Histatin-1 antimicrobial peptide
A naturally derived peptide that kills or slows harmful bacteria; 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.
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 histatin-1 kill or weaken microbes mainly by binding up zinc rather than by tearing holes in their membranes?
Understanding this could guide design of better antifungal or antibacterial peptides that target metal availability, a strategy that is harder for microbes to develop resistance against.
Does histatin-1 trigger cell movement and tissue repair through a receptor signaling pathway rather than by killing bacteria, and can a short core piece do the same?
If a short core motif drives wound healing through this pathway, it could be developed as a simple topical gel to help mouth sores, post-surgical wounds, or diabetic ulcers heal faster.
Does histatin-1 get inside Candida through the same fungal transporters that carry its relative histatin-5, explaining why it targets fungi more than bacteria?
If fungi cannot easily shut this entry route without harming themselves, histatin-1 derived antifungals could be harder for Candida to resist, which matters for immunocompromised patients.
Is the secreted, active form of histatin-1 the shorter mature peptide that remains after the front signal sequence is cleaved off?
This points drug developers and researchers to use the mature fragment rather than the full precursor, which would behave more like the natural secreted peptide and be simpler to make.
Does the aromatic, acidic end of histatin-1 contribute to holding the peptide onto tooth enamel, alongside its known anchoring regions?
If true, histatin-1 inspired coatings could be engineered into toothpastes or dental treatments that shield enamel from bacterial colonization.
▸full evidence table1 metrics
| metric | value | tool |
|---|---|---|
| ranking score | 0.5270271897315979 | 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{pep05581,
sequence = {MKFFVFALILALMISMTRADSHEKRHHGYRRKFHEKHHSHREFPFYGDYGSNYLYDN},
target = {antimicrobial},
author = {peptidemodel},
year = {2026},
status = {bioassayed}
}