Phage-ligand technology

Phagenligand the technology is based on the high affinity binding of phage proteins of bacteria and is, for example, as a method for bonding, for the detection and removal of bacterial endotoxins. For the experimental, industrial or clinical use recombinant phage proteins compared to other common methods offer the advantage of high specificity and a defined activity.

Origin / Technology

These phage proteins are the main constituent of the host recognition, wherein the staple, the ends of the tail fibers of bacteriophage to surface structures of the bacteria. The adsorption to the host via highly host-specific binding proteins. The end of the replication cycle lysis of the bacterial cell wall is accomplished by phage- induced expression of the enzyme endolysin, which new bacteriophages are released and the bacterial cell dies.

The highly specific binding activity of these recombinant phage proteins, for example, used to quantify or remove immunostimulatory lipopolysaccharides. Thus, the highly specific interactions of naturally occurring bacteriophages can be done scientifically and industrially usable with the host.

Applications

The Phagenligand technology found in the removal of microbial contaminants in food ( see magnetic affinity separation) as well as contaminated with endotoxins using laboratory samples. Furthermore, human diagnostic applications arise, especially in the clinical area for decolonization of pathogenic bacteria such as MRSA hospital. By biotechnological change the phage proteins can be optimized for each application. At therapeutic use in Germany has so far not allowed.