Physicochemical characterization, cellular bioactivity, and biosafety evaluation of type A recombinant humanized collagen type XVII

Collagen type XVII is a unique transmembrane protein that plays a crucial role in anchoring epithelial cells to the underlying basement membrane. However, the low natural abundance of collagen type XVII in the human body poses significant challenges for large-scale extraction and production. With a development in biosynthesis technology, type A recombinant humanized collagen type XVII (rhCol XVII) has emerged as a promising and innovative alternative. In this study, rhCol XVII was successfully synthesized and expressed using genetic engineering techniques. The amino acid composition of rhCol XVII was analyzed, and its molecular weight was determined to be consistent with the theoretical design. Key physicochemical properties, including isoelectric point, particle size, and thermal stability, were evaluated. The experimentally measured pI was approximately 9.00, a particle size ranges from 820 to 857 nm, and thermal stability up to 23.60°C. The structure of rhCol XVII was characterized using infrared spectroscopy and circular dichroism. Furthermore, the cytocompatibility of rhCol XVII was assessed in vitro, and its systemic safety was evaluated in vivo. This research provided a solid foundation for the potential application of rhCol XVII in tissue engineering and regenerative medicine.