The vast majority of theses in this collection are open access and freely available. There are a small number of theses that have access restricted to the WWU campus. For off-campus access to a thesis labeled "Campus Only Access," please log in here with your WWU universal ID, or talk to your librarian about requesting the restricted thesis through interlibrary loan.
Date Permissions Signed
Date of Award
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.
Staphylococcus aureus--Analysis, Enzymes--Analysis, Protein engineering, Combinatorial chemistry, Peptide drugs--Synthesis, Proteomics--Synthesis
Western Washington University
Copying of this thesis in whole or in part is allowable only for scholarly purposes. It is understood, however, that any copying or publication of this thesis for commercial purposes, or for financial gain, shall not be allowed without the author's written permission.
Nikghalb, Keyvan Dastkhosh, "Profiling Sortase Substrate Specificity using Peptide Libraries" (2015). WWU Graduate School Collection. 430.