15% OFF $150+· CodeFALL15
Ends October 15Shop now
Lot certificates published
Discreet shipping

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.

Published: 2026-09-14Literature/identifier verification: 2026-09-13

01

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 formulaC171H267N51O53S2
Molecular mass3949.4 Da
CAS Registry Number151126-32-8
PubChem CID70691388
UNIID3FM8FA78T
One-letter sequenceKCNTATCATQRLANFLVHSSNNFGPILPPTNVGSNTY

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.

03

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

Terminal features: C-terminal amide at Tyr37.

04

Molecular targets & mechanisms

05

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 reports stability at pH 4 across roughly 1.8 to 8.8 mg per mL and a tendency to aggregate at pH 6 to 7.5. 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.

06

Verified bibliography

  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

    current
  2. Amyloidogenesis of the amylin analogue pramlintide.

    da Silva DC, Fontes GN, Erthal LC, Lima LM

    Biophysical chemistry · 2016-09-20 · Journal Article

    current
  3. Effects of sequential proline substitutions on amyloid formation by human amylin20-29.

    Moriarty DF, Raleigh DP

    Biochemistry · 1999-02-09 · Journal Article

    current
  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
  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
  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

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.

Read the full methodology →