Date of Graduation
Fall 2025
Degree
Master of Science in Chemistry
Department
Chemistry & Biochemistry
Committee Chair
Keiichi Yoshimatsu
Abstract
Peptides are a class of molecules that are gaining interest of the pharmaceutical industry and academia. This would be due to the variety of applications that peptides can offer in terms of healthcare and fundamental research. Naturally this lends itself to an increased demand for an efficient method of peptide synthesis. Solid-phase peptide synthesis is the most common method for synthesizing peptides; however, the longer the peptide is, the less efficient the process becomes. The utilization of omniligase-1 helps alleviate the decreasing purity of solid-phase peptide synthesis product, but the utilization of omniligase-1 is not a panacea. Omniligase-1 is expensive to purchase from commercial sources. The previous reports used Bacillus sp., which is not a commonly used host for protein expression. Along those lines, I investigated the possibility for expressing omniligase-1 in E. coli, which is the most commonly used host for recombinant protein expression. Additionally, I explored the utility of cell-free protein synthesis as it allows for recombinant expression of proteins that could exhibit toxicity toward host cells.
Keywords
omniligase-1, cell-free protein synthesis, peptides, E. coli, recombinant protein expression
Subject Categories
Biochemistry
Copyright
© Jacob Linhardt
Recommended Citation
Linhardt, Jacob, "Towards the Expression of Omniligase-1 Using E. COLI and Cell-Free Protein Synthesis" (2025). Graduate Theses/Dissertations. 4137.
https://bearworks.missouristate.edu/theses/4137
