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Compound monograph

Exenatide

Exenatide is synthetic exendin-4, a 39-residue peptide with an N-terminal histidine and a C-terminal serine amide; the natural peptide was isolated from Heloderma suspectum venom and characterized as a member of the glucagon superfamily. Horváth et al. (PMID 37528104) place the exendins among the gastrointestinal peptides of the glucagon family.

Published: 2026-09-04Last updated: 2026-10-12Literature/identifier verification: 2026-08-23
Also known asExendin-4
GLP-1 receptor peptide analogs

01

Identity & nomenclature

Exenatide is synthetic exendin-4, a 39-residue peptide with an N-terminal histidine and a C-terminal serine amide; the natural peptide was isolated from Heloderma suspectum venom and characterized as a member of the glucagon superfamily. Horváth et al. (PMID 37528104) place the exendins among the gastrointestinal peptides of the glucagon family.

Hudson and Andersen (PMID 15386269) describe exenatide as synthetic exendin-4; Eng et al. (PMID 1313797) isolated exendin-4 from the venom of the lizard Heloderma suspectum. Exendin-3, isolated from Heloderma horridum, differs by two substitutions at positions 2 and 3. Both are members of the glucagon superfamily.

Declared aliases and development codes: Exendin-4.

02

Molecular properties

Molecular formulaC184H282N50O60S
Molecular mass4187 Da
CAS Registry Number141758-74-9
PubChem CID45588096
UNII9P1872D4OL
One-letter sequenceHGEGTFTSDLSKQMEEEAVRLFIEWLKNGGPSSGAPPPS
Three-letter sequenceHis–Gly–Glu–Gly–Thr–Phe–Thr–Ser–Asp–Leu–Ser–Lys–Gln–Met–Glu–Glu–Glu–Ala–Val–Arg–Leu–Phe–Ile–Glu–Trp–Leu–Lys–Asn–Gly–Gly–Pro–Ser–Ser–Gly–Ala–Pro–Pro–Pro–Ser
Terminal groupsFree N-terminus; C-terminal serine amide

Thirty-nine residues, all L, with a free N-terminus and a C-terminal amide on Ser39. The methionine at position 14 is the only sulfur-containing residue and there is no cysteine, which is what the single sulfur atom in the recorded formula corresponds to. Exendin-3 differs at positions 2 and 3 only — Ser2-Asp3 in place of Gly2-Glu3 — so those two positions are the whole of the difference this entry describes. With the Ser39 amide applied, these residues derive the recorded formula and mass, and the automated sequence verifier now checks that on every build rather than leaving it to prose.

03

Structural characteristics

Exenatide is synthetic exendin-4 and shares GLP-1 receptor agonism with the native hormone. Its direct sequence parent is exendin-4, a peptide of non-human origin, not human GLP-1. Shared receptor activity and general architecture do not establish human GLP-1 scaffold ancestry, and no human-GLP-1 substitution table applies to it. The related GLP-1(7-36) amide entry is a native receptor comparator only, not a structural parent. The isolation report describes a 39-amino-acid peptide recovered using a sequencing assay for peptides bearing an amino-terminal histidine. Exendin-4 differs from exendin-3 by two amino acid substitutions, Gly2-Glu3 in place of Ser2-Asp3, and is otherwise identical; the report notes that this difference is sufficient to change the observed bioactivity profile. In dispersed guinea pig pancreatic acini, exendin-4 produced a monophasic increase in cAMP that was progressively inhibited by the antagonist exendin-(9-39) amide, whereas exendin-3 produced a biphasic response and interacted additionally with VIP receptors.

Terminal features: Free N-terminus, C-terminal serine amide.

04

Molecular targets & mechanisms

Glucagon-like peptide-1 receptor

GLP-1R

GLP-1R is a class B G-protein-coupled receptor. The cited structural and pharmacology records characterize semaglutide and retatrutide as peptide agonists at this receptor.

05

Analytical considerations

The single sulfur atom in the molecular formula corresponds to one sulfur-containing residue. The C-terminal amide is part of the declared identity and distinguishes the peptide from a free-acid preparation of the same sequence.

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

  • Heloderma suspectum venom in an amino-acid sequencing assay

    Eng et al. reported isolation of the 39-amino-acid peptide exendin-4 from Heloderma suspectum venom using an amino-acid sequencing assay.

    Reference [1]

  • Dispersed guinea pig pancreatic acini

    Eng et al. reported a monophasic cAMP increase beginning at 100 pM and reaching a plateau at 10 nM for natural and synthetic exendin-4 in dispersed guinea pig pancreatic acini.

    Reference [1]

  • Dispersed guinea pig pancreatic acini

    Eng et al. observed no amylase release or inhibition of radiolabeled vasoactive-intestinal-peptide binding with exendin-4 in dispersed guinea pig pancreatic acini.

    Reference [1]

  • Dispersed guinea pig pancreatic acini

    Eng et al. reported progressive inhibition of the exendin-4-induced cAMP increase by the exendin-receptor antagonist in dispersed guinea pig pancreatic acini.

    Reference [1]

06

Verified bibliography

Cited studies by type

The 7 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

    Isolation and characterization of exendin-4, an exendin-3 analogue, from Heloderma suspectum venom. Further evidence for an exendin receptor on dispersed acini from guinea pig pancreas.

    Eng J, Kleinman WA, Singh L, Singh G, Raufman JP

    The Journal of biological chemistry · 1992-04-15 · Journal Article

    current
    PMID 1313797ExenatideGLP-1R

  2. Reference 2

    Exendin peptides.

    Eng J

    The Mount Sinai journal of medicine, New York · 1992-03 · Journal Article

    current
    PMID 1574068ExenatideGLP-1R

  3. Reference 3

    Pharmacology, physiology, and mechanisms of incretin hormone action.

    Campbell JE, Drucker DJ

    Cell metabolism · 2013-05-16 · Review

    current
    PMID 23684623DOI 10.1016/j.cmet.2013.04.008TirzepatideSemaglutideRetatrutideExenatideLiraglutideGLP-1RGIPR

  4. Reference 4

    Cryo-EM structure of the activated GLP-1 receptor in complex with a G protein.

    Zhang Y, Sun B, Feng D, Hu H, Chu M, Qu Q, Tarrasch JT, Li S, Sun Kobilka T, Kobilka BK, Skiniotis G

    Nature · 2017-05-24 · Journal Article

    current
    PMID 28538729PMC5587415DOI 10.1038/nature22394SemaglutideLiraglutideExenatideTirzepatideRetatrutideGLP-1R

  5. Reference 5

    Structural basis for ligand recognition of incretin receptors.

    Underwood CR, Parthier C, Reedtz-Runge S

    Vitamins and hormones · 2010 · Review

    current
    PMID 21094903DOI 10.1016/B978-0-12-381517-0.00009-6SemaglutideLiraglutideExenatideTirzepatideRetatrutideGLP-1RGIPR

  6. Reference 6

    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
    PMID 37528104PMC10394066DOI 10.1038/s41467-023-40294-xGIP(1-42)GlucagonGLP-1(7-36) amideGLP-1(7-37)Human GLP-2(1-33)Exenatide

  7. Reference 7

    Exenatide: NMR/CD evaluation of the medium dependence of conformation and aggregation state.

    Hudson FM, Andersen NH

    Biopolymers · 2004 · Journal Article

    current
    PMID 15386269DOI 10.1002/bip.20126Exenatide

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
Eng J et al. 1992Study models reported: in vitro · from the abstract
Eng J 1992Study type not determinable from the abstract
Campbell JE et al. 2013Review article
Zhang Y et al. 2017Study models reported: in vitro · from the abstract
Underwood CR et al. 2010Review article
Horváth D et al. 2023Chemical, structural or analytical study; no biological model reported
Hudson FM et al. 2004Chemical, structural or analytical study; no biological model reported

Record history

Published 2026-09-04.

  • : Identity and nomenclature, References
  • : Sequence and structure
  • : Sequence and structure
  • : 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. Exenatide. Published 2026-09-04; updated 2026-10-12. https://purelypeptides.org/research/compounds/exenatide/

10

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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