Andrew Dale

• BSc (Hons) Biomedical Sciences
• Lipopolysaccharide binding site of the antibacterial toxin Colicin N

Colicins are antibacterial proteins released by and active against E. coli. They evade bacterial defences and we hope to discover bacterial Achilles’ heels by understanding their function. Recently we showed that colicin “N” binds a small molecule on the outer surface of bacteria, called LPS. In the next step we want to find out which part of the toxin binds LPS. This was done by the student who ran pre-prepared mutants on SDS page to identity which one prevents binding. In this way the LPS “binding site” will be defined and we will use this knowledge to design better antimicrobials.

Funding Source: Newcastle University