Date of Graduation
Bachelor of Science in Chemical Engineering
Servoss, Shannon S.
Protein purification is essential for advancements in biotechnology. There are several different methods employed in purifying a particular protein from a complex sample such as a cell lysate. These methods take advantage of differences in the size, charge or binding affinity of the protein. One such method is affinity chromatography which utilizes the binding affinity of a protein toward a certain ligand to purify a protein. This is usually used as a final step to extract the desired protein after the mixture has undergone other purification steps to remove unwanted materials. The goal of this project was to develop a one-step peptoid-based protein purification method. Poly-N-substituted glycines, or peptoids, were developed in the early 1990s and have been shown to have many biological applications. Peptoid side chains can be manipulated for unique circumstances by utilizing any free amine in synthesis. This is an advantageous quality in the determination of protein ligands. This study investigated using peptoids as a specific and efficient one-step process for purification methods. It showed there is potential of proteins binding to peptoids by determining protein concentration changes caused by incubation studies. However, these results could not be verified.
Dunn, M. (2013). Protein Isolation Using Peptoid Based Affinity Chromatography. Chemical Engineering Undergraduate Honors Theses Retrieved from https://scholarworks.uark.edu/cheguht/8