Enterocin-HF antimicrobial peptide
A naturally occurring antimicrobial peptide that kills or stops the growth of bacteria and other microbes; 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.
Does Enterocin-HF latch onto a particular structure on the bacterial surface, or does it just punch holes at random?
If it turns out to dock on a specific protein gate that common food-borne and hospital pathogens rely on, researchers would know exactly what to optimize for. That could make it far easier to design more potent or selective versions for food preservation or infection control.
Does breaking one molecular link in this peptide turn a bacteria-killing agent into a merely bacteria-slowing one?
If this holds, it could give researchers a way to tune the peptide for the job at hand. A bacteria-slowing version might be safer for use near human tissue, while the intact form would be kept for situations where outright elimination matters.
Could this peptide work against the dangerous drug-resistant bacteria that colonize hospital patients and that current antibiotics often cannot touch?
Vancomycin-resistant Enterococcus is a serious hospital threat with very few treatment options. If this peptide could clear it from the gut at doses the intestine naturally tolerates, it might offer a path to decolonizing high-risk patients without adding to the antibiotic resistance problem.
Could changing just two components of this peptide reduce the risk of harming human cells while leaving it just as deadly to bacteria?
Many natural antimicrobial peptides are too toxic to human cells at useful doses. If this swap works as predicted, it would point toward a cleaner, safer version of the peptide, and would help scientists understand which part of its activity is precise and which part is crude collateral damage.
Would this peptide kill the Listeria that makes people sick while leaving a closely related but harmless species unaffected?
Listeria monocytogenes causes serious foodborne illness, but not all Listeria strains are dangerous. If Enterocin-HF could reliably distinguish between them based on a single protein they do or do not carry, it would serve both as a precise food-safety tool and as confirmation that the peptide works through the expected mechanism.
▸full evidence table1 metrics
| metric | value | tool |
|---|---|---|
| ranking score | 0.4648950695991516 | boltz-2 |
▸3-letter notation
▸recipeboltz-2 2.2.1
| parameter | value |
|---|---|
| model | boltz-2 2.2.1 |
| weights | — |
| hardware | vast_v100_32gb |
| mlx version | — |
| python | — |
| random seed | 1 |
| msa strategy | none_monomer |
| runtime | — |
| predicted by | — |
| predicted at | 2026-05-23 |
▸citationbibtex
@peptide{pep05536,
sequence = {MKKLTSKEMAQVVGGKYYGNGVSCNKKGCSVDWGKAIGIIGNNSAANLATGGAAGWKS},
target = {antimicrobial},
author = {peptidemodel},
year = {2026},
status = {computed}
}