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Master of Science (MS)
Antos, John M.
Murphy, Amanda R.
Anthony-Cahill, Spencer J.
The use of enzymes for protein modification chemistry has gained traction in recent years due to the remarkable site-selectivity that enzymes afford. Among enzymes reported for this purpose, sortase A from Staphylococcus aureus (SrtAStaph) has garnered significant attention because of its selectivity, and its ability to install a wide range of non-natural modifications. In addition to SrtAStaph, it is now appreciated that sortase homologs exist in many bacterial strains, each with the potential to serve as a new catalyst for protein engineering. However, the majority of these enzymes has not been studied biochemically, and in order to utilize these enzymes for protein modification it is critical that the activity and specificity of each enzyme be verified experimentally. This includes determination of optimal substrate sequences and amine nucleophile preferences. Here we present progress toward characterizing the in vitro substrate specificity of ten sortase homologs using libraries of synthetic peptide substrates.
Western Washington University
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Nikghalb, Keyvan Dastkhosh, "Profiling Sortase Substrate Specificity using Peptide Libraries" (2015). WWU Graduate School Collection. 430.