Biosynthesis of Recombinant Human Collagen

Collagen is a trimeric molecule composed of repeating glycine-proline-hydroxyproline trimers, and depending on the type of collagen, homo- or heterotrimers of the alpha subunits of these trimers combine to form a right-handed triple helix structure. To date, numerous collagen preparations are commercially and clinically available; they have been extracted from animal tissues, including human and fish, or from human or land animal cells grown in vitro or have been produced by recombinant expression or direct peptide synthesis, but the risk of animal origin diseases and other risks of collagen extracted from animal tissues limit its potential application and development. Therefore, the use of genetic engineering technology to produce recombinant collagen is very important.

Recombinant collagens are categorized as recombinant human collagen, recombinant humanized collagen and recombinant collagen-like protein, as differentiated by specific compositions and structures. Among them, recombinant human collagen features a full-length amino acid sequence with a specific type of human collagen and a triple helix structure. The recombinant human collagen is obtained by transferring the DNA sequence of human collagen into different hosts (such as microorganisms, animals and plants) through fermentation, isolation and purification. For instance, Myllyharju [2] reported that recombinant human type I-III collagen can be expressed in Pichia pastoris.

References

Wenbo Liu, Hai Lin, Peng Zhao, et al. A regulatory perspective on recombinant collagen-based medical devices. Bioactive Materials, 2022, Volume 12.

Myllyharju J, Nokelainen M, Vuorela A, Kivirikko KI. Expression of recombinant human type I-III collagens in the yeast pichia pastoris. Biochem Soc Trans. 2000;28(4):353-7.