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- Title
Temperature-Controlled Expression of a Recombinant Human-like Collagen I Peptide in Escherichia coli.
- Authors
Xie, Wenjie; Wu, Qiqi; Kuang, Zhanpeng; Cong, Jianhang; Zhang, Qirong; Huang, Yadong; Su, Zhijian; Xiang, Qi
- Abstract
Collagen is the functional protein of the skin, tendons, ligaments, cartilage, bone, and connective tissue. Due to its extraordinary properties, collagen has a wide range of applications in biomedicine, tissue engineering, food, and cosmetics. In this study, we designed a functional fragment of human type I collagen (rhLCOL-I) and expressed it in Escherichia coli (E. coli) BL21(DE3) PlysS containing a thermal-induced plasmid, pBV-rhLCOL-I. The results indicated that the optimal expression level of the rhLCOL-I reached 36.3% of the total protein at 42 °C, and expressed in soluble form. In a 7 L fermentation, the yield of purified rhLCOL-I was 1.88 g/L. Interestingly, the plasmid, pBV220-rhLCOL-I, was excellently stable during the fermentation process, even in the absence of antibiotics. Functional analyses indicated that rhLCOL-I had the capacity to promote skin cell migration and adhesion in vitro and in vivo. Taken together, we developed a high-level and low-cost approach to produce collagen fragments suitable for medical applications in E. coli.
- Subjects
PEPTIDES; ESCHERICHIA coli; COLLAGEN; SKIN proteins; CONNECTIVE tissues; TISSUE engineering
- Publication
Bioengineering (Basel), 2023, Vol 10, Issue 8, p926
- ISSN
2306-5354
- Publication type
Article
- DOI
10.3390/bioengineering10080926