Compound monograph
Pramlintide
Pramlintide is an engineered analog of human amylin carrying three proline substitutions, designed to address the aggregation behaviour of the native human sequence.
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Identity & nomenclature
Pramlintide is an engineered analog of human amylin carrying three proline substitutions, designed to address the aggregation behaviour of the native human sequence.
Pramlintide is not another name for human amylin and not identical to rat amylin. It differs from human amylin at exactly three positions: A25P, S28P, S29P. The CAS recorded here is the peptide; a pramlintide acetate record describes a salt and must not replace this identity.
Declared aliases and development codes: AC137.
02
Molecular properties
| Molecular formula | C171H267N51O53S2 |
|---|---|
| Molecular mass | 3949.4 Da |
| CAS Registry Number | 151126-32-8 |
| PubChem CID | 70691388 |
| UNII | D3FM8FA78T |
| One-letter sequence | KCNTATCATQRLANFLVHSSNNFGPILPPTNVGSNTY |
| Terminal groups | Free N-terminus; C-terminal amide at Tyr37 |
Thirty-seven residues, Cys2-Cys7 disulfide, C-terminal Tyr37 amide — identical to human amylin except at three positions, where alanine 25 and serines 28 and 29 are each replaced by proline. It is not lipidated.
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Structural characteristics
Why this molecule exists belongs at the front of any description of it: human amylin aggregates, and the three prolines were introduced to reduce that propensity. The substitutions place it structurally between human amylin and cagrilintide — cagrilintide retains all three prolines and adds N14E, V17R, a Pro37 amide and N-terminal lipidation. The corpus records that chain as a structural relationship only; it is not a claim that the three molecules have interchangeable receptor profiles or physical behaviour. The receptor-comparison study PMID 33727283 tests pramlintide itself alongside selective and nonselective calcitonin-family receptor agonists. Its native amylin comparator is rat amylin, whose sequence differs from human amylin; those comparator data are not evidence for the human-amylin sequence.
- Cys2-Cys7 disulfide
- A25P
- S28P
- S29P
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). Registry source: FDA GSRS UNII D3FM8FA78T; PubChem CID 70691388.
Terminal features: Free N-terminus, C-terminal amide at Tyr37.
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Molecular targets & mechanisms
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Analytical considerations
THE AGGREGATION CLAIM NEEDS CARE, and this is the entry where the library should be most explicit. Pramlintide is widely described as non-aggregating. Exact-compound work reports it assembling into multimers and forming amyloid fibrils in vitro in a pH-dependent process, characterised by thioflavin T binding, loss of soluble peptide, transmission electron microscopy, atomic force microscopy and X-ray diffraction. Separate biophysical work reported pH-dependent stability and aggregation. Reduced propensity relative to human amylin is real; categorical immunity is not established. Neither the three prolines nor a chromatographic purity figure establishes the absence of higher-order assemblies in a given sample. Identity confirmation should also target positions 25, 28 and 29 specifically rather than relying on regions shared with human amylin.
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 · Chemical behaviour
How the aggregation of pramlintide is describedOften mixed up · Name or substance
Pramlintide vs human and rat amylinOften mixed up · Salt or form
Pramlintide CAS number: peptide vs acetate salt record
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
Pramlintide in ion-mobility mass-spectrometry assays
The study by da Silva et al. observed pramlintide multimer assembly using ion-mobility mass spectrometry.
Reference [2]Pramlintide in cell-free amyloid-formation assays
The study by da Silva et al. observed pH-dependent pramlintide amyloid-fibril formation using thioflavin-T fluorescence, soluble-peptide quantification, electron microscopy, atomic-force microscopy, and X-ray diffraction.
Reference [2]
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Verified bibliography
Cited studies by type
The 6 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
A biophysical characterization of the peptide drug pramlintide (AC137) using empirical phase diagrams.Nonoyama A, Laurence JS, Garriques L, Qi H, Le T, Middaugh CR
Journal of pharmaceutical sciences · 2008-07 · Journal Article
currentReference 2
Amyloidogenesis of the amylin analogue pramlintide.da Silva DC, Fontes GN, Erthal LC, Lima LM
Biophysical chemistry · 2016-09-20 · 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
AM833 Is a Novel Agonist of Calcitonin Family G Protein-Coupled Receptors: Pharmacological Comparison with Six Selective and Nonselective Agonists.Fletcher MM, Keov P, Truong TT, Mennen G, Hick CA, Zhao P, Furness SGB, Kruse T, Clausen TR, Wootten D, Sexton PM
The Journal of pharmacology and experimental therapeutics · 2021-03-16 · 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 |
|---|---|
| Nonoyama A et al. 2008 | Chemical, structural or analytical study; no biological model reported |
| da Silva DC et al. 2016 | 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 |
| Fletcher MM et al. 2021 | Study models reported: in vitro · from the abstract |
Compare
Record history
Published 2026-09-14.
- : Analytical notes
- : Sequence and structure
- : Sequence and structure
- : 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. Pramlintide. Published 2026-09-14; updated 2026-10-16. https://purelypeptides.org/research/compounds/pramlintide/
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Methodology & citation verification
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