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Cagrilintide / Studies
Synthetic analog · 37 amino acids · 4,409.1 Da

Cagrilintide studies and research data

PepBank has 45 cagrilintide studies with results. 26 of them gave cagrilintide, with 130 results, grouped by what the studies measured. In each group, results from studies in people come first. Data as of 2026-10-30.

Searches 130 results and 128 papers. Newer studies from Europe PMC

Results in people
75
58% of 130 results
Results in animals
43
33% of 130 results
Results in lab cells
12
9% of 130 results
From computer models
0
0% of 130 results
The molecule

Cagrilintide identity

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

Cagrilintide is a 37-residue analogue of human amylin with six residue changes (N14E, V17R, A25P, S28P, S29P, Y37P), a Cys2-Cys7 disulfide, a C-terminal proline amide and a C20 fatty diacid attached to the N-terminal amine of Lys1 through L-gamma-Glu (GSRS). It was developed as a stable, lipidated, long-acting amylin analogue (Kruse et al. 2021) and is a non-selective agonist of amylin receptors and the calcitonin receptor (PMID 33727283; cryo-EM structures PMID 40204768). Novo Nordisk develops it alone and in the fixed-dose combination CagriSema with semaglutide; an NDA for CagriSema was submitted to FDA in December 2025. It is not approved in the US or EU.

Kind
Synthetic analog · 37 residues
Identifiers
ChEMBLCHEMBL4802169 (opens in a new tab)CHEMBL4860423 (opens in a new tab)PubChem CID164618153 (opens in a new tab)171397054 (opens in a new tab)UNIIAO43BIF1U8 (opens in a new tab)DrugBankDB18887 (opens in a new tab)CAS1415456-99-3PDB9BP3 (opens in a new tab)9BQ3 (opens in a new tab)9BTW (opens in a new tab)9BUB (opens in a new tab)+5IUPHAR13768 (opens in a new tab)
Parent
Analog of Amylin, human (islet amyloid polypeptide)GSRS classes cagrilintide as an amylin analog of human sequence origin and links it to amlintide (human amylin) as a mimetic; Kruse et al. 2021 (PMID 34288673) call it a long-acting amylin analogue. Substitutions are a direct alignment with human amylin (UniProt P10997, residues 34-70). The N-terminal acylation is not a substitution.
Development
Phase 3Novo NordiskPhase 3 trials test cagrilintide alone (for example NCT07220642, NCT07220759) and in CagriSema with semaglutide (for example REDEFINE 3, NCT05669755; NCT05567796; NCT05394519). ClinicalTrials.gov lists 54 studies (22 phase 3) for query.intr=cagrilintide OR NNC0174-0833 OR CagriSema. Novo Nordisk announced the CagriSema NDA submission to FDA on 2025-12-18. ChEMBL max_phase 3. Source (opens in a new tab)The note counts 54 studies from a registry search made when the note was written, with its own search terms. PepBank links 53 registered trials to Cagrilintide today, so the two numbers differ.

Targets

Molecular targets with action and evidence source
TargetActionEvidence
Calcitonin receptorCALCRP30988 (opens in a new tab)Agonistprimary literatureSource (opens in a new tab)
Amylin receptor 1 (CALCR + RAMP1)CALCR/RAMP1P30988 (opens in a new tab)Agonistprimary literatureSource (opens in a new tab)
Amylin receptor 2 (CALCR + RAMP2)CALCR/RAMP2P30988 (opens in a new tab)Agonistprimary literatureSource (opens in a new tab)
Amylin receptor 3 (CALCR + RAMP3)CALCR/RAMP3P30988 (opens in a new tab)Agonistprimary literatureSource (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

37 amino acids · 3 modifications · 1 disulfide bond

Residues 1 to 10:
CNTATCATQ
Residues 11 to 20:
RLAEFLRHSS
Residues 21 to 30:
NNFGPILPPT
Residues 31 to 37:
NVGSNTP
  • HydrophobicA V I L M
  • AromaticF W Y
  • PositiveK R H
  • NegativeD E
  • PolarS T N Q
  • SpecialC G P
  • Modified residue
  • Disulfide partner

Modifications

Lys1 N-alpha
Lipidation
The N-terminal alpha-amine of Lys1 is acylated by L-gamma-Glu, whose alpha-amine carries 19-carboxynonadecanoyl (C20 fatty diacid). GSRS fragment N-(19-carboxy-1-oxononadecyl)-L-gamma-glutamyl-L-lysine (UNII XKP2SC88E6). The Lys1 side-chain amine is free.
Pro37-NH2
C-terminal amide
C-terminal prolinamide (GSRS fragment UNII VD6PQK9DHG).
Cys2–Cys7
Disulfide bond
Intramolecular disulfide between Cys2 and Cys7 (GSRS). The GSRS name says 'cyclic (3->8)-disulfide' because it counts gamma-Glu as residue 1.

Alignment to Amylin, human (islet amyloid polypeptide)

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

31 of 37 aligned residues identical (84%) · 6 substitutions · 2 modified residues · Amylin, human (islet amyloid polypeptide) 1–37

  • Top row: Amylin, human (islet amyloid polypeptide) (parent)
  • Bottom row: Cagrilintide
NTATCATQ
RLAFLHSS
NNFGILT
NVGSNT
  • Same as parent
  • Substituted
  • Non-canonical or D-form
  • Added
  • Gap
  • Modified side chain or end

Differences from the parent

  1. 1Parent 1 · analog 1Lys, modified · LipidationThe N-terminal alpha-amine of Lys1 is acylated by L-gamma-Glu, whose alpha-amine carries 19-carboxynonadecanoyl (C20 fatty diacid). GSRS fragment N-(19-carboxy-1-oxononadecyl)-L-gamma-glutamyl-L-lysine (UNII XKP2SC88E6). The Lys1 side-chain amine is free.
  2. 2Parent 2 · analog 2Cys, modified · Disulfide bondIntramolecular disulfide between Cys2 and Cys7 (GSRS). The GSRS name says 'cyclic (3->8)-disulfide' because it counts gamma-Glu as residue 1.
  3. 3Parent 14 · analog 14Asn → Glu · Substitution
  4. 4Parent 17 · analog 17Val → Arg · Substitution
  5. 5Parent 25 · analog 25Ala → Pro · Substitution
  6. 6Parent 28 · analog 28Ser → Pro · Substitution
  7. 7Parent 29 · analog 29Ser → Pro · Substitution
  8. 8Parent 37 · analog 37Tyr → Pro · SubstitutionPro37 keeps the C-terminal amide. C-terminal prolinamide (GSRS fragment UNII VD6PQK9DHG).

Basis: GSRS classes cagrilintide as an amylin analog of human sequence origin and links it to amlintide (human amylin) as a mimetic; Kruse et al. 2021 (PMID 34288673) call it a long-acting amylin analogue. Substitutions are a direct alignment with human amylin (UniProt P10997, residues 34-70). The N-terminal acylation is not a substitution.

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
C194H312N54O59S2
Molecular weight
4,409.08 g/mol
Monoisotopic mass
4,406.2515 Da

Calculated from the sequence

Some values cannot be calculated. A modification changes this value and is not modeled here (for example a lipid, metal or linker).

Average mass
Not calculated
Monoisotopic mass
Not calculated
Isoelectric point (pI)
Not calculated
Net charge at pH 7.4
Not calculated
GRAVY (hydropathy)
−0.476
Mean Kyte-Doolittle hydropathy · Kyte and Doolittle 1982
Negative: hydrophilic on average.
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.
Extinction coefficient, 280 nm (all Cys as cystines)
125 M⁻¹ cm⁻¹
5500 x Trp + 1490 x Tyr + 125 x cystine · Pace et al. 1995 (ExPASy ProtParam)
Instability index
23.92
Dipeptide instability weights (DIWV) · Guruprasad et al. 1990
40 or below: classed as stable (ExPASy).
Aliphatic index
58.1
Mole % A + 2.9 V + 3.9 (I + L) · Ikai 1980
Boman index
1.87 kcal/mol
Mean solubility value (negated) · Boman 2003
2.48 or below: lower protein-binding potential (Boman).
Hydrophobic moment (μH)
0.632
Eisenberg scale, 100° per residue, best 11-residue window · Eisenberg et al. 1982, 1984
  • Not included: lipid chain. 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

A modification changes this value and is not modeled here (for example a lipid, metal or linker).

Composition

  • Hydrophobic22% (8)
  • Aromatic5% (2)
  • Positive11% (4)
  • Negative3% (1)
  • Polar38% (14)
  • Special22% (8)

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

A Ala3 · 8%
I Ile1 · 3%
L Leu3 · 8%
M Met0 · 0%
V Val1 · 3%
F Phe2 · 5%
W Trp0 · 0%
Y Tyr0 · 0%
H His1 · 3%
K Lys1 · 3%
R Arg2 · 5%
D Asp0 · 0%
E Glu1 · 3%
N Asn5 · 14%
Q Gln1 · 3%
S Ser3 · 8%
T Thr5 · 14%
C Cys2 · 5%
G Gly2 · 5%
P Pro4 · 11%

3D structure

ExperimentalPDB 9BP3

Loads the 3D viewer (3Dmol.js, about 150 KB) and the model file from RCSB PDB.

RCSB Protein Data Bank · CC0 1.0

2D structure

Cagrilintide has 37 residues. A full-atom drawing is hard to read at this size; the sequence view is the reference.

SMILES fromPubChem CID 164618153(opens in a new tab)

CC[C@H](C)[C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)N2CCC[C@H]2C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N3CCC[C@H]3C(=O)N)NC(=O)[C@@H]4CCCN4C(=O)CNC(=O)[C@H](CC5=CC=CC=C5)NC(=O)[C@H](CC(=O)N)NC(=O)[C@H](CC(=O)N)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H](CC6=CNC=N6)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC7=CC=CC=C7)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCC(=O)N)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](C)NC(=O)[C@@H]8CSSC[C@@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H](C(=O)N8)[C@@H](C)O)C)[C@@H](C)O)CC(=O)N)NC(=O)[C@H](CCCCN)NC(=O)CC[C@@H](C(=O)O)NC(=O)CCCCCCCCCCCCCCCCCCC(=O)O

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 Cagrilintide, 37 residues at 100 degrees per residue. Hydrophobic moment 0.25 pointing at 26 degrees.Lys 1, Eisenberg consensus (normalized) -1.50K+1Cys 2, Eisenberg consensus (normalized) 0.29C2Asn 3, Eisenberg consensus (normalized) -0.78N3Thr 4, Eisenberg consensus (normalized) -0.05T4Ala 5, Eisenberg consensus (normalized) 0.62A5Thr 6, Eisenberg consensus (normalized) -0.05T6Cys 7, Eisenberg consensus (normalized) 0.29C7Ala 8, Eisenberg consensus (normalized) 0.62A8Thr 9, Eisenberg consensus (normalized) -0.05T9Gln 10, Eisenberg consensus (normalized) -0.85Q10Arg 11, Eisenberg consensus (normalized) -2.53R+11Leu 12, Eisenberg consensus (normalized) 1.06L12Ala 13, Eisenberg consensus (normalized) 0.62A13Glu 14, Eisenberg consensus (normalized) -0.74E−14Phe 15, Eisenberg consensus (normalized) 1.19F15Leu 16, Eisenberg consensus (normalized) 1.06L16Arg 17, Eisenberg consensus (normalized) -2.53R+17His 18, Eisenberg consensus (normalized) -0.40H18Ser 19, Eisenberg consensus (normalized) -0.18S19Ser 20, Eisenberg consensus (normalized) -0.18S20Asn 21, Eisenberg consensus (normalized) -0.78N21Asn 22, Eisenberg consensus (normalized) -0.78N22Phe 23, Eisenberg consensus (normalized) 1.19F23Gly 24, Eisenberg consensus (normalized) 0.48G24Pro 25, Eisenberg consensus (normalized) 0.12P25Ile 26, Eisenberg consensus (normalized) 1.38I26Leu 27, Eisenberg consensus (normalized) 1.06L27Pro 28, Eisenberg consensus (normalized) 0.12P28Pro 29, Eisenberg consensus (normalized) 0.12P29Thr 30, Eisenberg consensus (normalized) -0.05T30Asn 31, Eisenberg consensus (normalized) -0.78N31Val 32, Eisenberg consensus (normalized) 1.08V32Gly 33, Eisenberg consensus (normalized) 0.48G33Ser 34, Eisenberg consensus (normalized) -0.18S34Asn 35, Eisenberg consensus (normalized) -0.78N35Thr 36, Eisenberg consensus (normalized) -0.05T36Pro 37, Eisenberg consensus (normalized) 0.12P37
μH, residues shown
0.252
μH, best 11-residue window
0.632
Arrow direction
26°
Residues
37 · 3 rings of 18
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)
1K0°-1.50
2C100°0.29
3N200°-0.78
4T300°-0.05
5A40°0.62
6T140°-0.05
7C240°0.29
8A340°0.62
9T80°-0.05
10Q180°-0.85
11R280°-2.53
12L20°1.06
13A120°0.62
14E220°-0.74
15F320°1.19
16L60°1.06
17R160°-2.53
18H260°-0.40
19S0°-0.18
20S100°-0.18
21N200°-0.78
22N300°-0.78
23F40°1.19
24G140°0.48
25P240°0.12
26I340°1.38
27L80°1.06
28P180°0.12
29P280°0.12
30T20°-0.05
31N120°-0.78
32V220°1.08
33G320°0.48
34S60°-0.18
35N160°-0.78
36T260°-0.05
37P0°0.12
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