Bacteriophage (phage) therapy is a potential solution for treating antibiotic-resistant infections7. Since bacteriophages are bacterial in origin and are ‘expressed’ in bacteria, it is paramount that endotoxins are removed before delivery to avoid immunogenic shock. Traditionally, the purification process requires chromatography and is a bottleneck in the industrial-scale production of bacteriophage therapies. Elastin-like peptides (ELPs) can reversibly aggregate when heated to their transition temperature (Tb) and cooled back down. Expressing ELPs on phages could provide a way to purify phages from endotoxins. Additionally, thermal responsive phages can potential localize to infection sites for targeted delivery because of the increased temperature. Two ELPs one containing glycine and one containing tryptophan were examined using dynamic light scattering (DLS). T7 phage display was used to begin the process of expressing the chosen peptides on the surface of the T7 phage.
Author: Rebecca Dun-Roseman, Microbiology Major
Advisor(s): Kevin Yehl, Chemistry and Biochemistry
Kevin Morrison, Chemistry and Biochemistry