Cagrilintide is a synthetic long-acting analogue of human amylin, engineered for stability and used as a reference agonist at the amylin receptors AMY1R, AMY2R and AMY3R and at the calcitonin receptor. It combines sequence substitutions drawn from both human and salmon calcitonin with a fatty diacid side chain, and it is used in receptor pharmacology and second messenger work in vitro. NuVion supplies Cagrilintide as a laboratory chemical for in vitro research use only.
Key facts
| Type | Synthetic acylated amylin analogue |
| Amino acid count | 32 |
| Parent peptide | Human amylin (IAPP) |
| Modification | C20 fatty diacid side chain via a linker |
| Structural feature | N-terminal disulfide loop, amidated C-terminus |
| Receptors | AMY1R, AMY2R, AMY3R and the calcitonin receptor |
| Molecular weight | Approximately 3.8 kDa |
| Supplied form | Lyophilised powder in a sealed vial |
Cagrilintide
$149 AUD
View productResearch use only. Not for human or veterinary use.
Structure and chemistry
Human amylin, also called islet amyloid polypeptide, is a 37-residue peptide co-secreted with insulin from pancreatic beta cells. It carries a disulfide bridge between cysteines 2 and 7 that closes a small N-terminal loop, and an amidated C-terminus. Both features are required for receptor activity. The native human sequence has a well-known liability: a segment in the middle of the chain drives self-association into amyloid fibrils, which makes the unmodified human peptide difficult to handle and unstable in solution.
Cagrilintide addresses that liability by substitution. Residues in the aggregation-prone region are replaced with those found in salmon calcitonin and in the non-aggregating rodent amylin sequence, giving a peptide that stays monomeric in solution far longer than human amylin. The N-terminal disulfide loop and the C-terminal amide are retained, since receptor activation depends on them. A C20 fatty diacid is attached through a hydrophilic linker to a lysine side chain, which promotes reversible association with serum albumin and extends the circulating half-life. Acylation of this kind is the same design approach used across several long-acting peptide analogues.
The acyl chain shapes handling. It gives the peptide surfactant-like character, so solutions foam readily and the peptide accumulates at air-liquid interfaces, and it also promotes association with albumin in serum-containing medium, which reduces the free concentration available to the receptor. Both effects need accounting for when setting up a concentration-response experiment. Purity is determined by RP-HPLC, where the acylated peptide retains strongly, and identity by mass spectrometry, with the disulfide bond confirmed by comparing reduced and non-reduced samples.
Mechanism of action
The amylin receptors are not separate gene products. Each is a complex formed when the calcitonin receptor associates with one of the receptor activity-modifying proteins: RAMP1 gives AMY1R, RAMP2 gives AMY2R and RAMP3 gives AMY3R. The RAMP changes the ligand binding pocket of the calcitonin receptor so that amylin is preferred over calcitonin, which means expressing the calcitonin receptor alone produces a different pharmacology from co-expressing it with a RAMP. Any cell-based assay with this compound therefore has to define which RAMP is present, and that requirement is the main methodological point in amylin receptor work.
Cagrilintide binds these complexes and couples principally to Gs, raising cyclic AMP and activating protein kinase A. It is described as a non-selective agonist across the amylin receptor subtypes with retained activity at the calcitonin receptor itself, which distinguishes it from more subtype-selective analogues. Readouts in cell systems are cyclic AMP accumulation by HTRF or reporter, competition binding against radiolabelled or fluorescent amylin, and beta-arrestin recruitment and internalisation by BRET or imaging. Because the compound is long-acting by design, kinetic experiments comparing association and dissociation rates against native amylin are a common use, and thioflavin T fluorescence assays are used to compare its aggregation behaviour with that of the unmodified human sequence.
Research applications
- Cyclic AMP accumulation assays in cells co-expressing the calcitonin receptor with a defined RAMP, as a reference amylin receptor agonist.
- Competition binding at AMY1R, AMY2R, AMY3R and the calcitonin receptor to determine affinity and subtype selectivity for analogues under test.
- RAMP dependence experiments comparing calcitonin receptor alone against each receptor complex under matched conditions.
- Beta-arrestin recruitment and receptor internalisation assays by BRET or high content imaging.
- Aggregation and fibrillation assays by thioflavin T fluorescence, comparing the analogue with native human amylin.
- Albumin binding and free fraction measurement by equilibrium dialysis or ultrafiltration, to relate nominal and free concentration in serum-containing medium.
Cagrilintide sits in NuVion’s Metabolism category alongside the other compounds used in metabolic receptor research.
Handling in the laboratory
Cagrilintide is supplied lyophilised and is reconstituted with bacteriostatic water added slowly down the side of the vial, then swirled gently until dissolved. It is never shaken or vortexed hard, because the fatty acyl chain makes the peptide surface-active and foaming drives both loss and aggregation. The reconstitution calculator converts vial content and diluent volume into a stock concentration. Dissolution is slower than for an unmodified peptide of the same length, so the vial is left to stand undisturbed if material remains undissolved.
Unopened vials are kept sealed, dry and refrigerated as stated on the product documentation. Reconstituted solution is refrigerated and used within the period given there, or aliquoted into single-use volumes and frozen. In serum-containing medium the acyl chain binds albumin, so the free concentration at the receptor is lower than the nominal figure; where absolute potency matters, free fraction is measured or a defined albumin concentration is used so that results are comparable between experiments.
Testing and supply from NuVion
NuVion’s Cagrilintide is manufactured at a GMP-audited facility and independently tested by Janoshik Analytical, with purity determined by RP-HPLC and identity confirmed by mass spectrometry. The Certificate of Analysis for a tested batch is published on the product page and in the COA library. The peptide is supplied lyophilised in sealed vials and dispatched from within Australia.
Related compounds
Other compounds used in metabolic receptor pharmacology include Tirzepatide, a dual GIP and GLP-1 receptor agonist, and Retatrutide, a multi-receptor agonist across GLP-1, GIP and glucagon receptors.
Frequently asked questions
What is Cagrilintide used for in research?
It is used as a reference agonist at the amylin receptor complexes and the calcitonin receptor in cyclic AMP accumulation and competition binding assays, in RAMP dependence experiments, in arrestin recruitment work, and in aggregation studies comparing it with native human amylin.
Why does the RAMP matter in amylin receptor assays?
The amylin receptors are complexes of the calcitonin receptor with a receptor activity-modifying protein. RAMP1, RAMP2 and RAMP3 each reshape the binding pocket differently, so the calcitonin receptor expressed alone gives different pharmacology from the same receptor co-expressed with a RAMP. Defining which RAMP is present is essential to interpreting a result.
Is Cagrilintide a therapeutic good in Australia?
No. NuVion’s Cagrilintide is a laboratory chemical for in vitro research. It is not included in the Australian Register of Therapeutic Goods, has not been assessed by the Therapeutic Goods Administration, and is not for human or veterinary use.
How should Cagrilintide be stored?
Lyophilised vials are kept sealed, dry and refrigerated per the product documentation. Reconstituted solution is refrigerated and used within the stated period, or aliquoted into single-use volumes and frozen. Solutions are swirled and never shaken, since the acyl chain makes the peptide surface-active.
Research use only. This product is a laboratory chemical supplied for in vitro research. It is not included in the Australian Register of Therapeutic Goods and has not been assessed by the Therapeutic Goods Administration for quality, safety or efficacy. It is not for human or veterinary use, and nothing on this page is a representation about therapeutic use.
