(640e) An Innovative Therapeutic Fusion Protein Approach for Chronic Wound Healing

In this study, the first steps in designing, expressing and in vitro testing were taken to investigate the properties of a potential therapeutic recombinant designed to release basic fibroblast growth factor (bFGF) at a wound site. It was hypothesized that by fusing bFGF to two collagen binding domains separated by a collagenase sensitive linker, the recombinant would preferentially locate to the site of a tear and eventually be released via enzymatic cleavage. This presentation will discuss the first steps in achieving this goal. The novel fusion protein was expressed in Escherichia coli BL-21using batch and fed batch techniques and purified by liquid chromatography from the lysate. Results showed that the target fusion protein was expressed and is sensitive to the protease, providing the initial data needed to establish the continued work on the project