Page data last changed: . Chemistry registry snapshot: . Registry refreshes and identity assessments are separate from scientific content review.
The hormone that inspired pramlintide — and a landmark model of peptide amyloid aggregation.
Also known as: IAPP · islet amyloid polypeptide
Part of the Metabolic & GLP-1 peptides cluster
Overview
Amylin, or islet amyloid polypeptide (IAPP), is a 37-residue peptide hormone co-secreted with insulin from pancreatic beta cells. It is studied both as a metabolic signal and as a model of peptide aggregation, since human amylin forms the amyloid deposits characteristic of pancreatic islets in type 2 diabetes.
Source & context
Biological / chemical source: Pancreatic beta cells (co-stored with insulin)
Primary research or clinical context: Endogenous hormone; basis for engineered analogs studied in metabolism research
Structure and modifications
Amylin carries a disulfide bridge between its two N-terminal cysteines and an amidated C-terminus, both important for receptor activity. It signals through calcitonin-receptor complexes paired with RAMP accessory proteins — an example of how a single peptide's biology depends on its receptor partners.
Aggregation biology
Human amylin is amyloidogenic: it readily forms fibrils, and these deposits are a hallmark of islet pathology. This aggregation problem is precisely why the drug analog pramlintide was engineered with proline substitutions. Amylin is therefore a recurring reference point in both metabolic and protein-misfolding research.
Sequence
One-letter sequence commonly cited for Amylin (educational; isoforms and modifications may differ):
KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY
Residues plotted ~100° apart around an α-helix — clustering of one color reveals an amphipathic face.
Structure & chemistry
Molecular identity & reference confidence
Source-supported reference
Reference values are taken from the cited molecular record or curated profile. A database match is not independent laboratory verification; modifications, counter-ions, and formulations can change the measured mass.
- Molecular form
- Amylin (source record; form not independently established)
- Species
- Not established by this molecular identity audit
- Termini (N / C)
- Not specified / Not specified
Average reference mass
Reference policy updated: 2026-10-05
- IUPHAR/BPS source snapshot · 2026-10-01
- PubChem molecular record · 2026-10-01
- Molecular formula
- C165H261N51O55S2
- Average reference mass
- ≈ 3,903.3
- PubChem CID: 16132430
- IUPHAR ligand: 688
- CAS RN: 124447-81-0
- UNII: U3U3114NE1
Chemistry values: PubChem, IUPHAR/BPS Guide to Pharmacology · fetched 2026-10-01.
Clinical development snapshot
ClinicalTrials.gov lists 109 registered studies with “Amylin” as an intervention (snapshot 2026-10-01). A registry footprint is not evidence of efficacy or approval.
| NCT | Title | Phase | Status | Updated |
|---|---|---|---|---|
| NCT07846033 | A Phase 1 Study of VK3019 in Overweight and Obese Adults Without Comorbidities | Phase 1 | recruiting | 2026-09-29 |
| NCT07392190 | A Study of Eloralintide (LY3841136) in Participants With Persistent Obesity Who Are Treated With a Weekly Incr | Phase 3 | recruiting | 2026-09-22 |
| NCT07832032 | Biological Profiles of Neuropeptides, Neurotrophins and miRNA in Migraine | — | not yet recruiting | 2026-09-21 |
| NCT07815678 | First-in-human Study of the Safety, Tolerability, Pharmacokinetics, and Food Effect of ACCG-2671 | Phase 2 | recruiting | 2026-09-14 |
| NCT07575932 | A Study of PF-08653945 and PF-08653944 in Adults With Overweight or Obesity | Phase 2 | active not recruiting | 2026-09-14 |
| NCT07010432 | The Role of the Amylin Analogue Cagrilintide in Bone Metabolism | Phase 1 | recruiting | 2026-09-10 |
Amylin — reconstitution calculator
Enter how much peptide is in the vial and how much diluent (e.g. bacteriostatic water) is added. The tool returns the resulting solution concentration — and, for any amount you type, the volume it corresponds to. This is educational arithmetic, not a dosing recommendation.
Reference form: Amylin (source record; form not independently established)Average reference mass: 3,903.3 Da
Enter an amount to see the volume it corresponds to.
Educational concentration mathematics only. This tool does not recommend a dose, amount, or protocol, and nothing here is medical advice. Many peptides are not authorized by Health Canada for human use — see our reconstitution and bacteriostatic-water guides for context.
Change log
Dated observations from the data pipeline (registry flags, trial footprints, identifiers) and editorial reviews of this profile.
- Trials3 registered studies added on ClinicalTrials.gov (now 109).
FAQ about Amylin
What is Amylin?+
Amylin, or islet amyloid polypeptide (IAPP), is a 37-residue peptide hormone co-secreted with insulin from pancreatic beta cells. It is studied both as a metabolic signal and as a model of peptide aggregation, since human amylin forms the amyloid deposits characteristic of pancreatic islets in type 2 diabetes.
What Canadian product status is recorded for Amylin?+
Canadian product status for Amylin has not been verified in this profile. No verified record here does not mean no authorization exists. Status depends on the product, formulation and use; consult Health Canada's product records.
What is the typical length of Amylin?+
Amylin is commonly described as approximately 37 amino acids (Hormone).
Related peptides
References & further reading
- 1.Hay (2017). Amylin. Headache
- 2.Secher et al. (2026). The story of amylin: from physiology to therapy. Nat Metab
- 3.Boccia et al. (2020). Amylin brain circuitry. Peptides
- 4.Castillo et al. (1995). Amylin/islet amyloid polypeptide: biochemistry, physiology, patho-physiology. Diabete Metab
- 5.Bahramikia et al. (2013). Inhibition of human islet amyloid polypeptide or amylin aggregation by two manganese-salen derivatives. Eur J Pharmacol
- 6.Lutz (2022). Creating the amylin story. Appetite
- 7.Höppener et al. (1993). Chronic overproduction of islet amyloid polypeptide/amylin in transgenic mice: lysosomal localization of human islet amyloid polypeptide and lack of marked hyperglycaemia or hyperinsulinaemia. Diabetologia
- 8.Smith et al. (2000). Islet amyloid polypeptide (amylin) modulates chylomicron metabolism in rats. Clin Exp Pharmacol Physiol
- 9.PubChem — compound summary for Amylin (CID 16132430)
- 10.Wikipedia — Amylin (islet amyloid polypeptide)