Nisin antimicrobial peptide
A naturally occurring peptide that kills or slows 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.
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 tweaking one flexible hinge in a natural antibiotic shift how it kills bacteria, and could that make resistance harder to develop?
Many bacteria become resistant to antibiotics by fortifying their membranes. If this variant kills mainly by blocking a building block bacteria need to survive (rather than tearing open their membrane), those membrane-based defenses might not work against it, potentially giving doctors a longer-lasting tool against hard-to-treat infections.
Could a modified version of a food-safe antibiotic be applied to implant surfaces to prevent the stubborn bacterial films that cause so many device-related infections?
Infections on implanted devices like pins and catheters are notoriously hard to treat and often require removing the device entirely. If this variant can kill those bacteria at doses safe for skin cells, it could become a surface coating that protects patients without needing systemic antibiotics, which would be a meaningful option for a problem that currently has very few good solutions.
Does the precise arrangement of certain amino acids in one region of this antibiotic control the three-dimensional shape that lets it latch onto and disable bacteria?
If researchers can pinpoint which specific positions in this region are critical for the antibiotic to fold into the right shape, it could make designing new and improved antibiotics much faster and cheaper, reducing the need for expensive trial-and-error lab work. This kind of map would be a practical tool for anyone working on next-generation antimicrobials.
▸full evidence table1 metrics
| metric | value | tool |
|---|---|---|
| ranking score | 0.3809323310852051 | 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{pep05573,
sequence = {MSTKDFNLDLVSVSKKDSGASPRITSISLCTPGCKTGALMGCAAATATCHCSIHVSK},
target = {antimicrobial},
author = {peptidemodel},
year = {2026},
status = {bioassayed}
}