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.
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 formula | C194H312N54O59S2 |
|---|---|
| Molecular mass | 4409.01 Da |
| CAS Registry Number | 1415456-99-3 |
| PubChem CID | 171397054 |
| UNII | AO43BIF1U8 |
| One-letter sequence | KCNTATCATQRLAEFLRHSSNNFGPILPPTNVGSNTP |
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.
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
Terminal features: C-terminal amide, N-terminal acylation via gamma-glutamyl linker.
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Molecular targets & mechanisms
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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.
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Verified bibliography
- Development of Cagrilintide, a Long-Acting Amylin Analogue.current
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
- Structural and dynamic features of cagrilintide binding to calcitonin and amylin receptors.current
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
- Cagrilintide lowers bodyweight through brain amylin receptors 1 and 3.current
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
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Methodology & citation verification
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