Penaeidin-3c cancer-fighting peptide
A peptide studied for its ability to fight cancer cells; experimental, not yet an approved drug.
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.
Is the rigid, cysteine-locked part of this shrimp peptide the key to attacking cancer cells?
If the disulfide scaffold is the active part, researchers could try building shorter, more stable versions that keep the cancer-killing region while dropping unnecessary bulk, which could lead to cheaper, more robust drug candidates.
If we remove the loose, wiggly end and keep only the rigid, cysteine-locked core, might it still kill cancer cells?
A shorter peptide is usually cheaper to make and can last longer in the body, so if a trimmed version still works it would lower the cost and complexity of developing this shrimp peptide into a drug candidate.
Could this peptide work not by punching holes in cancer cells but by latching onto a sugar-coated receptor scaffold on their surface?
If the peptide binds a cell-surface sugar that cancer cells use to receive growth signals, it could slow tumor growth by a different route than chemotherapy, opening the door to new drug combinations.
Could this peptide, currently studied for cancer, also act against the drug-resistant fungal infections that plague hospital patients?
Drug-resistant Candida infections sicken many hospital patients each year and new treatments are needed, so if this shrimp peptide retains its family's antifungal activity it could offer a fresh option.
Does this positively charged shrimp peptide target a molecular flag that many cancer cells put on their outside but healthy cells keep hidden?
If cancer cells are targeted because of this surface feature, the peptide could spare healthy tissue, which might allow higher, more effective doses with fewer toxic side effects.
▸full evidence table1 metrics
| metric | value | tool |
|---|---|---|
| ranking score | 0.5083625316619873 | 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{pep05276,
sequence = {KGGYTRPISRPPYGGGYGNVCTSCHVLTTSQARSCCSRFGRCCVPRRGYSG},
target = {anticancer},
author = {peptidemodel},
year = {2026},
status = {bioassayed}
}