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Pramlintide vs Amylin (human IAPP)

Pramlintide differs from the recorded human amylin sequence at three positions, carrying proline in place of Ala25, Ser28 and Ser29.

Published: 2026-10-03Library record comparison: 2026-10-03

01

Identity side by side

Recorded molecular identities of Pramlintide and Amylin (human IAPP)
Recorded fieldPramlintideAmylin (human IAPP)
Canonical namePramlintideAmylin
Aliasesnot recordedHuman islet amyloid polypeptide; IAPP; hIAPP; Amlintide
Development codesAC137not recorded
CAS151126-32-8122384-88-7
UNIID3FM8FA78TU3U3114NE1
PubChem CID7069138816132430
Molecular formulaC171H267N51O53S2C165H261N51O55S2
Molecular weight (Da)3949.43903.3
Sequence length (residues)3737
Terminal modificationsC-terminal amide at Tyr37C-terminal amide at Tyr37
Structural modificationsCys2-Cys7 disulfide; A25P; S28P; S29PCys2-Cys7 disulfide

Pramlintide: nomenclature notes

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.

Amylin (human IAPP): nomenclature notes

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.

02

Residue sequence comparison

Positions are numbered from each stored sequence’s first residue. Highlighted cells differ or extend beyond the other chain; a dash indicates no aligned residue. One-letter notation does not encode terminal groups or stereochemistry. Read the recorded notes below.

Aligned one-letter residue sequences
Pramlintide1K2C3N4T5A6T7C8A9T10Q11R12L13A14N15F16L17V18H19S20S21N22N23F24G25P26I27L28P29P30T31N32V33G34S35N36T37Y
Amylin (human IAPP)1K2C3N4T5A6T7C8A9T10Q11R12L13A14N15F16L17V18H19S20S21N22N23F24G25A26I27L28S29S30T31N32V33G34S35N36T37Y

Differences in text

  • Pramlintide: residue 25 = P; Amylin (human IAPP): residue 25 = A.
  • Pramlintide: residue 28 = P; Amylin (human IAPP): residue 28 = S.
  • Pramlintide: residue 29 = P; Amylin (human IAPP): residue 29 = S.

Pramlintide

Terminal modifications
C-terminal amide at Tyr37
Structural modifications
Cys2-Cys7 disulfide; A25P; S28P; S29P
Sequence notes
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.

Amylin (human IAPP)

Terminal modifications
C-terminal amide at Tyr37
Structural modifications
Cys2-Cys7 disulfide
Sequence notes
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

Recorded mechanisms

These lists show the links recorded in each monograph. An unlisted link does not establish its absence from the molecule’s biology.

Shared recorded links

Recorded only for Pramlintide

not recorded

Recorded only for Amylin (human IAPP)

not recorded

04

Recorded compound classes

Recorded only for Pramlintide

not recorded

Recorded only for Amylin (human IAPP)

not recorded

05

References for the relationship

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

    Moriarty DF, Raleigh DP

    Biochemistry · 1999-02-09 · Journal Article

    current
  2. 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

06

Read the full monographs