VIP hormone copy: relaxes blood vessels, calms inflammation (research peptide, code CHEMBL3102922)
A lab-made version of a natural body hormone (called VIP) that widens blood vessels, helps control insulin, and quiets inflammation. Used only as a research tool, not a medicine.
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.
What this is
This is a 30-amino-acid analog of vasoactive intestinal peptide (VIP), a hormone made by nerves and gut cells that relaxes blood vessels and smooth muscle, helps regulate insulin release, and acts as an anti-inflammatory signal in the immune system. The molecule is catalogued in the ChEMBL bioactivity database under identifier CHEMBL3102922 and was reported by Giordanetto and colleagues (ACS Medicinal Chemistry Letters, 2013) as part of a series of VIP derivatives designed to be more drug-like than the natural 28-residue peptide. It is a research compound — not a marketed drug — used to study how VIP-family receptors respond to engineered changes in the peptide backbone.
What it does
Native VIP binds two closely related class B G-protein-coupled receptors, VPAC1 and VPAC2. Both receptors couple to Gαs and raise intracellular cAMP when activated (Couvineau and colleagues, Frontiers in Endocrinology, 2012). Through this signaling, VIP causes vasodilation, smooth-muscle relaxation in the gut and airway, glucose-dependent insulin secretion from pancreatic β-cells, and a shift of T-cell populations toward anti-inflammatory phenotypes. This analog was characterized as a cAMP-stimulating agonist in cells expressing a human VIP-family receptor (Giordanetto and colleagues, 2013); the same family of designed analogs in that study showed sub-nanomolar potency in glucose-dependent insulin-secretion assays in MIN6 β-cells.
Mechanism
The stored sequence HSDAVFTDNYTRLRKQIAVKEYLNKILNGK is a 30-mer derived from native human VIP (HSDAVFTDNYTRLRKQMAVKKYLNSILN, 28 aa) with three internal substitutions (M17→I, K20→E, S25→K) and a C-terminal Gly-Lys (GK) extension. Giordanetto and colleagues (2013) used the I17-VIP-GK template as a reference scaffold for their series; the I17 substitution and GK tag improve handling and assay behavior versus the native sequence, and the K20/S25 positions correspond to the i, i+4 register exploited in their lactamized and olefin-stapled analogs to stabilize the receptor-bound α-helix. The 30-residue analog therefore captures the helical pharmacophore that engages the receptor extracellular domain and transmembrane bundle of class B GPCRs as described for VPAC1 (Couvineau and colleagues, 2012), with side-chain changes intended to bias secondary structure toward the active conformation.
Evidence
- In vitro: ChEMBL bioassay record CHEMBL3102922 reports EC50 = 0.21 nM for cAMP accumulation in CHO Flp-in cells expressing a human VIP-family receptor, measured by TR-FRET, with the source publication being Giordanetto and colleagues (ACS Medicinal Chemistry Letters, 2013). That paper situates this compound within a series whose lead stapled and lactamized analogs showed improved helical content, protease stability, and insulinotropic potency relative to native VIP in MIN6 β-cell assays.
- Animal: No in vivo studies of this specific 30-mer are present in the dossier sources.
- Human: No human studies.
Regulatory status
This is a research-grade compound. It has no FDA or EMA approval and no marketing authorization in any jurisdiction. It is not a controlled substance.
Related peptides
- VIP itself and other VIP-family analogs share the same receptors (VPAC1 and VPAC2) and the same general mechanism of cAMP elevation. Related research analogs from the same medicinal-chemistry program target VPAC2 for glucose-dependent insulin secretion (Giordanetto and colleagues, 2013).
- PACAP (pituitary adenylate cyclase-activating peptide) is the other endogenous high-affinity ligand for VPAC1 and VPAC2 (Couvineau and colleagues, 2012).
▸full evidence table1 metrics
| metric | value | tool |
|---|---|---|
| EC50 | 0.21 nM | GPCRDB/ChEMBL |
▸structural qualityopenfold3
| metric | value | note |
|---|---|---|
| gpde | 0.807 | global PDE — lower = better |
| disorder | 0.189 | fraction disordered |
| chain pair ipTM (A, B) | 0.840 | 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 | 409s |
| predicted by | mlx@peptide |
| predicted at | 2026-04-24 |
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{pep10477,
sequence = {HSDAVFTDNYTRLRKQIAVKEYLNKILNGK},
target = {vpac1},
author = {peptidemodel},
year = {2026},
status = {bioassayed}
}