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Research Catalog

Compound monograph

Amylin (human IAPP)

Amylin is the endogenous 37-residue human pancreatic peptide hormone, co-secreted with insulin, from which pramlintide and cagrilintide are both derived.

Published: 2026-09-14Literature/identifier verification: 2026-09-13
Human islet amyloid polypeptideIAPPhIAPPAmlintideAmylin and calcitonin receptor agonists

01

Identity & nomenclature

Amylin is the endogenous 37-residue human pancreatic peptide hormone, co-secreted with insulin, from which pramlintide and cagrilintide are both derived.

Amylin and IAPP are the same molecule under two names when both refer to this mature human peptide. They are NOT synonyms for the IAPP gene, for proIAPP, for a processing intermediate, for the reduced peptide, or for rodent amylin — rat amylin differs in sequence and is a common substitute in structural work. The FDA substance record uses 'amlintide' as a preferred name for this peptide; amlintide is NOT pramlintide, which carries three proline substitutions and is a separate entry in this library.

Declared aliases and development codes: Human islet amyloid polypeptide, IAPP, hIAPP, Amlintide.

02

Molecular properties

Molecular formulaC165H261N51O55S2
Molecular mass3903.3 Da
CAS Registry Number122384-88-7
PubChem CID16132430
UNIIU3U3114NE1
One-letter sequenceKCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY

Thirty-seven residues with a Cys2-Cys7 disulfide and a C-terminal Tyr37 amide. The backbone string alone is not a complete description: both the disulfide and the amide are required, and neither is visible in a linear sequence.

03

Structural characteristics

It was identified twice in 1987 by independent groups — once from human insulinoma and cat islet amyloid, once from amyloid-rich pancreatic extracts — reaching the same 37-residue sequence, with roughly 40 to 46 percent identity to calcitonin gene-related peptide. That evolutionary relationship to CGRP is why its receptors are calcitonin receptor complexes rather than a receptor of its own. Amylin receptors are CALCR associated with receptor activity-modifying proteins: AMY1, AMY2 and AMY3 correspond to RAMP1, RAMP2 and RAMP3. CALCRL is a different gene and must not be substituted for CALCR, and there is no standalone IAPP receptor gene to name.

  • Cys2-Cys7 disulfide

Terminal features: C-terminal amide at Tyr37.

04

Molecular targets & mechanisms

Amylin and calcitonin receptors

CALCR · CTR · AMY1 · AMY2 · AMY3 · RAMP1 · RAMP2 · RAMP3

The calcitonin receptor, and the amylin receptor complexes it forms when associated with receptor activity-modifying proteins RAMP1, RAMP2 or RAMP3. Because the amylin receptors are heteromers rather than distinct gene products, receptor construct and accessory-protein expression must accompany any selectivity claim; a potency ranking is not transferable between assay systems.

05

Analytical considerations

Sequence identity, disulfide connectivity, terminal amidation and AGGREGATION STATE are four separate attributes and a matching intact mass establishes only the first. This peptide was discovered in amyloid deposits; a correct mass says nothing about whether a given preparation is monomeric or already contains higher-order assemblies, and the library should not assert an aggregation state it has not measured. Rat amylin is a frequent comparator in structural work and differs in sequence, so a structure obtained with it is not evidence about this molecule.

06

Verified bibliography

  1. Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells.

    Westermark P, Wernstedt C, Wilander E, Hayden DW, O'Brien TD, Johnson KH

    Proceedings of the National Academy of Sciences of the United States of America · 1987-06 · Journal Article

    current
    PMID 3035556PMC304980DOI 10.1073/pnas.84.11.3881Amylin (human IAPP)
  2. Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients.

    Cooper GJ, Willis AC, Clark A, Turner RC, Sim RB, Reid KB

    Proceedings of the National Academy of Sciences of the United States of America · 1987-12 · Journal Article

    current
    PMID 3317417PMC299599DOI 10.1073/pnas.84.23.8628Amylin (human IAPP)
  3. Effects of sequential proline substitutions on amyloid formation by human amylin20-29.

    Moriarty DF, Raleigh DP

    Biochemistry · 1999-02-09 · Journal Article

    current
    PMID 10026261DOI 10.1021/bi981658gAmylin (human IAPP)Pramlintide
  4. Development of Cagrilintide, a Long-Acting Amylin Analogue.

    Kruse T, Hansen JL, Dahl K, Schäffer L, Sensfuss U, Poulsen C, Schlein M, Hansen AMK, Jeppesen CB, Dornonville de la Cour C, Clausen TR, Johansson E, Fulle S, Skyggebjerg RB, Raun K

    Journal of medicinal chemistry · 2021-07-21 · Journal Article

    current
    PMID 34288673DOI 10.1021/acs.jmedchem.1c00565CagrilintideAmylin (human IAPP)PramlintideCALCR
  5. Structural and dynamic features of cagrilintide binding to calcitonin and amylin receptors.

    Cao J, Belousoff MJ, Johnson RM, Keov P, Mariam Z, Deganutti G, Christopoulos G, Hick CA, Reedtz-Runge S, Glendorf T, Ballarín-González B, Raun K, Bayly-Jones C, Wootten D, Sexton PM

    Nature communications · 2025-04-10 · Journal Article

    current
    PMID 40204768PMC11982234DOI 10.1038/s41467-025-58680-yCagrilintideAmylin (human IAPP)PramlintideCALCR

10

Methodology & citation verification

Reference identity is checked against official PubMed metadata. Local deterministic receipts bind each normalized title and canonical metadata record to its verification date. Scientific values remain absent when an authoritative source has not been verified.

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