Experimental anticancer peptide
A lab-studied peptide that researchers are exploring for its potential to fight cancer cells; experimental, not 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)
Fork this card to add platform evidence →
Activity measured in linked reference(s) — IC50/MIC/cytotoxicity data
Fork this card to add platform evidence →
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 this molecule kill cancer cells by physically ripping apart their surface, rather than by blocking a protein signal?
If true, cancer cells could not become resistant by simply switching off a receptor, because the attack would be physical, not chemical. This could matter for patients whose tumours have stopped responding to drugs that target specific proteins.
If we trim the peptide down to its most essential piece, would it still kill cancer cells, and could it be made reliably at reasonable cost?
Long peptides are expensive and tricky to produce as medicines. If a short 15-piece fragment works just as well, it could clear a major manufacturing hurdle and bring a usable drug candidate much closer to clinical testing.
Could this peptide tell cancerous cells apart from normal ones by sensing a surface molecule that tumours accidentally expose?
Many cancer drugs cause collateral damage to healthy tissue. If this peptide targets a marker that cancer cells display and normal cells do not, it could kill tumours while leaving surrounding tissue largely unharmed, potentially reducing side effects for patients.
Does a floppy middle section in the peptide act like a hinge, letting each end anchor into a cell's outer wall from opposite sides?
Understanding exactly how the peptide's shape drives its activity would let researchers engineer shorter or more stable versions with better performance, which could speed up the path toward a usable treatment.
▸full evidence table1 metrics
| metric | value | tool |
|---|---|---|
| ranking score | 0.44210514426231384 | 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{pep05243,
sequence = {GCVWPDGKAITTHKLQTTMLETKALIMGYFKSIATGGAMMAKPQEQLTPVIYPAV},
target = {anticancer},
author = {peptidemodel},
year = {2026},
status = {bioassayed}
}