Derived from the mammalian immune system, antimicrobial peptides are powerful molecules that can rapidly and selectively kill bacteria—including antibiotic resistant bacteria—and prevent bacterial infections.
Until today, antimicrobial peptides have had poor stability
These peptides have been present in mammals for millions of years and have a unique way of killing bacteria by rapidly disrupting the bacteria’s cell membrane through something called electrostatic and amphiphilic interaction. You can think of peptides as a highly specialised soap-like molecule designed to kill bacterial cells by ripping off their skin.
Antimicrobial peptides carry a net-positive charge and a molecular structure that includes hydrophobic and hydrophilic characteristics. These two factors allow peptides to attract bacterial cells—which carry a net-negative charge and are also amphiphilic—and bind to them, before puncturing their membrane and killing the cell.
Peptides destroy bacterial cells in a physical process, which means bacteria have a very low probability of evolving resistance the way they have been able to against antibiotics, which work chemically.
Until today, antimicrobial peptides have had poor stability. In the past, their fragility has made antimicrobial peptides challenging for clinical applications. High doses of antimicrobial peptides were needed, which increased costs and, since at those doses peptides were classified as pharma products, prolonged the time-to-market.
As a result, past efforts to develop market-ready products featuring this valuable antimicrobial technology have faced substantial hurdles.
Amferia has solved this problem by implementing a scientifically robust approach that covalently and permanently bind antimicrobial peptides to the surface of a soft, ordered and amphiphilic hydrogel pad.
These permanent bonds protect the vulnerable portion of the peptide molecule and fix them in place, while leaving their bacteria-killing mechanism free to attract and destroy bacterial cells. They also ensure no peptides leak into the wound. Antimicrobial peptides fixed to an underlying hydrogel pad allowed Amferia to develop a safe, efficient and cost-effective design for an antimicrobial wound dressing.
Amferia has solved this problem by permanently binding the peptides to an amphiphilic hydrogel
This design provides the needed balance between stability and activity.
The end-product is a singular material that does not leach or release any peptides or substances into the body, but rather acts locally as a contact-killing medical device—which will enable faster clinical translation.
Previous antimicrobial peptide technologies utilize peptides in their pristine form, which renders them inactive in a few minutes. Amferia’s innovation enables the bound peptides to remain stable and active for up to five days. Current testing indicates the product we’re developing for wound care will be shelf-stable for up to eighteen months, and potentially up to two years.
