Palustrin-2CG1 germ-killing peptide
A short protein fragment that kills or slows the growth of bacteria or 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.
Is there a natural peptide that attacks cancer cells but ignores healthy ones because of a built-in charge filter?
Cancer cells have an unusual electrical charge on their outer surface that healthy cells lack. If this hypothesis holds, palustrin-2CG1 could selectively kill melanoma and leukemia cells while leaving normal blood cells untouched, pointing toward a new class of targeted anticancer drugs for people who need treatments with fewer side effects.
Could swapping one amino acid turn a manufacturing headache into a stable, high-yield drug candidate?
Long peptide drugs often tangle and degrade during production, driving up costs and limiting shelf life. If this single substitution works as predicted, it could raise manufacturing yields and extend how long the peptide survives in the body, making it more practical to develop as an actual medicine for patients with drug-resistant infections.
Does this peptide tear bacterial membranes apart like a detergent, or does it poke precise holes, and why does that matter?
The way an antibiotic kills bacteria determines which resistance tricks bacteria can use against it. If palustrin-2CG1 works by smothering the bacterial surface rather than forming fixed channels, resistance would be much harder for bacteria to evolve, and the active region could potentially be shortened into a smaller, cheaper drug for people with resistant infections.
Does this peptide get captured by proteins in the blood before it can do its job?
Many promising antibiotics look great in lab tests but underperform in the body because blood proteins intercept them. If this hypothesis is confirmed, small tweaks to the peptide's charged end could prevent that interception, potentially turning a lab curiosity into a drug that actually works at lower doses in patients with systemic infections.
Could palustrin-2CG1 tackle the stubborn fungal films that form on catheters and implants and resist standard drugs?
Candida biofilms on medical devices cause life-threatening infections in hospital patients, and existing antifungals often fail against them. If this peptide disrupts those biofilms through a different mechanism than current drugs, it could work alongside azole antifungals to treat infections that are currently very difficult to clear, especially in immunocompromised patients.
Can trimming the end of this peptide make it safer without making it weaker against bacteria?
One of the main obstacles to turning antimicrobial peptides into drugs is that they can rupture red blood cells. If removing the C-terminal ring reduces that toxicity while leaving the bacteria-killing activity intact, the result would be a shorter, cheaper peptide with a wider safety margin, making it a more realistic candidate for treating serious bacterial infections in people.
▸full evidence table1 metrics
| metric | value | tool |
|---|---|---|
| ranking score | 0.6093378067016602 | 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{pep05657,
sequence = {GTISSLCEQERDANEDEVLEEVKRGIWDSIKTFGKKFALNIMDKIKCKIGGGCPP},
target = {antimicrobial},
author = {peptidemodel},
year = {2026},
status = {computed}
}