Beta-conglycinin blood-pressure-lowering peptide
A natural peptide that blocks ACE, the enzyme that raises blood pressure, helping to keep blood pressure in check. 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 a shorter version of this soy-derived peptide block the enzyme that raises blood pressure more effectively than the original?
If true, a trimmed version of this peptide could be a more potent, gut-stable ingredient for blood-pressure-lowering foods or supplements. That would matter for the millions of people with mild hypertension who prefer dietary options over daily medication.
Could this peptide lower blood pressure without triggering the facial swelling risk linked to drugs that block two enzymes at once?
A past drug that blocked both enzymes caused dangerous swelling in some patients and was pulled from use. If this peptide naturally avoids that second enzyme, it could be a safer dietary route to blood pressure control, particularly for people who cannot tolerate certain medications.
Is one specific amino acid acting as a structural hinge that holds the peptide in the right shape to do its job?
If this structural hinge is confirmed, researchers could design shorter, cheaper versions of the peptide that keep only the part that actually works. Shorter peptides tend to survive digestion better and are easier to deliver in food products.
Could this peptide zero in on the part of the enzyme that raises blood pressure while leaving a blood-cell-regulating part untouched?
The enzyme it targets has two active regions with different jobs. Blocking only the one responsible for blood pressure, while leaving the other alone, could mean fewer off-target effects compared to standard ACE-inhibitor drugs. If this holds, the peptide would be a notably precise dietary ingredient.
Could the negatively charged end of this peptide be helping it dock in an unusual way that still blocks the blood-pressure enzyme?
Most known dietary blood-pressure peptides are short and oily-ended. This one breaks that pattern, and understanding why it still works could open a new design strategy for peptide ingredients, potentially allowing researchers to tune potency and selectivity in ways not possible with conventional short peptides.
▸full evidence table2 metrics
| metric | value | tool |
|---|---|---|
| ipTM | 0.7388739585876465 | boltz-2 |
| ranking score | 0.8406808972358704 | boltz-2 |
▸structural qualityopenfold3
| metric | value | note |
|---|---|---|
| gpde | 1.173 | 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{pep04633,
sequence = {EDENNPFYLR},
target = {ace},
author = {peptidemodel},
year = {2026},
status = {bioassayed}
}