Cagrilintide 5mg

▎Cagrilintide Structure

▎Cagrilintide Research

Molecular Background

Cagrilintide is a synthetic, long-acting acylated amylin analogue composed of 37 amino acids with a C20 fatty diacid modification. It acts as a non-selective agonist at amylin receptors (AMY1R, AMY2R, and AMY3R) and the calcitonin receptor (CTR). PubChem lists Cagrilintide under CID 171397054, with the molecular formula C194H312N54O59S2 and a molecular weight of approximately 4409 g/mol.[7]

Research Progress

Using single-nucleus RNA sequencing (snRNA-seq), Ludwig et al. constructed a transcriptomic atlas comprising more than 530,000 cells from the caudal brainstem of rats, mice, and macaques and combined this with spatial transcriptomics. The investigators used cagrilintide exposure to examine neuronal populations in the dorsal vagal complex (DVC). They reported acute transcriptional responses in Calcr/Ramp3 neurons of the area postrema and, after longer exposure in rats, increased Prlh expression in NTS Calcr/Prlh neurons. Follow-up experiments supported a role for these neuronal populations in the long-term food-intake and body-weight responses observed in the rat model. The findings describe cross-species neural-circuit and transcriptomic responses under the experimental conditions used.[2]

Fig. 1: Cross-species single-nucleus transcriptomic atlas of the dorsal vagal complex in the cited study.[2]
The source figure summarizes the in vivo study design in diet-induced obese rats and mice, untreated macaques, UMAP-defined neuronal and glial populations, and the contribution of each population across species. Complete group definitions, cell numbers, and analytical methods are reported in the original publication.[2]

Carvas et al. investigated the contribution of amylin receptor subtypes to cagrilintide responses using male wild-type and RAMP1/3 knockout mice maintained on a high-fat diet. During the 3-week study, animals received vehicle, salmon calcitonin, or cagrilintide. The authors reported differences in body-weight and food-intake measurements between wild-type and RAMP1/3 knockout mice, together with changes in cFos signaling in the dorsal vagal complex and lateral parabrachial nucleus. Bulk RNA sequencing was also used to examine gene-expression patterns in selected brain regions. The results supported involvement of AMY1R and AMY3R in the responses to cagrilintide observed in this mouse model.[3]

Fig2. Food-intake and body-weight measurements used to select a cagrilintide dose in high-fat-diet-fed wild-type mice in the cited study.[3]
The source figure compares daily and weekly food intake, daily body weight, and cumulative body-weight change across vehicle and cagrilintide study groups. Group sizes, doses, statistical methods, and complete experimental procedures are reported in the original publication.[3]

Petersen et al. used a diet-induced obesity model in male rats to compare cagrilintide and GLP-3 alone and in combination, together with matched-dose comparator combinations containing semaglutide or GLP-2. The investigators measured body weight, food intake, adipose-tissue mass, circulating metabolic markers, plasma proteomics, and brain transcriptomic responses. They reported larger changes in body weight and food intake with the cagrilintide-GLP-3 combination than with the equimolar monotherapies under the study conditions, together with differences in cholesterol, triglycerides, insulin, plasma proteins, and central neuronal gene programs. Because this was a combination study, the reported findings should not be attributed to cagrilintide alone.[4]

Vera Wulfmeyer and colleagues used an ex vivo kidney-tubule model from 20 male Zucker Diabetic Fatty (ZDF) rats, including lean controls and obese diabetic animals, to explore renal signaling associated with cagrilintide. Cortical and medullary tubule fractions were exposed to vehicle, cagrilintide, or salmon calcitonin after phosphodiesterase inhibition, and intracellular cAMP was measured. The authors reported phosphorylation changes involving ion transporters such as NKCC2 and NCC in healthy rat tubules and a significant cAMP increase in cortical tubules from diabetic ZDF rats after cagrilintide exposure, while healthy rats did not show the same cAMP response. The publication is a conference abstract describing preliminary ex vivo findings, with phosphoproteomic analyses reported as ongoing at the time of publication.[5]

Cao et al. used cryo-electron microscopy and molecular-dynamics approaches to characterize cagrilintide bound to active AMY1R, AMY2R, AMY3R, and CTR complexes. The authors reported an amylin-like binding mode together with receptor-specific conformational dynamics across the calcitonin-family receptors.[6] Gu et al. independently determined cryo-EM structures of cagrilintide bound to AMY1R and CTR and described molecular contacts associated with non-selective Gs-coupled receptor activation. These structural studies define peptide-receptor interactions under experimental conditions and do not by themselves establish clinical efficacy or safety.[1]

Fig3. Amino-acid sequence alignment and cryo-EM structures of cagrilintide bound to amylin receptors and the calcitonin receptor in the cited structural study.[6]
The source figure shows the cagrilintide sequence and lipid modification together with active, Gs-coupled AMY1R, AMY2R, AMY3R, and CTR complexes. Structural alignment and receptor components are presented as reported by the study authors.[6]

Research Limitations

The studies summarized above use different preclinical and analytical systems, including rodent models, ex vivo kidney tubules, transcriptomic profiling, and purified receptor complexes. Results from these systems are not directly interchangeable. The cagrilintide-GLP-3 study evaluated a combination and therefore cannot determine the independent contribution of cagrilintide to every reported outcome.[4] The kidney study was published as a conference abstract with preliminary ex vivo findings and did not evaluate long-term renal accumulation, clinical safety, or human kidney outcomes.[5]

Cagrilintide is a modified amylin analogue, whereas native amylin is known for its propensity to aggregate under some biological conditions. Structural modification of cagrilintide was designed in part to reduce fibrillation, but the studies cited here do not establish the long-term safety, pharmacokinetics, or clinical performance of independently supplied research material. Interpretation should remain tied to the exact molecular form, experimental model, and study conditions reported in each publication.[1,5,6]

COCER Peptides presents Cagrilintide solely for laboratory research and analytical use. It is not intended for human or veterinary use. This COCER Peptides material is not an FDA-approved drug product. The research described above summarizes findings reported in third-party publications and is not a statement of clinical efficacy, safety, diagnosis, treatment, prevention, or an instruction for use.

▎Relevant Citations

References

[1] Gu Y, Yuan Q, Li X, et al. Structural and mechanistic insights into dual activation of cagrilintide in amylin and calcitonin receptors[J]. Acta Pharmacologica Sinica, 2026,47(1):162-172.

DOI:10.1038/s41401-025-01635-2.

[2] Ludwig M Q, Coester B, Gordian D, et al. A cross-species atlas of the dorsal vagal complex reveals neural mediators of the effects of cagrilintide on energy balance[J]. Nature Diabetes, 2026,8(6):1350-1367.

DOI:10.1038/s42255-026-01539-3.

[3] Carvas A O, Leuthardt A, Kulka P, et al. Cagrilintide lowers bodyweight through brain amylin receptors 1 and 3[J]. eBioMedicine, 2025,118:105836.

DOI:10.1016/j.ebiom.2025.105836.

[4] Petersen J, Merrild C, Holm S K, et al. Cagrilintide and GLP-3 combination therapy enhances weight loss and metabolic outcomes in obese male rats[J]. Nature Diabetes, 2026.

DOI:10.1038/s42255-026-01603-y.

[5] Wulfmeyer V, Billing A, Bhayana S, et al. #2426 Exploration of cagrilintide's mechanism of action in the kidney[J]. Nephrology Dialysis Transplantation, 2025,40(Supplement_3):gfaf116.1902.

DOI:10.1093/ndt/gfaf116.1902.

[6] Cao J, Belousoff M J, Johnson R M, et al. Structural and dynamic features of cagrilintide binding to calcitonin and amylin receptors[J]. Nature Communications, 2025,16:3388.

DOI:10.1038/s41467-025-58680-y.
[7] NCBI PubChem. Cagrilintide. PubChem CID 171397054.

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