I. Targeted β-catenin Ubiquitination and Degradation Using Bifunctional Stapled Peptides II. Studies on Cell Penetration by Stapled Peptides

Abstract

Hydrocarbon-stapled alpha-helical peptides represent a relatively new class of synthetic peptidomimetics capable of inhibiting protein-protein interactions. It has been shown that hydrocarbon "staples" spanning one or two helical turns in a peptide increase alpha-helical content and protease resistance, enhance target binding affinity, and promote cell penetration. This technology has been applied to the development of cell-permeable ligands targeting several intracellular targets. This dissertation describes efforts to further the development of stapled peptide technology.