x Tyr · Pace et al. 1995 (ExPASy ProtParam)
- No Trp: ExPASy reports more than 10 % error without Trp.
- Instability index
- Not calculated
- Aliphatic index
- Not calculated
- Boman index
- Not calculated
- Hydrophobic moment (μH)
- Not calculated
- 4 non-canonical residues (X) are not included in calculated values.
- D-amino acids have the same mass and charge as L forms. Hydrophobicity scales were measured on L forms.
- 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
- Hydrophobic20% (2)A L
- Aromatic10% (1)Y
- Positive10% (1)R
- Polar10% (1)S
- Special10% (1)P
- Non-canonical40% (4)X
10 residues. Each residue counts in one class; F and W count as aromatic.
A Ala1 · 10%
I Ile0 · 0%
L Leu1 · 10%
M Met0 · 0%
V Val0 · 0%
F Phe0 · 0%
W Trp0 · 0%
Y Tyr1 · 10%
H His0 · 0%
K Lys0 · 0%
R Arg1 · 10%
D Asp0 · 0%
E Glu0 · 0%
N Asn0 · 0%
Q Gln0 · 0%
S Ser1 · 10%
T Thr0 · 0%
C Cys0 · 0%
G Gly0 · 0%
P Pro1 · 10%
X Xaa4 · 40%
3D structure
PredictedAlphaFold DB · P01148
Loads the 3D viewer (3Dmol.js, about 150 KB) and the model file from AlphaFold DB (EMBL-EBI).
2D structure
Draws the structure in your browser with RDKit (about 2.3 MB, loaded once).
SMILES fromPubChem CID 25074887(opens in a new tab)
C[C@H](C(=O)N)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](CCCNC(=O)N)NC(=O)[C@H](CC2=CC=C(C=C2)O)NC(=O)[C@H](CO)NC(=O)[C@@H](CC3=CN=CC=C3)NC(=O)[C@@H](CC4=CC=C(C=C4)Cl)NC(=O)[C@@H](CC5=CC6=CC=CC=C6C=C5)NC(=O)CResults 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
Newer studies
PepBank reads each paper before it shows the results. This search looks in Europe PMC for newer papers that PepBank has not read yet.
Status and safety
Data