our focus

We focus on fighting antimicrobial resistance with the help of our engineered fusion endolysins.
antibiotic resistance
Bacteria are all around us. Most of them are good and protect us, but some can cause irritation or infection. Antibiotics do not distinguish between good and bad bacteria and their use can lead to side effects and resistance. This renders them unsuitable for long-term use. As they have been broadly used - often inappropriately - the emergence of antibiotic-resistant 'superbugs' is now a global concern.
"Mitigating AMR will have a huge impact on reaching 6 of the 17 sustainable development goals (SDGs) set out by the world health organization."
$ 1.7 trillion
additional health spending per year expected by 2050 due to the rise of antimicrobial resistance.
our solution:
Engineered fusion endolysins dervived from bacteriophages

Since the rise in multi-drug resistant bacterial infections seems unstoppable, alternative strategies to combat these pathogens are of high unmet need.  Bombilysin, a combination of the prefix "Bombinin" (an antimicrobial peptide derived from the amphibian Bombina orientalis) with an "endolysin" (the enzyme that a phage produces to kill a bacteria) is a novel antimicrobial platform technology to combat bacterial pathogens that show high resistance rates to other antimicrobials such as antibiotics. Our platform can be adapted to design specific fusion endolysins that either target gram-positive or gram-negative bacterial species. Even multi-drug resistant or persistent cells can be addressed by their unique mode of action.

In addition, Bombilysins have also been shown to be more effective in killing strain-specific bacteria in comparison to wild-type endolysins.  This is due to the fusion of highly effective target peptide moieties based on Bombinin, resulting in novel chimeric endolytic enzymes with improved affinity to the bacterial cell wall, (thermo)stability, and without the possibility of building up resistance.

structural design

Bombilysins are recombinant fusion endolysins derived from bacteriophages.  These muralytic enzymes have a modular structure composed of an enzymatically active domain (EAD) and a cell wall-binding domain (CBD). The EAD provides the actual enzymatic activity that cleaves  peptidoglycan structures, whereas the CBD recognizes and leads the endolysin to the specific cell wall-associated ligand molecules of a specific bacteria species.

In addition, Bombilysins have also been shown to be more effective in killing bacteria in comparison to native endolysins.  This is due to the fusion of a highly effective antibacterial peptide moiety of the antibacterial protein Bombinin, derived from the amphibian Bombina orientalis


The fusion results in novel chimeric endolytic enzymes with improved affinity to the bacterial cell wall, (thermo)stability, and killing rate.

bombilysins vs

While classic antibiotics require non-resistant cells, work within hours or even days and only kill cells that are metabolically active, our fast-acting Bombilysins destroy sensitive, resistant and persistent bacterial cells within minutes. 

Bombilysins selectively attack the cell wall of gram-negative or gram-positive bacterial cells leading to cell death caused by high osmotic pressure. Antibiotics also target the bacterial cell wall. However, they inhibit the assembly of a functional peptidoglycan by specific binding to enzymes of dividing cells. They are translocated through the outer membrane via porins into the periplasmic space of the bacteria.

Subsequently, most antibiotics bind to enzymes called peptidoglycan transpeptidases and thus inhibit the crosslinking of peptidoglycan precursors to build the functional cell wall of metabolically active and dividing cells. This leads to the death of the bacteria.


Unlike antibiotics, Bombilysins do not require an active metabolism because they work directly on the cell envelope by combining electrostatic and hydrophobic peptides with a muralytic moiety. Under high osmotic pressure, the inner membrane blebs out and finally the bacterial cell bursts.


*Phage endolysins are highly conserved in different bacteriophage strains (95% at the amino acid level), which implies that endolysins from bacteriophage are active against most strains of a specific bacteria. Phage endolysins have been used as  antimicrobials both in vitro and in vivo with promising results.


Furthermore, no resistance to phage endolysins has been reported. It has been shown that even though there is a possibility that bacteria can become resistant to phages, they will remain sensitive to its endolysin destruction.



We're growing a robust clinical program on
several targets to tackle antimicrobial resistance.