Compound monograph
GLP-1(7-36) amide
GLP-1(7-36) amide is an endogenous processing form of glucagon-like peptide-1 and the native ligand against which the GLP-1 receptor agonists in this library are compared. Deacon et al. (PMID 7556682) isolated this form from human colon and conclude that it is a product of proglucagon processing. Horváth et al. (PMID 37528104) place GLP-1 among the gastrointestinal peptides of the glucagon family.
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Identity & nomenclature
GLP-1(7-36) amide is an endogenous processing form of glucagon-like peptide-1 and the native ligand against which the GLP-1 receptor agonists in this library are compared. Deacon et al. (PMID 7556682) isolated this form from human colon and conclude that it is a product of proglucagon processing. Horváth et al. (PMID 37528104) place GLP-1 among the gastrointestinal peptides of the glucagon family.
'GLP-1(7-36)' without an amidation designation is not sufficiently specified. This entry is the AMIDATED form; GLP-1(7-37) is a separate molecule with an additional terminal glycine and a free carboxyl, recorded separately in this library. Amidation is not a counterion difference. GLP-1(1-37) is the N-terminally extended proform and is not this hormone; describing it as an inactive precursor is appropriate only in the sense that it is not the conventional mature insulinotropic form. The name Insulinotropin belongs to GLP-1(7-37) and is recorded on that entry; it is not an alias of this amidated form.
Canonical name: Glucagon-like peptide-1 (7-36) amide.
Declared aliases and development codes: GLP-1(7-36)amide, GLP-1 7-36 amide.
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Molecular properties
| Molecular formula | C149H226N40O45 |
|---|---|
| Molecular mass | 3297.7 Da |
| CAS Registry Number | 107444-51-9 |
| PubChem CID | 16133831 |
| UNII | 0JS9125PIZ |
| One-letter sequence | HAEGTFTSDVSSYLEGQAAKEFIAWLVKGR |
| Terminal groups | Free N-terminus; C-terminal amide |
Thirty residues ending in an amidated arginine. The conventional 7-36 numbering is retained rather than renumbering the mature N-terminal histidine as residue 1 — every modification table for every GLP-1 analog in this library uses that convention, and silently renumbering produces wrong records.
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Structural characteristics
Its N-terminal His-Ala is a substrate for dipeptidyl peptidase IV, which removes the dipeptide to give the des-His-Ala product. The enzymology was characterised directly, with kinetics consistent with degradation at nanomolar concentrations, and the released His-Ala identified. Since an intact N-terminus is required for activity in this peptide family, that cleavage is an identity question and not merely sample ageing. It is also the reason essentially every GLP-1-derived analog in this library carries a substitution at position 8.
Terminal features: Free N-terminus, C-terminal amide.
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Molecular targets & mechanisms
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Analytical considerations
The C-terminal modification must be part of the identity record; a generic GLP-1 measurement is not form-specific without demonstrated assay discrimination. Intact peptide must also be distinguished from the DPP-IV product; total GLP-1 immunoreactivity does not establish intact-molecule identity. This entry and GLP-1(7-37) are distinct native processing forms, not aliases — though note that the source comparing them directly found them equipotent, so the distinction recorded here is chemical rather than functional.
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.
Often mixed up · Name or substance
GLP-1(7-36) amide vs GLP-1(7-37)Also noted in GLP-1(7-37)
Often mixed up · Name or substance
"Insulinotropin" names GLP-1(7-37), not the 7-36 amideAlso noted in GLP-1(7-37)
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
Purified human placental dipeptidyl-peptidase IV assay
Mentlein et al. reported hydrolysis of GLP-1(7-36)amide to its des-His-Ala derivative by dipeptidyl-peptidase IV purified from human placenta.
Reference [3]Human serum degradation assay
Mentlein et al. identified des-His-Ala GLP-1(7-36)amide and His-Ala as major products in human serum incubations, and dipeptidyl-peptidase IV inhibitors completely abolished production of these fragments.
Reference [3]Human colon peptide extracts
Deacon et al. identified GLP-1(7-36)amide in extracts from four human colons by amino-acid sequence analysis and mass spectrometry.
Reference [4]
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Verified bibliography
Cited studies by type
The 5 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.
- In vitro3
- Human participants (interventional)1
- Chemical, structural or analytical; no biological model1
- Study type not determined1
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
Glucagon-like peptide-1 7-36: a physiological incretin in man.Kreymann B, Williams G, Ghatei MA, Bloom SR
Lancet (London, England) · 1987-12-05 · Journal Article
currentReference 2
Biological effects and metabolic rates of glucagonlike peptide-1 7-36 amide and glucagonlike peptide-1 7-37 in healthy subjects are indistinguishable.Orskov C, Wettergren A, Holst JJ
Diabetes · 1993-05 · Journal Article
currentReference 3
Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum.Mentlein R, Gallwitz B, Schmidt WE
European journal of biochemistry · 1993-06-15 · Journal Article
currentReference 4
Human colon produces fully processed glucagon-like peptide-1 (7-36) amide.Deacon CF, Johnsen AH, Holst JJ
FEBS letters · 1995-09-25 · Journal Article
currentReference 5
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.
| Reference | Study models |
|---|---|
| Kreymann B et al. 1987 | Study models reported: in vitro; human participants (interventional) · from the abstract |
| Orskov C et al. 1993 | Study type not determinable from the abstract |
| Mentlein R et al. 1993 | Study models reported: in vitro · from the abstract |
| Deacon CF et al. 1995 | Study models reported: in vitro · from the abstract |
| Horváth D et al. 2023 | Chemical, structural or analytical study; no biological model reported |
Compare
Record history
Published 2026-09-14.
- : Sequence and structure
- : 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(7-36) amide. Published 2026-09-14; updated 2026-10-14. https://purelypeptides.org/research/compounds/glp-1-7-36-amide/
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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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