Blood-pressure-lowering peptide (FRAHPFL)
A small protein fragment that blocks ACE, the enzyme that raises blood pressure; studied as a potential treatment for high blood pressure, 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.
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.
Could this blood-pressure peptide be mostly inactive until your digestive system chops it into its working form?
If true, the real active ingredient is a shorter fragment produced during digestion, meaning lab tests on the whole peptide understate how well it actually works in a living body. For researchers and formulators, this would mean the right target to study and refine is the digested fragment, not the original sequence.
Does one specific building block in this peptide act like a hinge that holds the active end in the right shape to block a blood-pressure enzyme?
If swapping out that proline consistently wrecks potency, it confirms exactly which part of the peptide to preserve or reinforce when designing stronger versions. That would give peptide engineers a clear and validated starting point rather than trial-and-error modifications.
What if a single peptide from food could block both of the main enzymes that drive high blood pressure, instead of just one?
Drugs that block both enzymes at once tend to lower blood pressure more effectively than single-target drugs, but existing versions carry a serious side-effect risk. If this food-derived peptide turns out to work on both, it could open a safer, oral route to the same dual effect, which would interest both functional food developers and pharmaceutical researchers.
Could a minor structural change make this peptide survive in the bloodstream long enough to actually do something useful?
Food-derived peptides often get destroyed in the blood before they can reach their target, which is why so many promising lab results fail in living systems. If this modification extends survival without hurting potency, it could be the step that bridges a food ingredient lead all the way to a serious drug candidate.
▸full evidence table2 metrics
| metric | value | tool |
|---|---|---|
| ipTM | 0.6481613516807556 | boltz-2 |
| ranking score | 0.8109986186027527 | 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{pep04813,
sequence = {FRAHPFL},
target = {ace},
author = {peptidemodel},
year = {2026},
status = {bioassayed}
}