Production of Bioactive Human Beta-Defensin-4 in <Emphasis Type="Italic">Escherichia coli</Emphasis> Using SUMO Fusion Partner |
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Authors: | Jian Feng Li Jie Zhang Zhen Zhang Hong Wei Ma Jia Xin Zhang Shuang Quan Zhang |
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Institution: | (1) Jiangsu Province Key Laboratory for Molecular and Medical Biotechnology, Life Science College, Nanjing Normal University, 210046 Nanjing, Jiangsu, People’s Republic of China;(2) Jiangsu Engineering Research Center for Biomedical Function Materials, Nanjing Normal University, Nanjing, People’s Republic of China;(3) Jiangsu Key Laboratory for Supermolecular Medicinal Materials and Applications, Nanjing Normal University, 210046 Nanjing, People’s Republic of China; |
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Abstract: | The human beta defensins-4 (hBD4) exhibit a broad range of antimicrobial properties and are thought to be ideal therapeutic
agents because of their potential ability to circumvent the problems of acquired resistance often observed with other antimicrobial
therapies. We report here the application of small ubiquitin-related modifier (SUMO) fusion technology to the expression and
purification of cationic antibacterial peptide hBD4. The fusion protein expressed in a soluble form was purified to a purity
of 90% by Ni-IDA chromatography and 637 mg protein of interest was obtained per liter of fermentation culture. After the SUMO-hBD4
fusion protein was cleaved by the SUMO protease at 30 °C for 1 h, the cleaved sample was re-applied to a Ni-IDA. Finally,
about 166 mg recombinant hBD4 was obtained from 1 L fermentation culture with no less than 96% purity and the recombinant
hBD4 had similar antimicrobial properties to the synthetic hBD4. Thus, the SUMO-mediated peptide expression and purification
system potentially could be employed for the production of recombinant cytotoxic peptides. |
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