Protein derivatives possessing chemical and biological attributes not found in nature hold great potential for a new generation of therapeutics, diagnostics, and protein-based materials. In addition, modified proteins continue to serve as indispensable tools for fundamental research in biochemistry and cell biology. Consequently, methods for constructing modified proteins are in high demand. To meet this need, the Antos group is studying the use of enzymes as catalysts for constructing unique protein derivatives.
Current projects are focused are exploring the expanding family of sortase enzymes. While sortase A from Staphylococcus aureus has historically been the most commonly used enzyme for protein modification, it is now appreciated that numerous sortase homologs exist across a range of bacterial species. Yet, only a small number of these putative sortases have been studied experimentally, and even fewer have been exploited as tools for protein modification chemistry. Using a combination of synthetic chemistry and molecular biology, students in the Antos group are characterizing the activity of these novel sortases with the goal of developing new methods for protein engineering, and applying those methods to the construction of protein derivatives for a range of biological, industrial, and therapeutic applications.
