Metabolic & Weight

Amylin

Amylin (IAPP) is a 37-aa peptide co-secreted with insulin by beta cells that suppresses glucagon, slows gastric emptying, and reduces food intake. Deficient in T1D and late T2D. Pramlintide is its FDA-approved synthetic analogue.

C165H267N51O55S2Half-life: ~15-20 minutesMolar mass: 3903.30 g/mol

⚠ Research & Educational Use Only. Amylin is a research chemical documented here for scientific education. All information references peer-reviewed literature and preclinical/clinical study data. Not for human consumption. Not medical advice. Consult a licensed researcher or healthcare professional before any laboratory use.

Medically reviewed by Dr. Amanda Reid, MDWritten by the KnowYourPeptide Research TeamLast updated April 2026
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Key Takeaways
  • Suppresses postprandial glucagon secretion by approximately 50% — reduces hepatic glucose output post-meal
  • Slows gastric emptying rate — blunts postprandial glucose spike by regulating nutrient absorption speed
  • Reduces food intake via area postrema and nucleus tractus solitarius (NTS) in the brainstem
  • Amylin is not FDA-approved for human use. It is a research chemical for scientific study only.

Research At a Glance

  • Suppresses postprandial glucagon secretion by approximately 50% — reduces hepatic glucose output post-meal
  • Slows gastric emptying rate — blunts postprandial glucose spike by regulating nutrient absorption speed
  • Reduces food intake via area postrema and nucleus tractus solitarius (NTS) in the brainstem
  • Complementary to insulin — together they create the complete postprandial neuroendocrine response
Calculate Amylin dose

What is Amylin?

Amylin (Islet Amyloid Polypeptide, IAPP) is a 37-amino acid peptide synthesized and co-secreted with insulin by pancreatic beta cells in a 1:100 molar ratio to insulin. It was first identified in 1987 in amyloid deposits isolated from the islets of Langerhans in type 2 diabetic patients (Westermark et al., Cooper et al.).

Amylin acts on the amylin receptor complex (a heterodimer of calcitonin receptor + RAMP proteins, particularly RAMP1/3) in the area postrema, the brainstem, and hypothalamus. Via these receptors it

  • **Suppresses postprandial glucagon**: Reduces alpha-cell glucagon secretion by 40-60%, limiting hepatic glucose output after meals
  • **Slows gastric emptying**: Creates a "brake" on the rate of nutrient delivery to the small intestine, smoothing glucose absorption kinetics
  • **Reduces food intake**: Acts centrally via area postrema → NTS → arcuate nucleus to induce satiety independent of leptin
  • **Modulates bone turnover**: Amylin/calcitonin receptor overlap means amylin has weak bone-anabolic properties

Amylin deficiency is complete in type 1 diabetes (total beta cell loss) and progressive in late type 2 diabetes (beta cell failure). This amylin deficit is why insulin therapy alone produces suboptimal glycemic control — the full postprandial hormonal response requires both insulin and amylin.

The pathological side of amylin is its tendency to misfold and aggregate into insoluble amyloid fibrils in islet tissue — a key finding in type 2 diabetes pathology. Human IAPP is approximately 100x more prone to fibrillation than rodent IAPP (which has several proline substitutions blocking aggregation). Pramlintide reproduces rodent IAPP's proline substitution pattern to create a stable, clinically usable amylin analogue.

Research applications include: T1D/T2D adjunct therapy research, obesity and satiety studies, islet amyloid toxicity research, and incretin axis investigations.

Key Research Benefits

Documented effects observed in preclinical and clinical studies on Amylin. See all Metabolic & Weight peptides for comparison.

Suppresses postprandial glucagon secretion by approximately 50% — reduces hepatic glucose output post-meal
Slows gastric emptying rate — blunts postprandial glucose spike by regulating nutrient absorption speed
Reduces food intake via area postrema and nucleus tractus solitarius (NTS) in the brainstem
Complementary to insulin — together they create the complete postprandial neuroendocrine response
Relevant to satiety research and the gut-brain axis regulation of meal size
Structural template for pramlintide; fibril-forming properties studied in islet amyloid pathology research

Side Effects & Risks

Adverse effects reported in the research literature. All data sourced from preclinical and clinical study reports.

Native amylin aggregates into islet amyloid plaques (a hallmark of type 2 diabetes) — relevant to research on islet inflammation
At research concentrations, may produce nausea via area postrema activation
Potent hypoglycemia risk when co-administered with insulin at high concentrations
Native form is not suitable for clinical use due to rapid aggregation and fibrillogenesis

Dosing Data from the Literature

Doses referenced below are sourced from published preclinical and clinical studies. Use the peptide dose calculator to convert these values to injection volume.

Research Dosing Protocol

Amylin is primarily used as a research reference standard in studies of islet biology, gastric emptying, glucagon regulation, and appetite. IV infusion at 4-8 pmol/kg/min has been used in acute human studies to assess its effects on glycemia and appetite.

For clinical research, pramlintide (the synthetic non-aggregating analogue) has replaced native amylin: - Type 1 diabetes: 15-60 mcg SC before meals - Type 2 diabetes: 60-120 mcg SC before meals

Enter your vial size and target dose to get the exact injection volume.

Administration in Research Settings

Standard reconstitution and administration methodology for laboratory research use.

Research tool for in vitro islet studies, in vivo gastric emptying studies, and central appetite research. Pramlintide (stable analogue) is used in clinical and translational research.

Explore Further

Quick Reference

Half-Life
~15-20 minutes
Molar Mass
3903.30 g/mol
Formula
C165H267N51O55S2
Legal Status
Research peptide. Native amylin is not clinically used. Pramlintide (Symlin) is FDA-approved as an adjunct to insulin.
Storage
Store lyophilized amylin at -20°C. Avoid aggregation conditions — do not store in high concentration, heat, or acidic pH. Use plastic tubes rather than glass to reduce nucleation.

Research Use Only

This information is for educational research purposes only. This is not medical advice. Consult a qualified healthcare professional.