Esculentin antiviral peptide
A short protein fragment studied for fighting viruses; experimental and 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)
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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.
Could the two ends of this peptide each do a different job, one fighting viruses and one fighting bacteria?
If true, scientists could cut the peptide in half and build a shorter, cheaper drug that does only what they need. It would also hint that the virus-fighting tip could be grafted onto other drug molecules as a reusable building block.
Does this peptide work by blocking the sticky surface that viruses use to grab onto your cells?
If this holds, the peptide could potentially work against a wide range of enveloped viruses, including herpes, SARS-CoV-2, dengue, and RSV, because all of them use the same docking mechanism. It would also mean the peptide is less likely to harm human cells, since it targets a viral attachment step rather than punching holes in membranes indiscriminately.
Could a single chemical change stop the blood from dismantling this peptide before it reaches its target?
Blood contains molecules that quickly break the chemical bond holding part of this peptide in shape. If swapping that bond for a tougher version extends its lifetime in the body by several times, it could turn a promising lab result into something worth testing in animals, accelerating the whole development timeline.
Could a peptide cataloged only for fighting viruses also work against fungal infections that resist most current drugs?
Candida biofilms, the sticky protective coatings fungi build inside the body, are notoriously hard to treat and cause serious illness in hospital patients. If this peptide disrupts those biofilms at safe doses, it could be repurposed using material already on hand, with no new synthesis needed.
Could this peptide keep working against future COVID variants because it targets the human cell surface rather than the virus's ever-changing spike protein?
Vaccines and antibodies that target the spike protein lose effectiveness as the virus mutates. If this peptide works by blocking a stable docking site on human cells instead, it could retain potency across variants, filling a real gap that current antivirals struggle with.
▸full evidence table1 metrics
| metric | value | tool |
|---|---|---|
| ranking score | 0.7322196364402771 | 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{pep05410,
sequence = {GLFSKLNKKKIKSGLIKIIKTAGKEAGLEALRTGIDVIGCKIKGEC},
target = {antimicrobial},
author = {peptidemodel},
year = {2026},
status = {bioassayed}
}