Recombinant Expression of Preptin Analogs for Alanine Scanning Mutagenesis of Residues 27-29
type: CreativeWork
description: 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: 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.
author: Anguilm, Tehgan N
language: English
keywords: Preptin Analogs, Alanine Scanning Mutagensis, Residues 27-19, Osteoporosis, Metabolic Activity, Diabetes, Chemistry, Organic Chemistry
date published: 2020-05-01T07:00:00Z
date modified: 2026-07-24T01:45:08Z
provider: Columbus State University
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: Columbus State University