Temporin-CDYe antimicrobial peptide
A naturally occurring peptide that kills or disables harmful bacteria and 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.
Does the full protein need to be cut down before it can fight bacteria, and if so, exactly where?
Many natural peptide antibiotics are first made as a longer, inactive form and only become active after being trimmed. If researchers can confirm precisely which piece of this frog-skin molecule is the live antibiotic, every future experiment, drug design effort, and safety test would be working with the right molecule, not a guess.
Can scientists adjust one tiny part of this peptide so it still kills Staph bacteria but is safer for human cells?
A major roadblock for turning natural peptide antibiotics into usable drugs is that they can also destroy red blood cells. If this targeted substitution works, it could open a path toward a safer antibiotic candidate for treating skin or wound infections caused by Staphylococcus aureus.
Is this antibiotic peptide too indiscriminate, attacking human blood cells as well as bacteria?
If the suspicion holds, this peptide in its current form would have a narrow safety margin and could not be used as-is in patients. Confirming the problem would also point directly to which part of the molecule needs to be redesigned, giving researchers a clear starting point for safer analogs.
Could this natural antibiotic miss a whole class of harmful bacteria because it cannot get through their outer shell?
Knowing which bacteria a peptide can and cannot reach narrows down the infections it might realistically treat, such as Staph skin infections versus gut or bloodstream infections caused by tougher Gram-negative bugs. If the limitation is confirmed, researchers could potentially pair it with a companion molecule to broaden its reach.
Does this peptide kill bacteria by punching through their outer layer rather than hitting a specific target inside?
Bacteria rapidly evolve resistance to drugs that block specific internal targets, but physically destroying a membrane is much harder to evolve around. If this mode of action is confirmed, it would support the case that this class of peptides could stay effective longer than conventional antibiotics, which is important for anyone facing recurring or hard-to-treat bacterial infections.
▸full evidence table1 metrics
| metric | value | tool |
|---|---|---|
| ranking score | 0.6178147196769714 | 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{pep05503,
sequence = {MFTLKKSMLLLLFLGTISLTLCEEERDANEEEENGGEVKVEEKRFIGPIISALASLFGG},
target = {antimicrobial},
author = {peptidemodel},
year = {2026},
status = {computed}
}