If you have any problems related to the accessibility of any content (or if you want to request that a specific publication be accessible), please contact us at firstname.lastname@example.org.
Active Insulin Analogs That Do Not Require Refrigeration
Microbiology and Immunology
Molecular Microbiology and Immunology
AltmetricsView Usage Statistics
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.