Cagrilintide

Research Background

Cagrilintide (CAS 2171674-71-6) is a long-acting amylin analog peptide supplied strictly as a reference material for in-vitro and preclinical laboratory research. Structurally it is a 32-residue peptide built on the amylin (islet amyloid polypeptide) scaffold, carrying a fatty-diacid lipidation motif that, in published pharmacokinetic literature, was engineered with the aim of extending the molecule's circulating half-life relative to native amylin in laboratory model systems. Its molecular formula is C194H312N54O59S2, corresponding to an average molecular weight of approximately 4409 g/mol, and it contains an intramolecular disulfide bridge reflected in the two sulfur atoms of the formula. This compound is intended solely for research use and is not a drug, food, or dietary product, and is not for human or veterinary use.

In the peer-reviewed literature, amylin and its synthetic analogs are studied as agonists at amylin and calcitonin receptor complexes. Cagrilintide specifically has been characterized in receptor-pharmacology and metabolic-signaling investigations as a tool for probing amylin-receptor engagement, and it has appeared in preclinical studies exploring combined preparations with incretin-class peptides. Research on this class remains preliminary and ongoing; the material described here is characterized only for laboratory experimentation, and nothing on this page describes or implies human or veterinary outcomes. This content is educational and is not medical advice.

What Has Been Studied

Published preclinical and in-vitro work involving cagrilintide and related amylin analogs has centered on documented laboratory endpoints rather than clinical outcomes. Reported research directions include:

• Receptor-binding and functional-agonism assays at amylin (AMY1-3) and calcitonin receptor complexes in transfected cell systems.
• In-vitro signal-transduction readouts such as cyclic-AMP accumulation used to profile potency and selectivity of the lipidated analog.
• Structure-activity and lipidation studies comparing acylated amylin analogs with native peptide to characterize protein-binding and stability behavior.
• Combination-preparation research pairing amylin analogs with incretin-class peptides in preclinical models to study additive receptor signaling.
• Analytical stability and aggregation studies relevant to handling a cysteine-containing, lipidated peptide in solution.

Analytical Characterization

Each research lot is specified at a purity of not less than 98 percent. Identity and purity are confirmed using orthogonal analytical methods before release, with a Certificate of Analysis (COA) available for the corresponding lot.

• HPLC (reversed-phase): area-percent purity determination confirming the >=98% specification and resolving process-related and deletion-sequence impurities.
• Mass spectrometry (ESI-MS): identity confirmation against the expected average mass near 4409 Da for the C194H312N54O59S2 composition.
• Peptide content / net-peptide assay and residual-solvent or water-content checks where applicable to a lyophilized peptide.
• Appearance and reconstitution notes documented per lot to support reproducible in-vitro handling.

Because cagrilintide is a lipidated, disulfide-containing peptide, laboratory handling follows standard practices for sensitive research peptides: work in a clean environment, minimize freeze-thaw cycles of reconstituted stock, and reference the lot-specific COA for the assayed purity and mass values used to plan in-vitro experiments. This guidance covers laboratory handling only and does not imply any in-vivo use.