Gut-healing experimental peptide (CHEMBL3824179)
A lab-made peptide that switches on a gut-repair signal, studied for its potential to heal and strengthen the intestinal lining; experimental, not yet an approved drug.
A researcher, an agent, or an algorithm wrote down the sequence and picked a target to hit.
An AI model like OpenFold3 or AlphaFold built a 3D structure and scored how well it fits the binding site.
A second contributor repeated the computation on their own hardware and the scores matched.
A chemistry service or a researcher ordered the sequence, it was manufactured, and mass spectrometry confirmed the right molecule was produced.
A binding or activity measurement confirmed that it actually does what the computer predicted — or didn't.
Research directions for this peptide, selected from the current sources — hypotheses you can explore and model. None of it is proven yet; tap any one to see the full thinking.
Could chemically pinning this peptide into a helical shape make it stable enough for once-daily dosing?
Native GLP-2 breaks down within minutes in the bloodstream. A stabilised version could become a practical once-daily pill or injection for patients with intestinal failure, dramatically improving quality of life.
Does this peptide grip the GLP-2 receptor at a different spot than the body's own GLP-2 signal?
If true, it could produce a gut-healing effect with a safer side-effect profile than current GLP-2 drugs, which is relevant for patients recovering from intestinal surgery or living with short bowel syndrome.
Could this peptide stimulate intestinal tissue growth without causing the fluid loss that full GLP-2 receptor activation can produce?
If true, patients with short bowel syndrome or chemotherapy-damaged intestines could benefit from a safer version of gut-repair therapy, one that builds tissue without causing problematic fluid shifts.
Does this peptide only take on a defined shape when it docks onto GLP-2R, rather than having a fixed structure in the bloodstream?
Peptides that fold on demand tend to bind their target more selectively, potentially reducing unwanted side-effects, which matters for any future drug built on this scaffold.
Is only the back half of this peptide doing the real work of binding to GLP-2R?
If a shorter version binds just as well, it would be cheaper to manufacture and more stable in the body, bringing a potential gut-healing drug closer to clinical use.
▸full evidence table1 metrics
| metric | value | tool |
|---|---|---|
| EC50 | 0.22 nM | GPCRDB/ChEMBL |
▸structural qualityopenfold3
| metric | value | note |
|---|---|---|
| gpde | 0.746 | global PDE — lower = better |
| disorder | 0.223 | fraction disordered |
| chain pair ipTM (A, B) | 0.875 | interface quality |
▸3-letter notation
▸recipeopenfold3-mlx 0.3.1
| parameter | value |
|---|---|
| model | openfold3-mlx 0.3.1 |
| weights | aedd8f3eb814e392… |
| hardware | apple_m4_base_16gb |
| mlx version | 0.31.1 |
| python | 3.14.3 |
| random seed | 42 |
| msa strategy | colabfold |
| diffusion samples | 1 |
| runtime | 647s |
| predicted by | mlx@peptide |
| predicted at | 2026-04-22 |
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
@peptide{pep10371,
sequence = {HGDGSFSDEMNTILDNLAARDFINWLIQTK},
target = {glp-2r},
author = {peptidemodel},
year = {2026},
status = {bioassayed}
}