Lot certificates published
Plain, secure packaging
Purely Peptides
Research Catalog

Compound monograph

Cagrilintide

Cagrilintide is a long-acting synthetic amylin analog, lipidated and disulfide-cyclized, characterised at the calcitonin receptor and at amylin receptor complexes.

Published: 2026-09-13Last updated: 2026-10-12Literature/identifier verification: 2026-09-13
Also known asAM833AM-833NNC0174-0833
Amylin and calcitonin receptor agonists

01

Identity & nomenclature

Cagrilintide is a long-acting synthetic amylin analog, lipidated and disulfide-cyclized, characterised at the calcitonin receptor and at amylin receptor complexes.

An FDA substance record displays C194H312N54O58S2 against an approximately 4409 Da mass. That oxygen count is inconsistent with both the stated mass and the covalent structure; reconstruction gives O59, matching PubChem. The O58 value is 15.9949 Da lighter and is not a salt or protonation difference. This library records O59 and notes the disagreement rather than silently choosing.

Declared aliases and development codes: AM833, AM-833, NNC0174-0833.

02

Molecular properties

Molecular formulaC194H312N54O59S2
Molecular mass4409.01 Da
CAS Registry Number1415456-99-3
PubChem CID171397054
UNIIAO43BIF1U8
One-letter sequenceKCNTATCATQRLAEFLRHSSNNFGPILPPTNVGSNTP
Terminal groupsC-terminal amide; N-terminal acylation via gamma-glutamyl linker

Thirty-seven residues with a Cys2–Cys7 disulfide and a C-terminal amide. The backbone string alone is an incomplete description: the N-terminal lysine carries a gamma-glutamyl linker acylated with a C20 dicarboxylic fatty acid, attached at the alpha-amino group rather than the lysine side chain. A 2026 review by Bousch et al. (PMID 41898461) instead describes the N-terminal lysine as lipidated on its side chain; this record keeps the alpha-amino attachment stated above.

03

Structural characteristics

A human amylin analog. Relative to native human amylin it carries glutamate at 14, arginine at 17, prolines at 25, 28 and 29, and proline in place of the C-terminal tyrosine, together with N-terminal lipidation through a gamma-glutamyl spacer to a C20 fatty diacid. The three prolines at 25, 28 and 29 are shared with pramlintide, so cagrilintide is also a lipidated, further-substituted relative of that engineered analog. The existing amylin and pramlintide links describe these structural relationships. The Glu14–Arg17 interaction reported for this peptide is a noncovalent ionic contact, not a lactam bridge. Descriptions that render it as an additional covalent ring describe a different molecule. The only covalent ring is the Cys2–Cys7 disulfide.

  • Cys2–Cys7 disulfide
  • C20 dicarboxylic fatty-acid acylation

Ring closures: covalent bonds between residues, by position counted from the first residue of the chain.

  • Disulfide Cys2–Cys7: thiol sulfur (Sγ) to thiol sulfur (Sγ). Registry source: FDA GSRS UNII AO43BIF1U8; PubChem CID 171397054.

Terminal features: C-terminal amide, N-terminal acylation via gamma-glutamyl linker.

04

Molecular targets & mechanisms

Amylin and calcitonin receptors

CALCR · CTR · AMY1 · AMY2 · AMY3 · RAMP1 · RAMP2 · RAMP3

The calcitonin receptor, and the amylin receptor complexes it forms when associated with receptor activity-modifying proteins RAMP1, RAMP2 or RAMP3. Because the amylin receptors are heteromers rather than distinct gene products, receptor construct and accessory-protein expression must accompany any selectivity claim; a potency ranking is not transferable between assay systems.

05

Analytical considerations

Intact mass cannot distinguish conjugation-site isomers: whether the C20 diacid and gamma-glutamyl linker sit on the N-terminal alpha-amino group or on the Lys1 side chain gives the same formula. Establishing the position requires sequence-resolved tandem MS with coverage across the conjugation site. Disulfide reduction gives a calculated +2.0157 Da change before alkylation, which supports disulfide accounting but does not map connectivity. A matching chromatographic peak or a cAMP response is not identity evidence — related amylin and calcitonin agonists share both.

Disagreements and mix-ups

Points where sources disagree about this compound's identity, or where a name or form is easily confused with another, as noted in this record. The discrepancy register quotes the passage for each one.

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

  • Human AMY1R, AMY2R, AMY3R and CTR complexes

    Cao et al. reported structures of cagrilintide bound to active human CTR, AMY1R, AMY2R and AMY3R complexes with Gs, with consensus-map resolutions of 2.2, 2.2, 2.7 and 3.0 angstroms, respectively, in vitro.

    Reference [2]

Animal studies

  • Chow-fed 129S2/SvEv-background wild-type and RAMP1/3 knockout male mice

    Carvas et al. observed significantly higher cFos signals in the area postrema, nucleus of the solitary tract and lateral parabrachial nucleus of chow-fed 129S2/SvEv-background wild-type male mice exposed to cagrilintide than in vehicle controls, while cagrilintide did not significantly activate these regions in RAMP1/3 knockout mice.

    Reference [3]

  • High-fat-diet 129S2/SvEv-background male mouse metabolic model

    Carvas et al. observed reduced body weight in 129S2/SvEv-background wild-type male mice exposed to cagrilintide in a prolonged high-fat-diet metabolic model, while RAMP1/3 knockout littermates had no body-weight response.

    Reference [3]

  • High-fat-diet 129S2/SvEv-background male mouse metabolic model

    Carvas et al. reported that cagrilintide did not significantly alter gene expression in the dorsal vagal complex or lateral parabrachial nucleus of 129S2/SvEv-background wild-type male mice in the high-fat-diet metabolic model.

    Reference [3]

  • High-fat-diet 129S2/SvEv-background male mouse metabolic model

    Carvas et al. reported that changes in body composition in 129S2/SvEv-background wild-type male mice exposed to cagrilintide did not reach statistical significance relative to vehicle controls in the high-fat-diet metabolic model; fat mass decreased by 7% (P = 0.2) and lean mass increased by 5% (P = 0.14).

    Reference [3]

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

    Development of Cagrilintide, a Long-Acting Amylin Analogue.

    Kruse T, Hansen JL, Dahl K, Schäffer L, Sensfuss U, Poulsen C, Schlein M, Hansen AMK, Jeppesen CB, Dornonville de la Cour C, Clausen TR, Johansson E, Fulle S, Skyggebjerg RB, Raun K

    Journal of medicinal chemistry · 2021-07-21 · Journal Article

    current
    PMID 34288673DOI 10.1021/acs.jmedchem.1c00565CagrilintideAmylin (human IAPP)PramlintideCALCR

  2. Reference 2

    Structural and dynamic features of cagrilintide binding to calcitonin and amylin receptors.

    Cao J, Belousoff MJ, Johnson RM, Keov P, Mariam Z, Deganutti G, Christopoulos G, Hick CA, Reedtz-Runge S, Glendorf T, Ballarín-González B, Raun K, Bayly-Jones C, Wootten D, Sexton PM

    Nature communications · 2025-04-10 · Journal Article

    current
    PMID 40204768PMC11982234DOI 10.1038/s41467-025-58680-yCagrilintideAmylin (human IAPP)PramlintideCALCR

  3. Reference 3

    Cagrilintide lowers bodyweight through brain amylin receptors 1 and 3.

    Carvas AO, Leuthardt A, Kulka P, Lommi G, Hassan S, Coester B, Lundh S, Pers T, Secher A, Raun K, Lutz TA, Le Foll C

    EBioMedicine · 2025-07-03 · Journal Article

    current
    PMID 40609154PMC12270663DOI 10.1016/j.ebiom.2025.105836CagrilintideCALCR

  4. Reference 4

    Molecular Mechanisms of Islet Amyloid Polypeptide Aggregation: Towards Chemical Strategies to Prevent Amyloid Formation and to Design Non-Aggregating Peptide Therapeutics.

    Bousch C, Bérubé F, Babych M, Ongeri S, Bourgault S

    International journal of molecular sciences · 2026-03-12 · Review

    current
    PMID 41898461PMC13026743DOI 10.3390/ijms27062598Cagrilintide

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
Kruse T et al. 2021Study models reported: in vitro; animal (rat) · from the full text
Cao J et al. 2025Study models reported: in vitro · from the abstract
Carvas AO et al. 2025Study models reported: animal (mouse) · from the abstract
Bousch C et al. 2026Review article

Compare

Record history

Published 2026-09-13.

  • : Sequence and structure, References
  • : Sequence and structure

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. Cagrilintide. Published 2026-09-13; updated 2026-10-12. https://purelypeptides.org/research/compounds/cagrilintide/

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 →