Mauriporin antimicrobial peptide
A peptide that kills or slows the growth of harmful 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 this peptide latch onto a specific part of the bacterial outer shell before punching through it, rather than just sticking by static charge?
If the FGGFF motif really does grip the bacterial surface first, researchers could design shorter, cheaper peptides that do two jobs at once: kill bacteria AND neutralize the toxic debris they release when they die. That matters most for treating severe infections where the dying bacteria themselves can trigger dangerous immune overreactions.
Could the acidic ends of this peptide act like a safety lock, keeping it folded and harmless until it reaches bacteria?
If the peptide really does switch on only near bacteria, it could explain why it works against multiple bug types without causing widespread harm to the body. This kind of built-in selectivity, if confirmed, could guide engineers toward next-generation antibiotics that are less toxic and less likely to cause side effects.
Does this peptide attack drug-resistant bacteria in a different way than colistin, bypassing the shield those bacteria built up?
Colistin-resistant Acinetobacter baumannii is on the WHO's most-dangerous-pathogens list, and doctors are nearly out of options for it. If mauriporin attacks this bacteria through a different route, it could become a treatment option for patients who have no other choices, particularly in intensive care settings.
Does this peptide stay folded and inactive in the bloodstream, then unfold and activate in the saltier environment of an infection site?
If confirmed, this would mean the peptide is naturally tuned to activate right where infection is happening and stay quiet elsewhere in the body. That kind of built-in geographic targeting could reduce side effects and might eventually allow doctors to fine-tune formulations for specific types of infections.
If we cut off the floppy ends of this peptide, would the remaining core last longer without being digested and still work just as well?
Most peptide drugs get chewed up by the body's own enzymes before they reach an infection. If trimming this peptide down to its active core makes it more resistant to that breakdown, it could be a more practical drug candidate, cheaper to manufacture and more effective in the bloodstream, which are two of the biggest hurdles for turning any peptide into a real medicine.
▸full evidence table1 metrics
| metric | value | tool |
|---|---|---|
| ranking score | 0.5176429748535156 | 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{pep05499,
sequence = {MLIVDEVNSSRFGGFFRRIWKSKLAKRLRSKGKELLKDYANRVINGGPEEEAAGPPARK},
target = {antimicrobial},
author = {peptidemodel},
year = {2026},
status = {computed}
}