Cathelicidin antimicrobial peptide
A naturally occurring germ-killing peptide that kills bacteria or stops them from growing; 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 the acidic FLAG tag attached to this peptide's tail cut its germ-killing power compared with the tag-free version?
If true, removing the tag could uncover a much more potent antibiotic peptide, giving researchers a stronger starting point for drug development. Patients with drug-resistant infections could eventually benefit from leads that were being artificially weakened.
Does the charge-lowering tag on this peptide make it better at killing Gram-positive bacteria while sparing Gram-negative ones?
A peptide with built-in Gram-selectivity could be useful for treating infections where you want to spare beneficial gut bacteria while targeting pathogens. This would matter for patients on long-term antibiotic therapy.
Can this peptide's built-in tag be used to attach it to medical device surfaces in an orientation that keeps it active against bacteria?
If this works, catheters, implants, and surgical tools coated with this peptide could resist bacterial colonization without releasing antibiotics into the bloodstream. This could reduce healthcare-associated infections for thousands of patients annually.
Is this peptide less likely to burst human red blood cells than standard cathelicidin peptides, because of its acidic tail?
If this peptide is safer for human cells while still killing bacteria, it could be developed into a systemic antibiotic drug. Patients with bloodstream infections could benefit from a new class of treatment that avoids the toxicity problem that has blocked most AMP drugs.
▸full evidence table1 metrics
| metric | value | tool |
|---|---|---|
| ranking score | 0.6249057650566101 | 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{pep05687,
sequence = {LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTESDYKDDDDKCQDSERTFY},
target = {antimicrobial},
author = {peptidemodel},
year = {2026},
status = {computed}
}