Active Insulin Analogs That Do Not Require Refrigeration

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.

Name thesis:degree_name

Molecular Microbiology and Immunology

Level thesis:degree_level

Honors Thesis

Grantor

University of Nevada, Reno

Year dc:date.issued

2016

Author dc:creator

• Suri, Reba

Advisor dc:contributor.advisor

• Tal-Gan, Yftah

Statement dc:rights

• In Copyright

Language dc:language.iso

en_US, English

Handle dc:identifier.uri

http://hdl.handle.net/11714/3326

OAI identifier oai:identifier

oai:scholarwolf.unr.edu:11714/3326