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Compound monograph

GLP-1(7-37)

GLP-1(7-37) is an endogenous processing form of glucagon-like peptide-1 retaining a C-terminal glycine, and the structural reference for several acylated GLP-1 analogs. Mojsov et al. (PMID 3543057) describe the glucagon-like peptides as liberated from proglucagon in both the pancreas and the intestine. Horváth et al. (PMID 37528104) place GLP-1 among the gastrointestinal peptides of the glucagon family.

Published: 2026-09-14Last updated: 2026-10-14Literature/identifier verification: 2026-09-14
Also known asGLP-1 7-37GLP-I(7-37)Insulinotropin

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Identity & nomenclature

GLP-1(7-37) is an endogenous processing form of glucagon-like peptide-1 retaining a C-terminal glycine, and the structural reference for several acylated GLP-1 analogs. Mojsov et al. (PMID 3543057) describe the glucagon-like peptides as liberated from proglucagon in both the pancreas and the intestine. Horváth et al. (PMID 37528104) place GLP-1 among the gastrointestinal peptides of the glucagon family.

This is the reference scaffold for the acylated GLP-1 analogs in this library, because they retain the C-terminal glycine. 'Both are GLP-1 analogs' is not sufficient for this corpus: which native form an analog is built on determines whether its modification table is right. GSRS UNII PI470C66NT and primary CAS 106612-94-6 describe the free 31-residue peptide represented by PubChem CID 16133830, although the GSRS CID cross-reference points to acetate CID 91820613. Mojsov et al. (PMID 3543057) named this glycine-extended form Insulinotropin; the name does not denote the amidated GLP-1(7-36) form.

Canonical name: Glucagon-like peptide-1 (7-37).

Declared aliases and development codes: GLP-1 7-37, GLP-I(7-37), Insulinotropin.

02

Molecular properties

Molecular formulaC151H228N40O47
Molecular mass3355.7 Da
CAS Registry Number106612-94-6
PubChem CID16133830
UNIIPI470C66NT
One-letter sequenceHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRG
Terminal groupsFree N-terminus; Free C-terminal carboxyl

Thirty-one residues ending in glycine with a FREE C-terminal carboxyl. Distinct from both the amidated 30-residue form and from GLP-1(1-37). Conventional 7-37 numbering retained: Ala8 is the second residue of the mature peptide, Lys26 the twentieth, Lys34 the twenty-eighth. Mixing numbering systems silently produces incorrect modification records for every analog derived from this scaffold.

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Structural characteristics

Work in the isolated perfused rat pancreas established this form as a potent stimulator of insulin secretion at concentrations as low as 5 x 10^-11 M, while the N-terminally extended GLP-1(1-37) had no effect at concentrations four orders of magnitude higher. That contrast is what makes the processing-form distinction a real identity question rather than a matter of notation. A separate human comparison of this form against the amidated form found them equipotent and concluded that C-terminal amidation is important for neither metabolism nor pancreatic effect — so this library records two distinct molecules on chemical grounds while reporting that the source examining them found no functional difference.

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

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Molecular targets & mechanisms

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Analytical considerations

Terminal glycine, terminal carboxyl state and N-terminal processing state must each be independently visible. An ambiguous GLP-1 identity cannot be resolved by matching only the internal sequence segment shared by both active forms, since that segment is identical.

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

  • Isolated perfused rat pancreas

    Mojsov et al. reported 3- to 10-fold increases over basal insulin secretion with GLP-I(7-37) at concentrations as low as 5 x 10^-11 M in isolated perfused rat pancreas with 6.6 mM glucose.

    Reference [1]

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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.

  1. Reference 1

    current
  2. Reference 2

  3. Reference 3

    Polymorphic amyloid nanostructures of hormone peptides involved in glucose homeostasis display reversible amyloid formation.

    Horváth D, Dürvanger Z, K Menyhárd D, Sulyok-Eiler M, Bencs F, Gyulai G, Horváth P, Taricska N, Perczel A

    Nature communications · 2023-08-01 · 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.

ReferenceStudy models
Mojsov S et al. 1987Study models reported: in vitro · from the abstract
Orskov C et al. 1993Study type not determinable from the abstract
Horváth D et al. 2023Chemical, structural or analytical study; no biological model reported

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Record history

Published 2026-09-14.

  • : Sequence and structure
  • : Identity and nomenclature
  • : 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. GLP-1(7-37). Published 2026-09-14; updated 2026-10-14. https://purelypeptides.org/research/compounds/glp-1-7-37/

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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.

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