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Metabolic & GLP-1 · Reference monograph

Pancreatic peptide hormone co-secreted with insulin

Reference compound — not available from Purity Peptides. Shown for research context.

Overview

Amylin, also called islet amyloid polypeptide (IAPP), is a 37-amino-acid peptide hormone stored in and co-secreted with insulin from pancreatic beta cells. It was identified in 1987, independently by Garth Cooper's team in Oxford and Per Westermark's group in Sweden, as the principal component of the amyloid deposits found in the islets of people with type 2 diabetes.

The mature peptide carries a disulfide bond between cysteines 2 and 7 and an amidated C-terminus, both required for full activity. Human amylin is highly prone to aggregation, whereas rodent amylin is not, owing to proline residues in the central region; this difference has made amylin a major model for studying protein misfolding and islet amyloid toxicity. Physiologically, amylin complements insulin by restraining postprandial glucagon secretion, slowing gastric emptying and promoting satiety. Its instability led to the development of pramlintide, an approved analogue, and newer long-acting amylin analogues are being explored in obesity research. Amylin itself is an endogenous peptide studied as a research reference.

Mechanism studied

  1. Beta cell
  2. Amylin
  3. Area postrema satiety
  4. Gastric emptying & glucagon ↓

Amylin acts through amylin receptors (AMY1, AMY2 and AMY3), each formed when the calcitonin receptor associates with one of three receptor activity-modifying proteins (RAMP1, RAMP2 or RAMP3). These heterodimers couple mainly to Gs, increasing cAMP. A key site of action is the area postrema in the hindbrain, which lacks a complete blood-brain barrier; activation there relays signals through the nucleus of the solitary tract to forebrain regions controlling satiety. Through central pathways amylin also reduces postprandial glucagon secretion and slows gastric emptying. Amylin has been reported to enhance leptin sensitivity in rodent models, an interaction relevant to combination research.

Research highlights

  • 01Discovered in 1987 as the main constituent of islet amyloid in type 2 diabetes.
  • 02Species differences in aggregation propensity made human versus rodent amylin a classic model of amyloid formation.
  • 03Amylin receptors were defined as calcitonin receptor-RAMP complexes, an important discovery in receptor pharmacology.
  • 04Rodent studies of amylin-leptin co-signalling helped inspire research into combination approaches in obesity.
  • 05Open questions include the role of amylin oligomers in beta-cell loss and potential links between amylin and amyloid-beta biology.

Latest published research

4,563 papers on PubMed →

  1. Association Between Serum Amylin, Irisin, and Sirtuin 1 in Male Patients with Type 2 Diabetes and Diabetic Nephropathy

    Sabih Wajdi S et al. · International journal of endocrinology and metabolism · 2027 Jan 31 · PMID 42807762

  2. Amylin and the renin-angiotensin system: risk or opportunity in amylin-based therapy?

    Muskiet MHA et al. · Lancet (London, England) · 2026 Dec 20 · PMID 41207308

  3. Determinants of variable response to GLP-1 receptor agonists: A mechanism-informed framework for precision treatment of obesity

    Ghosal S et al. · Obesity pillars · 2026 Dec · PMID 42898214

  4. Inhibitory Activity of Red Panda Islet Amyloid Polypeptide on Human IAPP Aggregation

    Phillips L et al. · Journal of peptide science : an official publication of the European Peptide Society · 2026 Dec · PMID 42888478

  5. Revisiting the β-Cell: The Key to the Type 2 Diabetes Puzzle: The 2025 Banting Medal for Scientific Achievement Award Lecture

    Kahn SE et al. · Diabetes · 2026 Nov 1 · PMID 42900804

  6. Hypermetabolic State Drives Platelet Dysfunction in Human and Mouse Metabolic Dysfunction-Associated Steatotic Liver Disease

    Maiorca F et al. · Arteriosclerosis, thrombosis, and vascular biology · 2026 Nov · PMID 42817874

  7. Petrelintide, a human amylin analogue for the treatment of obesity (ZUPREME 1): a randomised, double-blind, placebo-controlled, phase 2 trial

    Garvey WT et al. · The lancet. Diabetes & endocrinology · 2026 Nov · PMID 42810355

  8. Petrelintide and the evolving role of amylin agonism in obesity

    Madsbad S et al. · The lancet. Diabetes & endocrinology · 2026 Nov · PMID 42810353

Live feed from PubMed (NCBI) for “Amylin”, updated 2026-10-30. Listing a paper is not an endorsement of its findings.

Registered studies

111 on ClinicalTrials.gov →

From the public ClinicalTrials.gov registry for “Amylin”, updated 2026-10-30. Shown for research context only; Purity Peptides products are not for human use.

Key references

  1. [1]Westermark et al., 2011 — Physiol Rev
  2. [2]PubMed — reviews on amylin and glucose regulation

FAQ

  • Human amylin readily forms amyloid fibrils and oligomers in solution, which complicates handling, storage and interpretation of results. Researchers often control aggregation using specific solvents, freshly prepared solutions or non-aggregating analogues such as rat amylin or pramlintide.

  • Receptor activity-modifying proteins are single-transmembrane accessory proteins that associate with certain class B G protein-coupled receptors. When paired with the calcitonin receptor, RAMPs create high-affinity amylin receptors, illustrating how accessory proteins can change receptor pharmacology.

  • Amylin is made by the same beta cells, stored in the same secretory granules and released together with insulin in response to nutrients. Conditions involving beta-cell loss, such as type 1 diabetes, therefore involve deficiency of both hormones.

FOR RESEARCH USE ONLY.Not for human or veterinary use. Not intended to diagnose, treat, cure, or prevent any disease.

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