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.
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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.
Canonical name: Amylin.
Declared aliases and development codes: Human islet amyloid polypeptide, IAPP, hIAPP, Amlintide.
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Molecular properties
| Molecular formula | C165H261N51O55S2 |
|---|---|
| Molecular mass | 3903.3 Da |
| CAS Registry Number | 122384-88-7 |
| PubChem CID | 16132430 |
| UNII | U3U3114NE1 |
| One-letter sequence | KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTY |
| Terminal groups | Free N-terminus; C-terminal amide at Tyr37 |
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. Young et al. (PMID 28970890) describe human IAPP as containing a disulfide bond between Cys-2 and Cys-7 and an amidated C-terminus. The IUPHAR/BPS Guide to Pharmacology (ligand 687, release 2026.3.1) names an amidated C-terminal proline in its modification text while its own sequence ends in amidated tyrosine; this record keeps the Tyr37 amide.
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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. Two mitochondrial-derived peptides in this library, HNG and SHLP2, were tested against this peptide's misfolding: thioflavin T fluorescence, seeded fluorescence and co-sedimentation supported binding to misfolded, seeding-capable IAPP species, while electron paramagnetic resonance and circular dichroism did not support binding to IAPP monomers. That distinction belongs on this record rather than only on theirs, because this entry specifies the mature monomeric peptide and the reported interaction is with aggregated species, not with the molecule described here.
- Cys2-Cys7 disulfide
Ring closures: covalent bonds between residues, by position counted from the first residue of the chain.
- Disulfide Cys2–Cys7: thiol sulfur (Sγ) to thiol sulfur (Sγ). Source: PMID 28970890.
Terminal features: Free N-terminus, C-terminal amide at Tyr37.
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Molecular targets & mechanisms
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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.
Disagreements and mix-ups
Points where sources disagree about this compound's identity, or where a name or form is easily confused with another, as noted in this record. The discrepancy register quotes the passage for each one.
Sources disagree · this Library follows one source · Registry record
Human amylin's C-terminus in the Guide to PharmacologyOften mixed up · Name or substance
Amylin, IAPP and related precursor and species namesOften mixed up · Name or substance
Amlintide vs pramlintideOften mixed up · Name or substance
Receptor genes CALCR and CALCRL
What the studies reported
Each finding describes one cited study in its stated model. These observations are specific to that study and do not establish effects in other settings.
Cell and tissue studies
Synthetic amylin 20-29 peptide fragments in aggregation assays
Moriarty et al. observed that a proline substitution at any position of the synthetic amylin 20-29 fragment inhibited aggregation and amyloid formation.
Reference [3]IAPP in thioflavin-T fluorescence assays
Okada et al. observed that humanin-S14G inhibited IAPP misfolding in cell-free thioflavin-T fluorescence assays.
Reference [6]IAPP monomers in EPR and circular-dichroism assays
Okada et al. found no evidence for binding of humanin-S14G or SHLP2 to IAPP monomers in electron-paramagnetic-resonance and circular-dichroism assays.
Reference [6]IAPP variants in ESI-IMS-MS and thioflavin-T fluorescence assays
Young et al. identified a subpopulation of extended IAPP monomers associated with amyloid assembly using electrospray ionization-ion mobility mass spectrometry and thioflavin-T fluorescence assays.
Reference [7]Human wild-type and S20G IAPP with rat IAPP in seeding assays
Young et al. found that wild-type human IAPP fibrils did not cross-seed rat IAPP fibril formation and that S20G IAPP fibrils did not cross-seed wild-type human or rat IAPP in thioflavin-T assays.
Reference [7]
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Verified bibliography
Cited studies by type
The 7 papers this record cites, counted by the kind of work each reports. A count is the size of this record's selection, not of the research that exists, and says nothing about results, safety, effectiveness or approval.
A paper can report more than one kind of work. Each count opens those papers in the bibliography. Compare every record on the Evidence Map.
Reference 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
currentReference 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
currentReference 3
Effects of sequential proline substitutions on amyloid formation by human amylin20-29.Moriarty DF, Raleigh DP
Biochemistry · 1999-02-09 · Journal Article
currentReference 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
currentReference 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
currentReference 6
The Mitochondrial-Derived Peptides, HumaninS14G and Small Humanin-like Peptide 2, Exhibit Chaperone-like Activity.Okada AK, Teranishi K, Lobo F, Isas JM, Xiao J, Yen K, Cohen P, Langen R
Scientific reports · 2017-08-10 · Journal Article
currentReference 7
Understanding co-polymerization in amyloid formation by direct observation of mixed oligomers.Young LM, Tu LH, Raleigh DP, Ashcroft AE, Radford SE
Chemical science · 2017-05-09 · Journal Article
current
Study models of these references
What kind of experiment each cited paper reports, taken from its abstract unless marked. Not a summary of results.
| Reference | Study models |
|---|---|
| Westermark P et al. 1987 | Study models reported: in vitro · from the abstract |
| Cooper GJ et al. 1987 | Study models reported: in vitro · from the abstract |
| Moriarty DF et al. 1999 | Study models reported: in vitro · from the abstract |
| Kruse T et al. 2021 | Study models reported: in vitro; animal (rat) · from the full text |
| Cao J et al. 2025 | Study models reported: in vitro · from the abstract |
| Okada AK et al. 2017 | Study models reported: in vitro · from the abstract |
| Young LM et al. 2017 | Study models reported: in vitro · from the abstract |
Compare
Record history
Published 2026-09-14.
- : Sequence and structure
- : Sequence and structure, References
- : Sequence and structure, References
Each entry names the parts of this record that changed on that date. Changes to links between records and to catalogue links are not listed. This history covers the tracked record fields; study findings are not listed here.
Cite this record: Purely Peptides Research Library. Amylin (human IAPP). Published 2026-09-14; updated 2026-10-14. https://purelypeptides.org/research/compounds/amylin/
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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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