Artificial Collagen for as a Biomaterial

Artificial Collagen as a Biomaterial

by James Houghton (VI), Michelle Lee (VI), Alexandra Drovetsky (V), Kirsten Lytle (V), Annabelle Shilling (IV), Theodore Strelecky (IV), Dr. Haven

Collagen is the most abundant protein in the human body and plays an essential structural and functional role in many physiological and pathogenic processes. At the molecular level, collagen consists of three polypeptide chains that form a secondary triple helical structure. These subunits then self-assemble in a lateral staggered association to create fibrils with a unique 67 nm gap-overlap repeat known as a D-period. The unique conformity and behavior of the collagen molecule arise from the repeating Glycine-X-Y pattern in its primary structure. The current goal of our project is to maximize the yield of collagen mimetic peptides that model the physical and chemical properties of natural type I collagen. We are currently utilizing a pre-existing peptide, named V-F877, which is 222 amino acids long and has a V-domain, a trimerization domain found in bacteria that is known to be integral for optimizing artificial collagen production. We will compare the yield of the V-F877 sequence with and without the V-domain to understand better the V-domain’s role in improving collagen yield. Currently, collagen is most commonly purified from animals for the medical field. This process is expensive and often results in a high degree of variation. Generating collagen mimetic peptides that successfully replicate human collagen could provide a safer, pathogen-free, and cost-effective alternative. We plan to provide critical research on these foundational steps to deepen knowledge of collagen’s structure and determine the best methods of creating viable artificial collagen that can be used as a biomaterial.

Figure 1. Hierarchical Organization of Collagen Structure (A. Collagen Fibrils under an Electron Microscope, B. Staggered and Intertwined arrangement of triple helices within a fibril, C. Different stages of Fibrillogenesis from the Primary Structure (Bottom))