Date of Award
5-2020
Type
Thesis
Major
Chemistry
Degree Type
Bachelor of Arts
Department
Chemistry
First Advisor
Jonathan Meyers
Second Advisor
Daniel Holley
Third Advisor
Cindy Ticknor
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.
Recommended Citation
Anguilm, Tehgan N., "Recombinant Expression of Preptin Analogs for Alanine Scanning Mutagenesis of Residues 27-29" (2020). Theses and Dissertations. 390.
https://csuepress.columbusstate.edu/theses_dissertations/390
