Columbus State University
Recombinant Expression of Preptin Analogs for Alanine Scanning Mutagenesis of Residues 27-29
Abstract
dc:description.abstract<p>The novel peptide preptin consists of 34 amino acid residues corresponding to Asp<sup>69</sup>-Leu<sup>102</sup> of proinsulin-like growth factor E-peptide. Preptin has been isolated from pancreatic beta cells, and it has been found to exhibit both metabolic and mitogenic activities. This makes preptin an attractive candidate to treat insulin-independent diabetes and osteoporosis. Alanine scanning mutagenesis was utilized to substitute an alanine for residues Trp<sup>27</sup>, Arg<sup>28</sup>, and Gln<sup>29</sup> of preptin in order to ultimately study the structure-activity relationship of these residues to preptin’s metabolic activity.</p>
Degree
thesis:*- Name thesis:degree_name
- Chemistry
- Level thesis:degree_level
- Thesis
- Discipline thesis:degree_discipline
- Chemistry
- Year dc:date.available
- 2020
Author and committee
dc:creator, dc:contributor.*- Author dc:creator
-
- Anguilm, Tehgan N
- Contributors dc:contributor
-
- Dr. Jonathan Meyers
- Dr. Daniel Holley
- Dr. Cindy Ticknor
Subjects
dc:subject × 8Rights
- Language dc:language
- English
Identifiers
dc:identifier.*- Repository record dc:identifier
- https://csuepress.columbusstate.edu/theses_dissertations/390
- OAI identifier oai:identifier
- oai:csuepress.columbusstate.edu:theses_dissertations-1390