Cagrilintide — wholesale 10-vial kits

Research context

Native amylin is a 37-residue peptide that is co-secreted with insulin, but it aggregates readily and lasts only minutes in circulation. Cagrilintide was engineered to fix both problems: amino-acid substitutions reduce its tendency to form fibrils, and a fatty-diacid lipidation at the N-terminus promotes albumin binding and a long half-life in experimental systems.

Origin and molecular design. Cagrilintide, development code AM833 (also NNC0174-0833), was developed at Novo Nordisk, and the structure–activity work behind it was published in the Journal of Medicinal Chemistry in 2021 (Kruse et al.), which frames amylin's high propensity to form amyloid fibrils as the central design problem. Relative to human amylin, the 37-residue sequence registered in FDA GSRS keeps the Cys2–Cys7 disulfide and the C-terminal amide, carries the three proline substitutions used in pramlintide (positions 25, 28 and 29), and adds Glu14, Arg17 and Pro37. The N-terminal lysine is acylated with a C20 fatty diacid through a γ-glutamic acid linker. Cryo-EM structures of cagrilintide bound to the amylin-1 receptor–Gs and calcitonin receptor–Gs complexes identify an E14–R17 intramolecular salt bridge that stabilizes the helix, Phe23 anchoring the peptide at the transmembrane bundle, and Pro37 contacting the receptor extracellular domain (Gu et al., Acta Pharmacologica Sinica, 2026).

Pharmacologically, cagrilintide acts at amylin receptors (the calcitonin receptor paired with receptor activity-modifying proteins, RAMPs) and at the calcitonin receptor itself, a dual amylin and calcitonin receptor agonist (DACRA) profile. One study profiled AM833 across 25 endpoints of receptor binding, activation and regulation against pramlintide (amylin-receptor selective), salmon calcitonin (non-selective), human calcitonin and rat amylin, and reported a profile distinct from every comparator (Fletcher et al., J Pharmacol Exp Ther, 2021). That makes it a tool compound for studying RAMP-dependent receptor pharmacology, amylin-pathway signaling in the hindbrain, and how amylin agonism combines with GLP-1 receptor agonism. It is frequently studied alongside semaglutide; the combination is known as CagriSema.

U.S. regulatory status: cagrilintide is investigational and is not approved by the FDA or any other regulator. Its standalone late-stage evidence is a single Phase 2 study published in the Lancet in 2021, and most of its late-stage development is as the amylin component of CagriSema in Novo Nordisk's Phase 3 REDEFINE program; REDEFINE 1 was published in the New England Journal of Medicine in 2025. The material sold by WholesalePeptide.us is a research reference compound supplied only for in-vitro, analytical and preclinical laboratory research.

Amylin analogs are among the harder peptides to handle in the lab because of their tendency to self-associate. Researchers comparing cagrilintide with native amylin or pramlintide typically check solution behavior by dynamic light scattering or thioflavin-T assays before running receptor work, and confirm the acylated mass by LC-MS on arrival. The material we supply is lyophilized, and each lot carries a COA reporting the measured mass, the full RP-HPLC trace and net peptide content.

Research areas

• Amylin and calcitonin receptor pharmacology
• RAMP-dependent receptor signaling
• Amylin / GLP-1 co-agonist studies
• Cryo-EM structures of amylin and calcitonin receptor complexes
• Peptide fibrillation and aggregation resistance
• LC-MS characterization of acylated peptides

U.S. regulatory status of the compound (as an active ingredient): Investigational peptide, not approved by the FDA or any regulator. The material sold here is a research reference chemical, not a drug product.

Handling and storage

• Store lyophilized vials at −20 °C, sealed, protected from light and moisture.
• Let the vial reach room temperature before opening to limit condensation on the powder.
• Amylin analogs can aggregate in solution; prepare working solutions fresh and avoid vigorous agitation.
• Aliquot reconstituted material and freeze once; avoid repeated freeze–thaw.