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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 × 8

Rights

Language dc:language
English

Identifiers

dc:identifier.*
OAI identifier oai:identifier
oai:csuepress.columbusstate.edu:theses_dissertations-1390

Chain of custody

source
Harvested from
Columbus State University
Base URL
csuepress.columbusstate.edu/do/oai/
Last updated
2026-07-24
Source record
OAI-PMH GetRecord
citation

Anguilm, Tehgan N. Recombinant Expression of Preptin Analogs for Alanine Scanning Mutagenesis of Residues 27-29. Thesis thesis, 2020. https://csuepress.columbusstate.edu/theses_dissertations/390