BYU

Abstract by Michael Lee

Personal Infomation


Presenter's Name

Michael Lee

Degree Level

Undergraduate

Abstract Infomation


Department

Chemistry and Biochemistry

Faculty Advisor

Steven Castle

Title

Substitution of Bulky Dehydroamino Acids in 310 Helices

Abstract

Peptide based pharmaceuticals are a large emerging field in medicine, and one of the major concerns for these types of therapeutics is their longer term stability. By substituting bulky dehydroamino acids into key portions of the 310 helix secondary structure, we hypothesize that the resulting peptide will have an increased resistance to proteolysis due to the increased A1,3 strain with the backbone induced by the double bond while still being resistant to conjugate addition reactions due to the bulky substituents. We will synthesize a tetrapeptide with a well defined secondary structure that resembles the beginning of a 310 helix, substitute various dehydroamino acids including dehydroalanine, dehydrovaline, and dehydrophenylalanine into key turn positions, and then test each peptide against proteolysis assays to analyze the fortifying effects of each residue.