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Nafarelin / Studies
Synthetic analog · 10 amino acids · 1,322.5 Da

Nafarelin studies and research data

PepBank has 87 nafarelin studies with results. 82 of them gave nafarelin, with 549 results, grouped by what the studies measured. In each group, results from studies in people come first. Data as of 2026-10-30.

Searches 549 results and 224 papers. Newer studies from Europe PMC

Results in people
448
82% of 549 results
Results in animals
91
17% of 549 results
Results in lab cells
10
2% of 549 results
From computer models
0
0% of 549 results
The molecule

Nafarelin identity

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

Nafarelin is a ten-residue GnRH agonist analog containing D-2-naphthylalanine at position 6. Its nasal product has indication-specific regimens.

Kind
Synthetic analog · 10 residues
Identifiers
PubChem CID25077405 (opens in a new tab)UNII1X0094V6JV (opens in a new tab)DrugBankDB00666 (opens in a new tab)CAS76932-56-4
Parent
Analog of GonadorelinNafarelin replaces glycine at position 6 of gonadorelin with D-2-naphthylalanine. Human UniProt P01148 contains gonadoliberin-1 at precursor residues 24-33. This is an analog relation, not an identical natural peptide.
Development
Approved in the US and EU (Synarel, 1990)An approved medicinal product exists. Availability and other indications can differ. Source (opens in a new tab)

Targets

Molecular targets with action and evidence source
TargetActionEvidence
Gonadotropin-releasing hormone receptorGNRHRP30968 (opens in a new tab)AgonistThe label identifies GnRH agonism. UniProt P30968 identifies the human GNRHR receptor.Source (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 · 2 modifications

Residues 1 to 10:
HWSYLRPG
  • HydrophobicA V I L M
  • AromaticF W Y
  • PositiveK R H
  • NegativeD E
  • PolarS T N Q
  • SpecialC G P
  • Non-canonicalX
  • Modified residue

Modifications

Residue 1
Other modification
Pyro-Glu
Residue 6
Non-canonical residue
D-2-Nal

Alignment to Gonadorelin

Calculated from the two sequences. Curated notes are shown as given.

8 of 10 aligned residues identical (80%) · 1 substitution · 1 non-canonical residue · Gonadorelin 1–10

  • Top row: Gonadorelin (parent)
  • Bottom row: Nafarelin
HWSYLRPG
  • Same as parent
  • Substituted
  • Non-canonical or D-form
  • Added
  • Gap
  • Modified side chain or end

Differences from the parent

  1. 1Parent 1 · analog 1Xaa → Glu · SubstitutionPyro-Glu
  2. 2Parent 6 · analog 6Gly → D-2-Nal · Non-canonical residueD-2-Nal

Basis: Nafarelin replaces glycine at position 6 of gonadorelin with D-2-naphthylalanine. Human UniProt P01148 contains gonadoliberin-1 at precursor residues 24-33. This is an analog relation, not an identical natural peptide.

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
C66H83N17O13
Molecular weight
1,322.5 g/mol
Monoisotopic mass
1,321.6356 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)
6,990 M⁻¹ cm⁻¹
5500 x Trp + 1490 x Tyr · Pace et al. 1995 (ExPASy ProtParam)
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.
  • Not included: other modification. Mass, charge and pI are not calculated; use the identity-source values.
  • The N-terminal group is not modeled.
  • 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

  • Hydrophobic10% (1)
  • Aromatic20% (2)
  • Positive20% (2)
  • Negative10% (1)
  • Polar10% (1)
  • Special20% (2)
  • Non-canonical10% (1)

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

A Ala0 · 0%
I Ile0 · 0%
L Leu1 · 10%
M Met0 · 0%
V Val0 · 0%
F Phe0 · 0%
W Trp1 · 10%
Y Tyr1 · 10%
H His1 · 10%
K Lys0 · 0%
R Arg1 · 10%
D Asp0 · 0%
E Glu1 · 10%
N Asn0 · 0%
Q Gln0 · 0%
S Ser1 · 10%
T Thr0 · 0%
C Cys0 · 0%
G Gly1 · 10%
P Pro1 · 10%
X Xaa1 · 10%

3D structure

PredictedAlphaFold DB · P01148

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 P01148, not an experimental structure of Nafarelin.

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

2D structure

Draws the structure in your browser with RDKit (about 2.3 MB, loaded once).

SMILES fromPubChem CID 25077405(opens in a new tab)

CC(C)C[C@@H](C(=O)N[C@@H](CCCN=C(N)N)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N)NC(=O)[C@@H](CC2=CC3=CC=CC=C3C=C2)NC(=O)[C@H](CC4=CC=C(C=C4)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC5=CNC6=CC=CC=C65)NC(=O)[C@H](CC7=CN=CN7)NC(=O)[C@@H]8CCC(=O)N8
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