Ovalbumin blood-pressure peptide
A small protein fragment that blocks ACE, an enzyme that pushes blood pressure up; used only as a lab research tool.
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 a food-derived peptide lower blood pressure without disturbing the other jobs ACE does in the body?
Most ACE-inhibiting drugs hit both active sites of the enzyme, which can interfere with blood cell production. If this peptide turns out to be selective for just the blood-pressure-controlling site, it could offer a cleaner safety profile for people who need long-term hypertension management.
Does the three-dimensional shape of this peptide matter more than its chemical charge for blocking ACE?
If the geometry of the peptide, not just its electric charge, is what makes it effective, drug designers could build shorter or ring-shaped versions that hold the right shape permanently. That could mean stronger blood-pressure-lowering compounds without making the molecule bigger or more complex.
Could this peptide survive digestion well enough, or break into pieces that still lower blood pressure?
If the peptide acts like a prodrug that releases active fragments in the gut, it could be added to everyday foods such as yogurt or protein drinks in its natural form and do its job after digestion. That would make formulation far simpler than engineering pre-digested peptide supplements.
Could this peptide influence two related enzymes at once, shifting the body toward its natural vasodilating hormones?
Standard blood-pressure drugs block ACE1 but leave ACE2 activity unchanged. If this peptide modulates both, it could tilt the renin-angiotensin system toward hormones that relax blood vessels rather than just cutting off the ones that tighten them. That wider action might offer a more balanced cardiovascular effect for people with hypertension.
Would curling this peptide into a closed loop make it stick to its target better and survive longer in the body?
Linear peptides flop around in solution, which costs energy when they bind to a target. Forming a ring could freeze this peptide in the shape it needs to work, potentially boosting potency severalfold and resisting digestive breakdown. If that holds, it could move from a mild food-derived compound to a genuine oral drug candidate for hypertension.
▸full evidence table2 metrics
| metric | value | tool |
|---|---|---|
| ipTM | 0.7840153574943542 | boltz-2 |
| ranking score | 0.8736600279808044 | boltz-2 |
▸structural qualityopenfold3
| metric | value | note |
|---|---|---|
| gpde | 1.051 | global PDE — lower = better |
| disorder | NaN | fraction disordered |
▸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 | none |
| diffusion samples | 1 |
| runtime | — |
| predicted by | mlx@peptide |
| predicted at | 2026-04-24 |
▸citationbibtex
@peptide{pep04561,
sequence = {AFKDEDTEEVPFR},
target = {ace},
author = {peptidemodel},
year = {2026},
status = {computed}
}