Krtap5-2 antibacterial peptide
A lab-made peptide that kills bacteria; used only as a 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.
Does the peptide need to fold into a specific structure before it can fight infection?
If true, it would mean the peptide naturally spares human cells (which would quickly unfold it) while staying active in the oxidized environment outside bacteria. That built-in safety switch could make it easier and safer to use than older antibiotic compounds.
Could we chop most of this peptide away and still get the full antibacterial effect?
If the shorter version holds up, manufacturing costs could drop by roughly two-thirds. Lower cost is one of the main reasons promising antibiotic peptides never make it to patients, so this could meaningfully shorten the path from lab to clinic.
Could this peptide be safe for human tissue while still being lethal to bacteria?
Most experimental antibiotic peptides are too toxic for the bloodstream because they punch holes in any cell they touch. If this one works by a different route that leaves human membranes alone, it might survive the safety hurdles that have blocked earlier antibiotic peptides from reaching patients.
What if this peptide works like a zinc magnet that disarms bacteria rather than tearing them apart?
Bacteria evolve resistance to drugs by changing their outer membrane, but they cannot easily evolve around losing zinc from their core machinery. If this mechanism holds, the peptide could stay effective longer than conventional antibiotics, and might even work on dormant bacteria that are notoriously hard to kill.
Could a single compound kill a dangerous bacterium and also block the enzyme that destroys surrounding tissue?
Vibrio vulnificus causes rapidly fatal wound infections, often progressing to limb loss or death within 48 hours. If this peptide can simultaneously eliminate the bacteria and neutralize the enzyme that destroys tissue, it could address both the infection and the spreading damage in a way no single current drug does.
▸full evidence table1 metrics
| metric | value | tool |
|---|---|---|
| ranking score | 0.6074571013450623 | 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{pep05600,
sequence = {CWSCMGHSCWSCMGHSCWSCAGHSCWSCMGHSCWSCMGHSCWSCAGHCCGSCWHGGM},
target = {antimicrobial},
author = {peptidemodel},
year = {2026},
status = {bioassayed}
}