Carolyn Zhou (VI), Ria Govil (VI), Ella Tabish (VI), Daniel Hall (V), Max Ventura (V), Julianna Zhang (IV), Rohan Goel (IV)
Project Summary
Collagen is the most abundant protein in the human body where it plays an important structural and functional role in many physiological and pathogenic processes. At the molecular level, collagen is made up of three polypeptide chains that form a secondary triple helical structure, which then self-assembles in a lateral staggered association to create fibrils with a unique 67 nm gap-overlap repeat; known as D-period. The unique conformity and behavior of the collagen molecule arises 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 the optimization of artificial collagen production. In order to better understand the role of the V-domain in improving the yield of collagen, we will compare the yield of the V-F877 sequence with and without the V-domain.
Currently, collagen is most commonly purified from animals for use in 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 in order to deepen knowledge of collagen’s structure as well as determine the best methods of creating viable artificial collagen that can be used as a biomaterial.
Project Goal
- Creating a collagen mimetic peptide that mimics structure and behavior of type 1 collagen
- Using a pre-existing plasmid design named V-F877 to start optimizing protein expression in bacteria
- Optimize the mimetic systems in bacteria for potential long-term use
Faculty Advisor
Dr. Haven
