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Date Permissions Signed
7-27-2015
Date of Award
Summer 2015
Document Type
Masters Thesis
Degree Name
Master of Science (MS)
Department
Chemistry
First Advisor
Antos, John M.
Second Advisor
Murphy, Amanda R.
Third Advisor
Anthony-Cahill, Spencer J.
Abstract
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.
Type
Text
DOI
https://doi.org/10.25710/28zk-0q45
Publisher
Western Washington University
OCLC Number
915140401
Subject – LCSH
Staphylococcus aureus--Analysis; Enzymes--Analysis; Protein engineering; Combinatorial chemistry; Peptide drugs--Synthesis; Proteomics--Synthesis
Format
application/pdf
Genre/Form
masters theses
Language
English
Rights
Copying of this document 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.
Recommended Citation
Nikghalb, Keyvan Dastkhosh, "Profiling Sortase Substrate Specificity using Peptide Libraries" (2015). WWU Graduate School Collection. 430.
https://cedar.wwu.edu/wwuet/430