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Molecular Weight
Purity
Storage
Appearance
Solubility
01
Cagrilintide is a long-acting synthetic analogue of human amylin, the 37-residue peptide hormone co-secreted with insulin. It keeps amylin’s length and its Cys2–Cys7 disulfide ring, carries six amino acid substitutions, and has a C20 fatty diacid attached to its N-terminus through a γ-glutamate spacer.
It acts as a non-selective agonist at the amylin receptors (AMY1, AMY2 and AMY3) and at the calcitonin receptor, a receptor family entirely different from the GIP, GLP-1 and glucagon receptors targeted by the other incretin peptides in this category. It is often studied alongside semaglutide, with which it has been investigated in combination. It is supplied as a lyophilized reference material for in vitro amylin-receptor pharmacology and analytical work on lipidated, disulfide-containing peptides.
02
Cagrilintide combines the amylin scaffold with stabilising substitutions and a lipid anchor.
Cys2–Cys7 disulfide
As in native amylin, the two cysteines form a disulfide that closes a small ring at the N-terminus. This ring is needed for receptor activation, so its integrity is a key quality attribute.
Six substitutions
Compared with human amylin, cagrilintide has Asn14→Glu, Val17→Arg, Ala25→Pro, Ser28→Pro, Ser29→Pro and Tyr37→Pro. The prolines in particular, as in pramlintide, reduce amylin’s strong tendency to form amyloid fibrils, and the other changes improve stability.
N-terminal lipid
Eicosanedioic acid (C20 diacid) is attached through γ-glutamic acid to the N-terminal amine of Lys1. This provides albumin binding, in the same way as the fatty diacids on semaglutide, tirzepatide and retatrutide, but at a different position.
Pro37-NH₂ C-terminus
The chain ends in an amidated proline, replacing the Tyr37-NH₂ of native amylin.
The sequence contains no methionine or tryptophan; its main chemical risks are disulfide reduction or scrambling, deamidation of its several asparagine and glutamine residues, and loss of the lipid.
03
In vitro, cagrilintide is characterised at the amylin and calcitonin receptors.
Amylin receptors
The amylin receptors AMY1, AMY2 and AMY3 are the calcitonin receptor paired with RAMP1, RAMP2 or RAMP3. cAMP assays in cells expressing each complex show that cagrilintide activates all three.
Calcitonin receptor
It also activates the calcitonin receptor on its own, without a RAMP partner, which is why it is described as a dual amylin/calcitonin receptor agonist.
Amyloid propensity
Thioflavin-T fluorescence assays have shown a much lower tendency to form fibrils than native human amylin, a key design goal of the substitutions.
Preclinical context
Published animal studies have examined its effects on food intake and on activation of brainstem regions, using receptor- and RAMP-knockout models to separate the contributions of individual receptors. These are cited as background only.
Characterisation of the reference material itself is limited to in vitro and analytical work.
04
Amylin-receptor panels
A reference agonist in binding and cAMP assays at AMY1, AMY2, AMY3 and the calcitonin receptor, compared with native amylin, pramlintide and salmon calcitonin.
Lipidated peptide HPLC
Its C20 diacid makes it a demanding test compound for reversed-phase methods for acylated peptides.
Disulfide integrity methods
Used to develop methods that compare reduced and non-reduced forms and to detect free thiol and scrambled species.
Multi-target metabolic panels
Provides the amylin-receptor reference alongside semaglutide, tirzepatide and retatrutide when comparing peptides across receptor families.
05
Storage
Store the lyophilized powder at −20 °C, sealed, desiccated and protected from light. Let the vial reach room temperature before opening.
Reconstitution
DMSO is commonly used for concentrated stocks. Aqueous solubility depends on pH and concentration, so check the certificate of analysis or test a small amount first. Avoid vigorous vortexing, which can promote aggregation.
Disulfide protection
Exclude reducing agents and thiols (DTT, TCEP, β-mercaptoethanol), and avoid basic pH above about 8, which promotes disulfide scrambling.
Aggregation
Although its substitutions greatly reduce fibril formation, amylin-derived peptides can still self-associate at high concentration. Thioflavin-T fluorescence or dynamic light scattering can be used to check concentrated solutions.
Labware
Use low-binding polypropylene tubes and tips, prepare dilutions just before use, and freeze single-use aliquots rather than storing dilute solutions.
06
Analysis must confirm the sequence, the disulfide and the N-terminal lipid.
HPLC
Wide-pore (300 Å) C4 or C8 columns at elevated temperature usually give the best peak shape and recovery for this lipidated peptide. Use formic acid rather than TFA when coupling to MS.
Mass spectrometry
ESI-MS shows multiply charged ions (around +4 to +7) that deconvolute to about 4409.0 Da. Because the N-terminal amine carries the lipid and the peptide is an amylin analogue, its mass and fragments are clearly different from the incretin peptides in this category.
Disulfide confirmation
The intact disulfide form is about 2 Da lighter than the reduced form. Reduction and alkylation with iodoacetamide (about +57 Da per cysteine), followed by digestion and LC-MS/MS, confirms the Cys2–Cys7 link.
Impurity profile
Typical checks include the des-lipid peptide, reduced and scrambled disulfide forms, asparagine/glutamine deamidation (+1 Da), truncated sequences and the free-acid C-terminus.
07
It acts on a different receptor family. Cagrilintide activates amylin receptors (the calcitonin receptor paired with RAMP1, 2 or 3) and the calcitonin receptor itself, whereas semaglutide acts only on the GLP-1 receptor.
The ring it forms is needed for receptor activation, so a reduced or mis-paired form is a significant impurity. Methods must distinguish the cyclic form from the reduced form (about 2 Da heavier) and from scrambled species.
Its C20 diacid is two carbons longer than semaglutide’s C18, and it sits at the N-terminus of a different peptide, so retention and peak shape differ. Like other lipidated peptides, it is best analysed on wide-pore C4 or C8 columns at elevated temperature.
Mainly the N-terminal C20 diacid, which binds serum albumin. The amino acid substitutions also improve stability and greatly reduce the amyloid-forming tendency of native amylin.
By its intact mass (about 4409.0 Da) and by MS/MS of digested fragments, which show the amylin-derived sequence, the lipid on the N-terminus and the Cys2–Cys7 disulfide. None of the incretin peptides in this category contain cysteine.
It has no methionine or tryptophan, so the usual oxidation sites are absent. Its main stability concerns are the disulfide, deamidation of asparagine and glutamine residues, and loss of the lipid.
No. It is supplied strictly as a reference compound for laboratory and analytical research and is not for human or animal use.
Cagrilintide Research Reference. (2026). Pure Peptides Labs Research Catalogue. Retrieved from https://purepeptideslabs.net/research-catalogue/metabolic-research-peptides/cagrilintide/
Materials listed on this platform are supported by independent testing and published documentation for laboratory research contexts.
