Amylin
Amylin (islet amyloid polypeptide)
Written by Aaron CuhaReviewed Sep 2026
Also known as: IAPP, Islet amyloid polypeptide, Diabetes-associated peptide
Co-released with insulin from the same beta cell, and the parent ligand of cagrilintide and CagriSema. Native human amylin clumps into amyloid, which is why it can never be a drug.
Overview
Amylin is secreted alongside insulin from the pancreatic beta cell in a roughly fixed ratio, which has a consequence people miss: someone with type 1 diabetes is deficient in two hormones, not one. It slows gastric emptying, suppresses glucagon after a meal, and produces satiation through the area postrema in the brainstem.
The central fact about human amylin is that it is amyloidogenic. It self-aggregates into the islet amyloid deposits that give it its other name, and that is not a footnote. It is the reason native human amylin cannot be formulated as a medicine at all, and the reason every amylin drug is a redesigned analogue. Pramlintide swaps in three prolines to block aggregation. Cagrilintide is engineered for a long half-life. Neither is amylin.
Mechanism of action
Acts at amylin receptors, which are not dedicated receptors at all but the calcitonin receptor in complex with a receptor activity-modifying protein. RAMP1, RAMP2 or RAMP3 give AMY1, AMY2 and AMY3 respectively, and that accessory-protein mechanism is why amylin pharmacology overlaps with calcitonin. Physiologically it slows gastric emptying, suppresses postprandial glucagon and drives satiation via the area postrema.
Human evidence
Deep for the analogues, essentially absent for the hormone. Pramlintide has randomised trials over a year in type 1 and type 2 diabetes, and cagrilintide has phase 3 data. Native amylin has never been given as a treatment because it cannot be.
- Pramlintide as a mealtime insulin adjunct in type 1 diabetes: 651 participants, 52 weeks, HbA1c down 0.29 to 0.34 points against 0.04 on placebo, with weight loss rather than the weight gain insulin usually brings.
- A pramlintide and insulin co-formulation lowered bodyweight against insulin lispro in type 1 diabetes in a randomised trial.
- Cagrilintide, a long-acting analogue, has phase 3 data both alone and combined with semaglutide as CagriSema, including in type 2 diabetes.
- The approved analogue's brand is marked Discontinued in Drugs@FDA, which we verified against the regulator directly.
What this does not tell you: No randomised trial shows that amylin or any analogue prevents or reverses islet amyloid deposition in a person, which is the mechanism the hormone is named for. No amylin analogue has cardiovascular outcome data on its own; CagriSema's outcome data belong to a combination that includes semaglutide, so the amylin contribution cannot be separated out. The satiety circuitry is largely rodent work.
Reading the research record
Amylin is a useful case study in the gap between a hormone and a drug. The biology has been understood for thirty years and the therapeutic history is thin, because the molecule sabotages itself: human amylin aggregates, and an aggregating peptide cannot be put in a vial.
There is also a regulatory fact most peptide sites omit. Pramlintide was the only amylin analogue ever approved for diabetes, and every Symlin product is now listed as Discontinued. Meanwhile cagrilintide is heading through phase 3 inside a combination product. The class went from approved-and-withdrawn to investigational-and-promising, which is unusual and worth knowing before reading any confident claim about amylin drugs.
The evidence, charted
Fig. 1 · evidence composition
2of 3 citations (67%) are in people
Counted from the citation list on this page. The Human count is the same number shown in the badge at the top. Both understate any literature larger than the sources we cite.
Fig. 2 · evidence over time
Evidence spans 3 distinct years, 2004 to 2025, counted from the citation list on this page.
Fig. 3 · legal status at a glance
US
Not approved
UK
Approved
AU
Not approved
CA
Not approved
Approved in 1 of 4, prescription route in 0, not approved in 3. A jurisdiction's classification is a regulatory fact, not a verdict on the science; see Legal status below for the full text and any notes.
Key studies & citations
- Review2015
Amylin: pharmacology, physiology, and clinical potential
The definitive pharmacology review, covering the calcitonin-receptor-plus-RAMP mechanism, the physiology, and why the amyloidogenicity of the human peptide constrains every drug built from it.
Pharmacological Reviews - Human2004
Amylin replacement with pramlintide as an adjunct to insulin therapy improves long-term glycaemic and weight control in type 1 diabetes mellitus: a 1-year, randomized controlled trial
651 people with type 1 diabetes, 52 weeks, randomised. HbA1c fell 0.29 to 0.34 percentage points against 0.04 on placebo. Statistically clear and clinically modest, and the page says so rather than rounding it up.
Diabetic Medicine - Human2025
Coadministered cagrilintide and semaglutide in adults with overweight or obesity
Phase 3a, 68 weeks, double-blind, with a cagrilintide-alone arm. That arm is the cleanest human read available on what an amylin receptor agonist does by itself rather than as half of a combination.
New England Journal of Medicine
Frequently asked questions
Can I take amylin?
No. Native human amylin aggregates into amyloid, which is why it has never been a medicine in its own form. The drugs are redesigned analogues: pramlintide substitutes three prolines to stop the clumping, and cagrilintide is engineered for a long half-life.
Why does type 1 diabetes involve amylin?
Because amylin and insulin come from the same beta cell in a roughly fixed ratio. When those cells are destroyed, both hormones go. That is the logic behind giving pramlintide alongside insulin rather than insulin alone.
Is pramlintide still available?
Drugs@FDA lists every Symlin product as Discontinued as of September 2026, which we checked directly against the regulator. It remains an approved drug on paper. Approved and available are not the same thing.
Does amylin cause the islet amyloid in type 2 diabetes?
Human amylin is the protein those deposits are made of, and the aggregation is well established in the laboratory. What no trial has shown is that giving an amylin analogue prevents or reverses that deposition in a living person.