Amylin
Amylin is a peptide, indexed here under Amylin and amylin receptor agonists.
Identity
| Field | Value |
|---|---|
| Classification | Peptide |
| Primary class | Amylin and amylin receptor agonists |
| CAS registry number | 122384-88-7[1] |
| PubChem CID | 16132430[1] |
| UniProt accession | Unknown No UniProt query was run in v1. |
| Molecular formula | C165H261N51O55S2[1] |
| Molecular weight | 3903.3 g/mol[1] |
| Amino-acid sequence | Unknown Not reported by the PubChem property set retrieved for this record; no sequence database query was run in v1. |
| Reported half-life | Unknown No pharmacokinetics source was retrieved in v1. PubChem does not carry half-life as a property, so this is recorded as not yet sourced rather than estimated. |
What the cited literature examines
Amylin, also called islet amyloid polypeptide, is the endogenous pancreatic hormone that the analogues in this class are modelled on. A 2011 Physiological Reviews article covers islet amyloid polypeptide, islet amyloid and diabetes mellitus, a 2002 Pharmacological Reviews nomenclature paper places it in the calcitonin gene-related peptide family, and a 1999 Molecular Pharmacology paper reports that multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product. A 1988 Nature paper reports that pancreatic amylin and calcitonin gene-related peptide cause insulin resistance in skeletal muscle in vitro.
Most of the retrieved records concern its aggregation. A 1990 Proceedings of the National Academy of Sciences paper pinpoints residues linked to amyloid fibril formation, a 1994 Nature paper reports islet cell toxicity of amylin associated with type 2 diabetes, 1996 and 1999 papers report pore formation and membrane disruption, a 2007 Biochemistry paper reports fibril conformation by solid-state NMR, a 2008 Proceedings of the National Academy of Sciences paper reports membrane damage through fibril growth, and a 2010 Nature Immunology paper reports activation of the NLRP3 inflammasome.
[3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13]Reported mechanism
The endogenous ligand of the amylin receptors, which the retrieved records describe as calcitonin receptor and receptor activity-modifying protein complexes; its aggregation into islet amyloid dominates the retrieved literature.
[5, 3]Stated in the titles of the cited 1999 Molecular Pharmacology and 2011 Physiological Reviews papers.
Targets named in the cited records: amylin receptors, calcitonin receptor.
FDA application register
A query of the FDA Drugs@FDA application register on 2026-10-09 returned no application records for this compound name. This compound is not approved by the FDA for human use.[2]
Scope statement: this records the result of a single automated query against the openFDA drugsfda endpoint on the stated date. It is not legal advice and is not a jurisdiction-by-jurisdiction legality assessment.
Retrieved 2026-10-09.
Amounts reported in the cited literature
Unknown. No retrieved record in this dataset states an amount, so none is shown. Where an amount is recorded it is what a named study reported administering in its own stated model, in the past tense, and is not a protocol.
No study-reported dose was taken from a source read in v1. Literature-reported values are only recorded where the retrieved citation metadata states the figure.
Adverse effects reported in the cited literature
Unknown. No retrieved record in this dataset reports an adverse effect for this compound, so no row is shown. Absence of a row records the absence of a retrieved report, nothing more.
No adverse-effect row was taken from a source read in v1. Rows are only recorded with the study model named and the reporting citation attached.
Other names
Amylin appears under these other names in the cited records or in common usage. Each one resolves to this page rather than to a separate page of its own.
- islet amyloid polypeptide
- IAPP
Where this page sits
Research records
Cited research records for Amylin, each with its identifier, the publication type it is indexed as, and the study model stated by its assigned subject headings.
Compounds indexed next to it
- Pramlintide — Amylin and amylin receptor agonists
- Cagrilintide — Amylin and amylin receptor agonists
Class page: Amylin and amylin receptor agonists. Full index: all indexed compounds.
Questions this page answers
What does the cited literature examine for Amylin?
Amylin, also called islet amyloid polypeptide, is the endogenous pancreatic hormone that the analogues in this class are modelled on. A 2011 Physiological Reviews article covers islet amyloid polypeptide, islet amyloid and diabetes mellitus, a 2002 Pharmacological Reviews nomenclature paper places it in the calcitonin gene-related peptide family, and a 1999 Molecular Pharmacology paper reports that multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product.
Which class is Amylin indexed under?
Amylin is indexed under Amylin and amylin receptor agonists. This class groups the pancreatic hormone amylin, also called islet amyloid polypeptide, and the synthetic analogues modelled on it.
What does the FDA application register show for Amylin?
A query of the FDA Drugs@FDA application register on 2026-10-09 returned no application records for this compound name. This compound is not approved by the FDA for human use.
Sources
- PubChem Compound Summary for CID 16132430, Islet Amyloid Polypeptide. PubChem, National Library of Medicine (2026). pubchem:16132430
- Drugs@FDA application register query for this compound, no application records returned. U.S. Food and Drug Administration, openFDA drugsfda endpoint (2026). fda:amylin
- Islet amyloid polypeptide, islet amyloid, and diabetes mellitus. Physiological reviews (2011). pmid:21742788
- International Union of Pharmacology. XXXII. The mammalian calcitonin gene-related peptides, adrenomedullin, amylin, and calcitonin receptors. Pharmacological reviews (2002). pmid:12037140
- Multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product. Molecular pharmacology (1999). pmid:10385705
- Pancreatic amylin and calcitonin gene-related peptide cause resistance to insulin in skeletal muscle in vitro. Nature (1988). pmid:3050530
- Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation. Proceedings of the National Academy of Sciences of the United States of America (1990). pmid:2195544
- Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus. Nature (1994). pmid:8152488
- Pore formation by the cytotoxic islet amyloid peptide amylin. The Journal of biological chemistry (1996). pmid:8567648
- The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles. Diabetes (1999). pmid:10078548
- Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR. Biochemistry (2007). pmid:17979302
- Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane. Proceedings of the National Academy of Sciences of the United States of America (2008). pmid:18408164
- Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1β in type 2 diabetes. Nature immunology (2010). pmid:20835230
On each stated value was matched to the record cited for it. That is record matching, not an appraisal of the research. Compiled and checked by: Peptide Monographs editorial desk. No qualified clinical reviewer.