Abstract

Collagen is a triple-helical mammalian protein, prolific due to its high tensile strength. Collagen’s properties give it applications spanning cosmetics to biomaterials for regenerative medicine. Most collagen is harvested from bovine sources, but this derivation process is unethical and poses health concerns in arsenic poisoning and zoonotic diseases. We developed a new process of generating functional collagen-like protein. Scl, streptococcal collagen-like protein, is a bacterial protein that emulates mammalian collagen properties. The distinction between bacterial and mammalian collagen is the hydroxyproline post-translational mechanisms. Mammalian collagen requires this complex process for high tensile strength, whereas bacterial collagen does not. Thus, Scl2 possesses superiority in mass production while maintaining the qualities of a good biomaterial. Our results include DNA and protein gel verification of our Gibson assembly and lithium acetate transformation into yeast. We also present the results of extracting animal collagen to work on our proposed implementation of collagen hydrogels