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SUMO Mediating Fusion Expression of Antimicrobial Peptide CM4 from two Joined Genes in Escherichia coli

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Abstract

Antibacterial peptide CM4 (ABP-CM4) is a small cationic peptide with broad-spectrum activities against bacteria, fungi, and tumor cells, which may possibly be used as an antimicrobial agent. To improve the expression level of CM4 in Escherichia coli, two tandem repeats of CM4 genes were cloned into the vector pSUMO to construct an expression vector pSUMO–2CM4. The fusion protein SUMO–2CM4, purified by Ni2+-chelating chromatography, was cleaved by hydroxylamine hydrochloride to release recombinant CM4. After the cleaved sample was re-applied to a Ni-IDA column, finally, about 48 mg recombinant CM4 was obtained from 1 L bacterial culture with no less than 96% purity, which was the highest yield of CM4 reported so far.

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Acknowledgements

This work was supported by the Grants of Nanjing Normal University and Jiangsu Province Graduate Innovation Project (No. CX07S-020z) administered by Prof. Zhang. This work was financially supported by National Nature Science Foundation of China (No. 30270193) and Natural Science Foundation of Jiangsu Province, China (No. BK2006221).

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Correspondence to Shuang Quan Zhang.

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Li, J.F., Zhang, J., Zhang, Z. et al. SUMO Mediating Fusion Expression of Antimicrobial Peptide CM4 from two Joined Genes in Escherichia coli . Curr Microbiol 62, 296–300 (2011). https://doi.org/10.1007/s00284-010-9705-3

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  • DOI: https://doi.org/10.1007/s00284-010-9705-3

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