Abstract by Jatinder Singh

Personal Infomation

Presenter's Name

Jatinder Singh

Degree Level


Abstract Infomation


Chemistry and Biochemistry

Faculty Advisor

Steven Castle


Rendering Helical Peptides More Suitable as Anti-Cancer Agents


Since the discovery of first peptide insulin in 1920, 7500 naturally occurring peptides have been identified. However, these peptides suffer from a major drawback of rapid digestion by enzymes, poor bioavailability, and lack of membrane permeability. Thus, they are less efficient than small-molecule drugs and very expensive. Previously, our lab successfully synthesized several medium-sized peptides (β-hairpins) of α, β-dehydroamino acids (DAAs) with 6-7 times more stability to proteolysis digestion than control peptide. Now, we are introducing DAAs in helical structures, synthesizing 310-helical peptides having conformational rigidity and thermodynamically favored folded structure. Stapling (stapled α-helical peptides, SAH) is another method to induce conformational stability in helical peptides, but recent evidences cast doubt on their suitability as drugs. We are synthesizing two DAA-containing helical peptides and then evaluating their proteolytic stability: Z-Aib-Pro-DEnv-Ala-OMe and Z-DEnv-Pro-Aib-Ala-OMe. Introduction of DAAs into helical structure could enable the future design of stabilized helical anti-cancer peptides.