Library / Metabolic Research / Amylin
Evidence: Early humanNatural hormone; analogues studiedWeight & metabolism

Amylin

Natural 37-amino-acid hormone released together with insulin from pancreatic beta cells.

37Amino acids
~3,903.3Daltons
C₁₆₅H₂₆₁N₅₁O₅₅S₂Formula
1987Research period
AmylinIllustrative conformer; drag to rotate.
CNO

Illustrative backbone only; the disulfide bond and terminal amidation are not represented as an experimentally determined structure.

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Overview

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In plain language

Amylin is a natural 37-amino-acid hormone released with insulin by pancreatic beta cells. It helps regulate food intake and glucose handling by promoting satiation, slowing gastric emptying and limiting post-meal glucagon release. (Le Foll & Lutz, 2026)

Native human amylin can aggregate under certain conditions. Pramlintide is a modified amylin analogue, not the same molecule: its FDA-approved role is as an adjunct to mealtime insulin in specified patients with diabetes. (Le Foll & Lutz, 2026) (FDA Symlin label, 2015)

Pramlintide used with insulin carries a boxed warning for severe hypoglycemia. Approval of an analogue does not make native amylin, other analogues or unrelated products approved treatments. (FDA Symlin label, 2015)

Molecular identity

Amino acids
37
Molecular weight
~3,903.3 Da
Formula
C₁₆₅H₂₆₁N₅₁O₅₅S₂
Sequence
KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY-NH₂ (Cys2–Cys7 disulfide)

Sequence map

HydrophobicPolarPositiveNegativeGly / Pro

Hydropathy

Kyte–Doolittle score per residue. Positive values are water-repelling.

Form clarification: Human amylin with C-terminal amide and one disulfide bond. Molecular weight is a reference value, not a certificate of analysis.

Origin and history

Amylin/IAPP emerged from work on pancreatic islet amyloid in the mid-1980s. Cooper and colleagues reported purification of a 37-amino-acid peptide from amyloid-rich pancreases of people with type 2 diabetes in 1987. (Le Foll & Lutz, 2026) (Cooper et al., 1987)

This discovery connected a physiological hormone with protein-aggregation research. Later analogue development is a separate story: the 2015 FDA Symlin label documents pramlintide's chemical substitutions, indication and safety limitations. (FDA Symlin label, 2015)

Human evidence

The native hormone has human physiological evidence. The Early human category here does not describe every analogue: pramlintide has its own FDA-approved product and safety requirements. Neither that approval nor a study of another analogue establishes approval of native human amylin. (Le Foll & Lutz, 2026) (FDA Symlin label, 2015)

Safety and regulatory status

Native amylin is not interchangeable with pramlintide. The latter's label includes a boxed warning for severe hypoglycemia when used with insulin. This is a non-exhaustive educational distinction, not prescribing advice; the linked 2015 label is a dated regulatory reference. (FDA Symlin label, 2015)

Editorial update · November 9, 2026

Separated the native hormone from pramlintide, added direct physiology and drug-label references, and removed an unsupported company-founding date. An analogue's approval is not approval of native amylin.

Sources

  1. Le Foll & Lutz, 2026https://pmc.ncbi.nlm.nih.gov/articles/PMC13588233/
  2. Cooper et al., 1987http://www.ncbi.nlm.nih.gov/pmc/articles/PMC299599
  3. FDA Symlin label, 2015https://www.accessdata.fda.gov/drugsatfda_docs/label/2015/021332s025lbl.pdf
Cite this page

Hernandez Gener, E. (2026, November 9). Amylin: molecular data, research history and evidence. VALREXA Biosciences. https://valrexa.com/peptides/amylin.html

APA style · Editorially updated November 9, 2026 · Our editorial standards

Editorially updated November 9, 2026. Trial and regulatory status can change; confirm in the linked registries. This profile is educational and is not medical advice, a treatment recommendation, or dosing or sourcing guidance. Report an error · Corrections policy

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