Blood-pressure-lowering peptide (FFGVRCVSP)
A small protein fragment that blocks ACE, the enzyme that raises blood pressure, helping to lower it; studied as an experimental compound, 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.
Literature-extracted sequence peptide — synthesized for bioassay as documented in linked reference(s)
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Activity measured in linked reference(s) — IC50/MIC/cytotoxicity data
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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.
Can a food-derived peptide block the part of a key blood pressure enzyme that matters, while leaving the part that causes coughing and swelling alone?
Many people stop taking ACE-inhibitor blood pressure drugs because of a nagging dry cough or dangerous facial swelling. If this peptide selectively hits only the enzyme domain that controls blood pressure and spares the one that triggers those reactions, it could offer a gentler, food-derived alternative for people who cannot tolerate standard ACE inhibitors.
If this peptide pairs up with itself when exposed to oxygen, does it lose its ability to lower blood pressure?
Peptides with a free sulfur group can spontaneously link into pairs when stored or when passing through the body, potentially becoming inactive. If that turns out to be the case here, developers would need to either protect the peptide chemically or reformulate it, which is a solvable engineering problem, but one that must be confirmed before any serious development can proceed.
Could a single food-derived peptide do what currently requires a combination of drugs to achieve?
Blocking two different enzymes that regulate blood vessel tone and fluid balance tends to lower blood pressure more effectively than blocking just one. If this peptide turns out to inhibit both targets, it could replicate the effect of a modern drug combination from a single natural molecule, which would be notable for both nutraceutical and pharmaceutical applications.
Could this peptide bind to a blood pressure enzyme the same way the prescription drug captopril does, producing a longer, stronger effect?
Most food peptides bind briefly and weakly to their targets. If this one uses its sulfur-containing building block to anchor directly to the zinc atom at the enzyme's active site, the way the drug captopril does, it could produce a slower, more sustained blood pressure reduction. That would be an unusual and valuable property for a peptide found in food.
If you flip one amino acid in the peptide to its mirror-image form, could the body stop digesting it so fast without losing its blood pressure effect?
Peptides are typically broken down within minutes in the bloodstream, which limits their usefulness as medicines. A targeted substitution at the vulnerable point in this peptide could, if the hypothesis holds, significantly extend how long it stays active in the body, moving it one step closer to being a practical drug candidate without redesigning the whole molecule.
Could this peptide make it through the digestive system intact enough to actually lower blood pressure when swallowed?
Most blood pressure peptides are destroyed in the gut before they can act. If the structural features of this particular peptide provide even partial protection from digestive enzymes, it could potentially be delivered as a food ingredient or dietary supplement rather than an injectable drug, which would make it far easier and cheaper for people to use.
▸full evidence table2 metrics
| metric | value | tool |
|---|---|---|
| ipTM | 0.5312891602516174 | boltz-2 |
| ranking score | 0.7867939472198486 | boltz-2 |
▸3-letter notation
▸recipeboltz-2 1.0
| parameter | value |
|---|---|
| model | boltz-2 1.0 |
| weights | — |
| hardware | nvidia_nim_api |
| mlx version | — |
| python | — |
| random seed | — |
| msa strategy | colabfold_nvidia |
| diffusion samples | 1 |
| runtime | — |
| predicted by | mlx@peptide |
| predicted at | 2026-04-25 |
▸citationbibtex
@peptide{pep04668,
sequence = {FFGVRCVSP},
target = {ace},
author = {peptidemodel},
year = {2026},
status = {bioassayed}
}