Zhanpeng Kuang
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Zhanpeng Kuang has a total of 7 co-authors. Here are the top co-authors by number of shared publications:
- Jianhang Cong
State Key Laboratory of Bioactive Molecules and Druggability Assessment, Jinan University, Guangzhou 510632, China
1 shared publication - Qi Xiang
Guangdong Provincial Key Laboratory of Bioengineering Medicine, Institute of Biomedicine, Jinan University, Guangzhou 510632, China
1 shared publication - Qiqi Wu
State Key Laboratory of Bioactive Molecules and Drug Gability Assessment, Jinan University, Guangzhou 510632, China
1 shared publication - Qirong Zhang
Biopharmaceutical R&D Center, Jinan University, Guangzhou 510632, China
1 shared publication - Wenjie Xie
Institute of Biomedicine and Guangdong Provincial Key Laboratory of Bioengineering Medicine, Jinan University, Guangzhou 510632, China
1 shared publication - Yadong Huang
Department of Cell Biology, Jinan University, Guangzhou, China
1 shared publication
Latest Publications
- Open Access
- 4 August 2023
- Published by MDPI AG in Bioengineering
- Vol. 10 (8) , 926
Temperature-Controlled Expression of a Recombinant Human-like Collagen I Peptide in Escherichia coli
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.
- 4 August 2023
- Published by MDPI AG in Bioengineering
- Vol. 10 (8) , 926
Open AccessTemperature-Controlled Expression of a Recombinant Human-like Collagen I Peptide in Escherichia coli
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.