Active Insulin Analogs That Do Not Require Refrigeration
type: CreativeWork
description: Due primarily to hydrophobic interactions between nonpolar amino acid residues, molecules of insulin tend to interact with each other and undergo fibrillation to form linear aggregates when partially unfolded. Formation of these insulin fibrils significantly decreases insulin stability and activity, and has complicated insulin's role in the therapy of diabetes. This study will investigate techniques to create bioactive insulin analogs that are not susceptible to fibrillation, a temperature sensitive process, and thus do not require refrigeration. Solid phase peptide synthesis techniques and the incorporation of backbone modified amino acids into peptide sequences will be used to design novel insulin analogs.
abstract: Due primarily to hydrophobic interactions between nonpolar amino acid residues, molecules of insulin tend to interact with each other and undergo fibrillation to form linear aggregates when partially unfolded. Formation of these insulin fibrils significantly decreases insulin stability and activity, and has complicated insulin's role in the therapy of diabetes. This study will investigate techniques to create bioactive insulin analogs that are not susceptible to fibrillation, a temperature sensitive process, and thus do not require refrigeration. Solid phase peptide synthesis techniques and the incorporation of backbone modified amino acids into peptide sequences will be used to design novel insulin analogs.
author: Suri, Reba
language: en_US
language: English
date published: 2016
date modified: 2026-07-27T21:45:34Z
provider: University of Nevada - Reno
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: University of Nevada, Reno

PropertyValue
property ID: Handle
value: http://hdl.handle.net/11714/3326