The novel peptide preptin consists of 34 amino acid residues corresponding to Asp69-Leu102 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 Trp27, Arg28, and Gln29 of preptin in order to ultimately study the structure-activity relationship of these residues to preptin’s metabolic activity.
","abstract_html":"<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>","abstract_has_math":false,"creators":["Anguilm, Tehgan N"],"institution":null,"degree_name":"Chemistry","degree_level":"Thesis","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":["Dr. Jonathan Meyers","Dr. Daniel Holley","Dr. Cindy Ticknor"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2020,"date_issued":"2020-05-01T07:00:00Z","date_published":"2020-05-01T07:00:00Z","updated_at":"2026-07-24T01:45:08Z","subjects":["Preptin Analogs","Alanine Scanning Mutagensis","Residues 27-19","Osteoporosis","Metabolic Activity","Diabetes","Chemistry","Organic Chemistry"],"languages":["English"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://csuepress.columbusstate.edu/theses_dissertations/390","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Dr. Jonathan Meyers","Dr. Daniel Holley","Dr. Cindy Ticknor"]},{"key":"dc:creator","label":"Author","values":["Anguilm, Tehgan N"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2020-06-22T07:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Chemistry"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Preptin Analogs","Alanine Scanning Mutagensis","Residues 27-19","Osteoporosis","Metabolic Activity","Diabetes","Chemistry","Organic Chemistry"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["English"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://csuepress.columbusstate.edu/theses_dissertations/390"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["The novel peptide preptin consists of 34 amino acid residues corresponding to Asp69-Leu102 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 Trp27, Arg28, and Gln29 of preptin in order to ultimately study the structure-activity relationship of these residues to preptin’s metabolic activity.
"]},{"key":"dc:title","label":"Title","values":["Recombinant Expression of Preptin Analogs for Alanine Scanning Mutagenesis of Residues 27-29"]}]}],"canonical_facts":{"dc:contributor":["Dr. Jonathan Meyers","Dr. Daniel Holley","Dr. Cindy Ticknor"],"dc:creator":["Anguilm, Tehgan N"],"dc:date.available":["2020-06-22T07:00:00Z"],"dc:description.abstract":["The novel peptide preptin consists of 34 amino acid residues corresponding to Asp69-Leu102 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 Trp27, Arg28, and Gln29 of preptin in order to ultimately study the structure-activity relationship of these residues to preptin’s metabolic activity.
"],"dc:identifier":["https://csuepress.columbusstate.edu/theses_dissertations/390"],"dc:language":["English"],"dc:subject":["Preptin Analogs","Alanine Scanning Mutagensis","Residues 27-19","Osteoporosis","Metabolic Activity","Diabetes","Chemistry","Organic Chemistry"],"dc:title":["Recombinant Expression of Preptin Analogs for Alanine Scanning Mutagenesis of Residues 27-29"],"thesis:degree_discipline":["Chemistry"],"thesis:degree_level":["Thesis"],"thesis:degree_name":["Chemistry"]},"updated_at":"2026-07-24T01:45:08Z"}