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Compound monograph

Oxyntomodulin

Oxyntomodulin is an endogenous proglucagon-derived peptide containing the complete glucagon sequence plus an eight-residue C-terminal extension, with reported activity at both the GLP-1 and glucagon receptors. A review by Bataille and Dalle (PMID 25115338) describes oxyntomodulin as a member of the glucagon family; that is a review-level family attribution.

Published: 2026-09-14Last updated: 2026-10-14Literature/identifier verification: 2026-09-14
Also known asOXMGlucagon-37

01

Identity & nomenclature

Oxyntomodulin is an endogenous proglucagon-derived peptide containing the complete glucagon sequence plus an eight-residue C-terminal extension, with reported activity at both the GLP-1 and glucagon receptors. A review by Bataille and Dalle (PMID 25115338) describes oxyntomodulin as a member of the glucagon family; that is a review-level family attribution.

Oxyntomodulin is ONE peptide, not a mixture of GLP-1 and glucagon. It is also not glicentin, which is a larger processing product that contains the oxyntomodulin region — and both carry the same KRNRNNIA C-terminus, so recognising that region does not distinguish them. Separately, 'oxyntomodulin-like' is a description of GLP-1R/GCGR pharmacology and does not establish oxyntomodulin-derived chemistry; a compound can have that pharmacology from a different scaffold entirely. PubChem CID 121494088 encodes the human 37-residue free peptide ending KRNRNNIA, whereas CID 16144019 ends KRNKNNIA and contains Lys33 in place of Arg33. Arginine carries two more nitrogens than lysine, which is why that record shows N59 against this entry's N61. Its formula and mass describe a variant and must not be applied to the human sequence.

Declared aliases and development codes: OXM, Glucagon-37.

02

Molecular properties

Molecular formulaC192H295N61O60S
Molecular mass4449.9 Da
PubChem CID121494088
UNIILV7ELH7V16
One-letter sequenceHSQGTFTSDYSKYLDSRRAQDFVQWLMNTKRNRNNIA
Terminal groupsFree N-terminus; Free C-terminal carboxyl

Thirty-seven residues, free at both termini. The first twenty-nine are the complete glucagon sequence; the C-terminal extension is KRNRNNIA. Species and the extension must both be explicit.

03

Structural characteristics

Its dual-receptor character was dissected using a single-residue variant: replacing glutamine with glutamate at position 3 retained comparable potency at the murine GLP-1 receptor while removing significant murine glucagon-receptor agonist activity in vitro and reducing the ability to stimulate glycogenolysis in perfused mouse liver by roughly one hundred-fold. These receptor and liver assays distinguish the GLP-1R and GCGR components of oxyntomodulin signaling. The library cites that work for this receptor dissection specifically. There is no separate established oxyntomodulin receptor to name; the mechanism is the two receptors it shares with other proglucagon-derived peptides.

Terminal features: Free N-terminus, Free C-terminal carboxyl.

04

Molecular targets & mechanisms

05

Analytical considerations

Identity work must discriminate oxyntomodulin from BOTH glucagon and glicentin. An internal glucagon-derived segment cannot identify it uniquely, because glucagon's entire sequence is contained within it. A C-terminal antibody does not solve this either: antisera raised against the KRNRNNIA extension cross-react completely with both oxyntomodulin and glicentin while showing none toward glucagon. Chromatographic or mass-spectrometric separation is therefore the appropriate approach, and a validated LC-MS/MS method distinguishing oxyntomodulin from glucagon exists. GSRS UNII LV7ELH7V16 matches the human sequence but reports C192H291N61O60S, four hydrogens below PubChem CID 121494088 and this record’s formula.

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.

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

  • OXM radioimmunoassay with rabbit antisera

    Blache et al. reported 100% cross-reactivity of C-terminal-directed rabbit antisera with oxyntomodulin and no cross-reactivity with glucagon in a radioimmunoassay.

    Reference [1]
  • Plasma liquid chromatography-tandem mass spectrometry assay

    Becker et al. validated a liquid chromatography-tandem mass spectrometry assay for oxyntomodulin in plasma that was linear from 1.1 to 13.7 pM and had imprecision below 13% CV.

    Reference [2]
  • CHO cells expressing mouse GLP1R or GCGR

    Kosinski et al. measured cAMP EC50 values for oxyntomodulin of 2.5 nmol/L at mouse GLP1R and 6.2 nmol/L at mouse GCGR in Chinese hamster ovary cell assays.

    Reference [3]

Animal studies

  • Diet-induced obese human-GCGR C57BL/6 mouse model

    Kosinski et al. reported body-weight changes of -9.1 plus or minus 1.2 grams with oxyntomodulin and -0.6 plus or minus 0.3 grams with vehicle in diet-induced obese C57BL/6 mice expressing human GCGR (P < 0.05).

    Reference [3]

06

Verified bibliography

Cited studies by type

The 4 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.

  1. Reference 1

    Development of an oxyntomodulin/glicentin C-terminal radioimmunoassay using a "thiol-maleoyl" coupling method for preparing the immunogen.

    Blache P, Kervran A, Martinez J, Bataille D

    Analytical biochemistry · 1988-08-15 · Journal Article

    current
  2. Reference 2

    Quantification of glucagon and oxyntomodulin by protein precipitation-immunoaffinity enrichment-LC-MS/MS.

    Becker JO, Shijo SK, Huynh HH, Forrest KL, MacCoss MJ, Emrick MA, Goonatilleke E, Hoofnagle AN

    Journal of mass spectrometry and advances in the clinical lab · 2025-04-11 · Journal Article

    current
  3. Reference 3

    The glucagon receptor is involved in mediating the body weight-lowering effects of oxyntomodulin.

    Kosinski JR, Hubert J, Carrington PE, Chicchi GG, Mu J, Miller C, Cao J, Bianchi E, Pessi A, Sinharoy R, Marsh DJ, Pocai A

    Obesity (Silver Spring, Md.) · 2012-03-16 · Journal Article

    current
  4. Reference 4

    The forgotten members of the glucagon family.

    Bataille D, Dalle S

    Diabetes research and clinical practice · 2014-07-03 · Review

    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.

ReferenceStudy models
Blache P et al. 1988Study models reported: in vitro · from the abstract
Becker JO et al. 2025Study models reported: in vitro · from the abstract
Kosinski JR et al. 2012Study models reported: in vitro; animal (mouse) · from the full text
Bataille D et al. 2014Review article

Compare

Record history

Published 2026-09-14.

  • : Sequence and structure
  • : Identity and nomenclature, Analytical notes
  • : Identity and nomenclature, 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. Oxyntomodulin. Published 2026-09-14; updated 2026-10-14. https://purelypeptides.org/research/compounds/oxyntomodulin/

10

Methodology & citation verification

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