pe
pep-10572 v1 CC-BY-SA-4.0

Glucagon-like peptide 2 (GLP-2): gut-lining repair hormone

A natural gut hormone released after meals that protects and repairs the intestinal lining, helping the gut absorb nutrients; studied as a drug for intestinal diseases, not a standalone approved drug.

statussynthesized targetGCGR length35 aa refs2
status 4 / 5
prediction metrics openfold3-mlx 0.3.1
ipTM0.743
pTM0.706
avg pLDDT53.7
ranking score0.814
STRUCTURE · PEP-10572 × GCGR
ranking0.814
target interface 4.5Å peptide drag rotate · ctrl+scroll zoom · right-click pan
openfold3-mlx 0.3.1 · mmCIF ↓ download
sequence35 aa
15101520253035
HADGSFS DEMNTIL DNLATRD FINWLIQ TKITDRK
in the news 16 articles
overview readme

What this is

Glucagon-like peptide-2 (GLP-2) is a gut hormone released after meals from L-cells lining the lower small intestine and colon. Its main job is to protect and grow the intestinal lining — it promotes the repair and expansion of the mucosa that absorbs nutrients, making it distinct from GLP-1, which controls blood sugar and appetite. GLP-2 is encoded by the same proglucagon gene that also produces glucagon and GLP-1; the three hormones arise from tissue-specific processing of the same precursor protein. The sequence stored here corresponds to a 35-residue proglucagon-derived GLP-2 variant of rat (Rattus norvegicus) origin; the canonical human GLP-2 sequence is 33 residues and differs at several positions, including position 19 (threonine in rat, alanine in human). Because native GLP-2 is degraded within minutes by the enzyme DPP-4, it is impractical as a drug itself — a DPP-4-resistant analog, teduglutide (/card/pep-04435), was developed from this scaffold and is FDA-approved for short bowel syndrome.

History

GLP-2 was first identified in the early 1980s as part of the structural characterization of the proglucagon gene. Seino and colleagues (FEBS Letters, 1986) showed that mutations in the guinea pig preproglucagon gene are restricted to a specific portion of the prohormone sequence, advancing understanding of the evolutionary conservation of these proglucagon-derived peptides. The intestinotrophic activity of GLP-2 — its ability to stimulate growth of the intestinal mucosa — was characterized in rodent models during the 1990s by Daniel Drucker and colleagues at the University of Toronto, who demonstrated that GLP-2 administration enhanced small bowel structure and function, improved nutrient absorption, and could reverse intestinal atrophy caused by total parenteral nutrition. These findings established GLP-2 as a potentially therapeutic target for intestinal insufficiency conditions, motivating the development of teduglutide.

What it does

GLP-2 acts on GLP-2 receptors located on subepithelial myofibroblasts, enteric neurons, and enteroendocrine cells in the intestinal wall. Activation of these receptors triggers the release of growth factors including keratinocyte growth factor (KGF), insulin-like growth factor-1 (IGF-1), and epidermal growth factor (EGF), which in turn drive crypt cell proliferation, inhibit enterocyte apoptosis, and increase villus height. The net result is a larger absorptive surface area and improved capacity for nutrient uptake. GLP-2 also increases mesenteric blood flow, inhibits gastric acid secretion, slows gastric emptying, and — perhaps counterintuitively — stimulates glucagon secretion from the pancreas. In the liver and adipose tissue, GLP-2 has been shown to enhance lipid absorption from the gut. These combined effects make GLP-2 a regulator of both intestinal architecture and postprandial nutrient partitioning.

Evidence

  • Human: Native GLP-2 has been studied in humans as an infused peptide in controlled research settings, demonstrating inhibition of gastric emptying, enhancement of lipid absorption, and stimulation of glucagon secretion. The clinical therapeutic evidence base belongs largely to teduglutide, the DPP-4-resistant analog, which completed pivotal Phase III trials (STEPS, STEPS-2, STEPS-3) for short bowel syndrome. No clinical trials of native GLP-2 for therapeutic use have been identified.
  • Animal: Extensive. GLP-2 administration in rodents on total parenteral nutrition restores small bowel structure and function, increases villus height and crypt depth, enhances absorptive capacity, and prevents intestinal atrophy. GLP-2 has also been shown to reduce mucosal injury in animal models of radiation enteritis and inflammatory bowel conditions.
  • In vitro: GLP-2 receptors have been characterized on intestinal subepithelial myofibroblasts, enteric neurons of the myenteric and submucosal plexus, and enteroendocrine cells; receptor activation induces downstream KGF and IGF-1 signaling that drives epithelial proliferation and survival.

Mechanism

GLP-2 is a member of the glucagon-secretin superfamily (also called the pituitary adenylate cyclase-activating peptide/glucagon hormone superfamily), a class of structurally related hormones that act through class B G protein-coupled receptors. Yang and colleagues (Journal of Biological Chemistry, 2016) characterized the structural determinants by which GLP-1 — a closely related proglucagon-derived peptide — binds the seven-transmembrane domain of its class B GPCR, work that illuminates how small sequence differences among glucagon-family peptides translate into distinct receptor selectivity. GLP-2 itself binds the GLP-2 receptor (GLP-2R), a distinct class B GPCR expressed primarily in the gastrointestinal tract, where its activation couples to Gαs/adenylyl cyclase signaling, increasing intracellular cAMP and activating downstream growth-factor cascades.

The short half-life of native GLP-2 results from DPP-4 cleavage at the bond after the second residue (Ala²), which removes the first two amino acids and destroys biological activity. This rapid degradation is the structural vulnerability that motivated the development of teduglutide, in which Ala² is substituted with glycine to confer DPP-4 resistance and substantially extend the circulating half-life.

Known effects

  • Intestinal mucosal growth — Preclinical (extensive rodent data); mechanistic in humans
  • Inhibition of gastric acid secretion — Human research studies
  • Enhancement of lipid absorption — Human research studies
  • Glucagon secretion stimulation — Human research studies
  • Inhibition of gastric emptying — Human research studies
  • Restoration of intestinal structure in short bowel syndrome — Phase III (teduglutide analog; no approved indication for native GLP-2)

Regulatory status

  • US: Native GLP-2 has no approved therapeutic indication. The approved clinical application of this peptide class belongs to teduglutide (Gattex), the DPP-4-resistant GLP-2 analog, which received FDA approval for short bowel syndrome in adults (December 2012) and children (2019).
  • EU/International: Teduglutide is approved as Revestive by EMA and in multiple other jurisdictions for short bowel syndrome. Native GLP-2 itself has no approved indication.
  • Research use: The rat-origin 35-residue sequence stored in this card (HADGSFSDEMNTILDNLATRDFINWLIQTKITDRK) is used in preclinical research; it is not a pharmaceutical entity.

Related peptides

  • Teduglutide — DPP-4-resistant GLP-2 analog with Ala²→Gly substitution; FDA-approved for short bowel syndrome as Gattex/Revestive; the clinical translation of the GLP-2 scaffold.
  • Glucagon-like peptide-2 (1–33), human — The canonical 33-residue human GLP-2 sequence; differs from the rat variant stored here at multiple positions.
  • Glucagon — The 29-residue counter-regulatory hormone encoded by the same proglucagon precursor gene; acts on GCGR rather than GLP-2R.
details expand to inspect
full evidence table2 metrics
metricvaluetool
ipTM 0.7426857352256775 openfold3-mlx
ranking score 0.8144311904907227 openfold3-mlx
structural qualityopenfold3
0
metricvaluenote
gpde0.781global PDE — lower = better
disorder0.158fraction disordered
chain pair ipTM (A, B)0.743interface quality
3-letter notation
His-Ala-Asp-Gly-Ser-Phe-Ser-Asp-Glu-Met-Asn-Thr-Ile-Leu-Asp-Asn-Leu-Ala-Thr-Arg-Asp-Phe-Ile-Asn-Trp-Leu-Ile-Gln-Thr-Lys-Ile-Thr-Asp-Arg-Lys
recipeopenfold3-mlx 0.3.1
parametervalue
modelopenfold3-mlx 0.3.1
weightsaedd8f3eb814e392…
hardwareapple_m4_base_16gb
mlx version0.31.1
python3.14.3
random seed42
msa strategycolabfold
diffusion samples1
runtime455s
predicted bymlx@peptide
predicted at2026-04-23
python3 openfold3/run_openfold.py predict --query_json {query.json} --runner_yaml examples/example_runner_yamls/mlx_runner.yml --output_dir {output_dir} --num_diffusion_samples 1
citationbibtex
peptidemodel (2026). Glucagon-like peptide 2 (GLP-2): gut-lining repair hormone (pep-10572, v1). PeptideModel. https://peptidemodel.com/card/pep-10572
@peptide{pep10572,
  sequence = {HADGSFSDEMNTILDNLATRDFINWLIQTKITDRK},
  target   = {gcgr},
  author   = {peptidemodel},
  year     = {2026},
  status   = {synthesized}
}
related peptides 5 by signal overlap
clinical trials 3157 on ct.gov · 33 on EUCTR · checked 2026-05-09
ct.gov trials 3157
with results 679
EUCTR 33
PubMed RCT 27
by phase
1phase 11phase 23phase 45no phase
by status
3completed3recruiting1terminated1withdrawn2unknown
references 2 papers
discussion no comments
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peptidemodel.com CC-BY-SA-4.0 research only · not for human use