Compound monograph
Apelin-13 (unmodified)
Apelin-13 is a 13-residue peptide with an N-terminal glutamine and a C-terminal phenylalanine. This record describes the unmodified parent with free terminal groups.
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Identity & nomenclature
Apelin-13 is a 13-residue peptide with an N-terminal glutamine and a C-terminal phenylalanine. This record describes the unmodified parent with free terminal groups.
This record specifies the unmodified free-terminal parent. Pyroglutamyl and amidated forms are distinct chemistry and are excluded as aliases. CAS and UNII are withheld under the dossier issuer-evidence limits.
Canonical name: Apelin-13.
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Molecular properties
| Molecular formula | C69H111N23O16S |
|---|---|
| Molecular mass | 1550.852 Da |
| PubChem CID | 25078060 |
| One-letter sequence | QRPRLSHKGPMPF |
| Three-letter sequence | Gln–Arg–Pro–Arg–Leu–Ser–His–Lys–Gly–Pro–Met–Pro–Phe |
| Terminal groups | Free N-terminus; Free C-terminal carboxyl |
Positions count the mature chain from 1. All chiral amino-acid residues are L; glycine is achiral. Terminal groups are recorded separately.
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Structural characteristics
The chain contains standard L-amino-acid residues and no inter-residue covalent closure.
Terminal features: Free N-terminus, Free C-terminal carboxyl.
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Molecular targets & mechanisms
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Analytical considerations
The molecular formula describes the parent; the average mass is calculated using CIAAW 2024 abridged atomic weights. PubChem reports 1550.8: +0.052 Da (+33.531 ppm), a mismatch as printed and a non-defining registry number. Published theoretical and observed analytical numbers retain their source conventions; no ion assignment is inferred.
What the studies reported
No verified findings are published for this record under Content Policy v1.
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Verified bibliography
Cited studies by type
The 3 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
Bicelle composition-dependent modulation of phospholipid dynamics by apelin peptides (1).Sarker M, Speckert M, Rainey JK
Biochemistry and cell biology = Biochimie et biologie cellulaire · 2018-08-09 · Journal Article
currentReference 2
Apelin-13 analogues show potent in vitro and in vivo insulinotropic and glucose lowering actions.O'Harte FPM, Parthsarathy V, Hogg C, Flatt PR
Peptides · 2018-02 · Journal Article
currentReference 3
The G protein-coupled receptor ligand apelin-13 ameliorates skeletal muscle atrophy induced by chronic kidney disease.Enoki Y, Nagai T, Hamamura Y, Osa S, Nakamura H, Taguchi K, Watanabe H, Maruyama T, Matsumoto K
Journal of cachexia, sarcopenia and muscle · 2022-12-23 · 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 |
|---|---|
| Sarker M et al. 2018 | Chemical, structural or analytical study; no biological model reported |
| O'Harte FPM et al. 2018 | Study models reported: in vitro; animal (mouse) · from the abstract |
| Enoki Y et al. 2022 | Study models reported: in vitro; animal (mouse) · from the abstract |
Record history
Published 2026-10-21.
No changes to this record's content have been recorded since publication.
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. Apelin-13 (unmodified). Published 2026-10-21. https://purelypeptides.org/research/compounds/apelin-13/
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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.
Read the full methodology →