Presenter: Henry Hochstatter − Human Physiology
Faculty Mentor(s): Jonathan Dorogin
Session: (In-Person) Poster Presentation
Wound healing is orchestrated by a complex sequence of proteins, including granulocyte-macrophage colony stimulating factor (GM-CSF), which facilitates myeloid stem cell differentiation into mature immune cells during the inflammatory response, and fibroblast growth factor-2 (FGF-2), which stimulates fibroblast proliferation. Delivery of these proteins to sites of injury may increase the efficacy of tissue repair, but current protein delivery methods fail to precisely control the temporal presentation of GM-CSF and FGF-2 at relevant stages of wound healing. The aim of this research is to develop affinity-based biomaterials that can facilitate the controlled delivery of these regenerative proteins for improved tissue regeneration. To accomplish this, small protein-binding peptides called affibodies have been identified from a randomized pool of ~860 million unique sequences via sorting of a yeast surface display library. Five affibodies were selected that specifically bind to GM-CSF or FGF-2 with varying affinities; the affinities of these affibodies have been characterized on the surface of yeast cells, and were expressed as soluble proteins in E. coli for further analysis. The wide range of affibody affinities for their protein targets will enable extensive modulation of temporal protein presentation. Conjugating these affibodies to biomaterials will allow for the spatiotemporal control of protein release to a wound site for improved wound healing in the clinic.