Technology · Platform
the peptide platform in detail
The peptides are cationic and are drawn to the negatively charged bacterial membrane. Activity is retained across isomers and fragments, which is what makes the mechanism purely physical rather than pharmacological [2]. Selectivity has been shown in vitro: no cytotoxicity to human keratinocytes was observed [4]. No human efficacy data exist.
ADMERCIN
- Molecule
- 3–4 kDa cationic peptide
- Mechanism
- Physicochemical membrane disruption
- Selectivity
- No keratinocyte cytotoxicity, in vitro
- Spectrum
- MRSA · ESKAPE · enveloped viruses, in vitro
- Status
- PRECLINICAL
Mechanism of action
Bind, collapse, select
01Bind
The cationic peptide is drawn to the negatively charged bacterial membrane.
02Collapse
The membrane is physically disrupted and pores form.
03Select
The human cell membrane is neutral and is left untouched.
Membrane disruption confirmed by SEM and TEM [1]
Publications
The peptide literature
2025
Materials Today Bio
In a preclinical porcine wound model the peptides eradicated S. aureus infection (<10 CFU/g vs 4.3×10⁶ in controls, p<0.0001) and promoted re-epithelialisation. [1]
2023
HeAliX research programme
Positive results against WHO-prioritised multi-resistant ESKAPE bacteria, in vitro. [6]
2022
PLoS One
Broad-spectrum antiviral activity in vitro, including enveloped viruses. [5]
2021
Scientific Reports
Selective for bacterial membranes: no cytotoxicity to human keratinocytes observed in vitro. [4]
2020
Scientific Reports
In vitro, the peptides reduced the required dose of rifampicin more than 30-fold and no resistance development was observed after 20 generations of exposure. [2]
2016
BMC Microbiology
The peptides bind to and permeabilise the membrane of P. gingivalis; rapid killing was demonstrated in vitro. [3]