BYU

Abstract by Collin Sanderson

Personal Infomation


Presenter's Name

Collin Sanderson

Co-Presenters

None

Degree Level

Undergraduate

Co-Authors

None

Abstract Infomation


Department

Chemistry and Biochemistry

Faculty Advisor

Steven Castle

Title

Dehydroamino Acid Substitution into 3-10 Helices

Abstract

Dehydroamino acids (dAAs) are a type of bulky residue that have been shown to give peptides increased resistance to proteolysis when compared to standard amino acids. Peptide-based drugs often suffer from quick proteolytic degradation, so fortifying these drugs with dAAs has a powerful therapeutic potential. dAA's have been shown to experience high A1-3 strain, restricting their acceptable phi and psi angles and secondary structures. Data from our recent publication shows that dAAs minimally affect the proper conformation of beta-hairpin peptides while providing them with proteolytic resistance. The 3-10 helix is a related secondary structure that is formed by consecutive beta-hairpins, suggesting that dAAs may have a similar fortifying effect on the 3-10 helix. My work is on the synthesis of a 3-10 helix-forming tetrapeptide with a dAA substituted at each of 3 possible sites.