Peptides with Polyproline II Helix Secondary Structure and Their Potential Role in Biomaterials Engineering

Bound peptide monolayers are a promising way to control surface properties because peptides are biocompatible, easily tunable, and can be designed to have, or not have, interactions with cells. Our lab is especially interested in establishing new engineering models and assembly techniques to control and understand the behavior of surface-bound peptides for use as biomaterials. Peptides with a polyproline II helix secondary structure (PPII helix peptides) have recently emerged as promising tools for biomaterials due to their unique antifouling properties and ability to form dense monolayers. Using a variety of characterization techniques, we uncover new details about the assembly mechanisms of PPII helix peptides and explore their antifouling capacity. In addition, we explore the interactions of these peptdies with human mesenchymal stem cells and 3T3 cells with and without bioactive peptides attached. Collectively, these results reveal greater understanding of the mechanisms behind PPII helix peptide assembly and antifouling and provide insight into their potential use as biomaterials for regenerative engineering.