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Int. J. Mol. Sci. 2007, 8(6), 478-491;

High-level Expression of Cecropin X in Escherichia coli

State Key Laboratory of Pharmaceutical Biotechnology, Department of Biochemistry, Nangjing University, Nanjing 210093, P.R. China
Zhejiang Medicine Company, Ltd., Xinchang Pharmaceutical Factory, Xinchang County, Zhejiang Province 312500, P.R. China
Author to whom correspondence should be addressed.
Received: 6 February 2007 / Revised: 23 April 2007 / Accepted: 25 May 2007 / Published: 4 June 2007
(This article belongs to the Special Issue Interaction of Biological Molecules)
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Cecropin X is a short cationic peptide with a broad antibacterial and antitumorspectrum. Here, we report the production of a tumor necrosis factor (TNFα)-cecropin Xfusion protein under the control of a temperature-inducible PR promoter in the bacterialexpression vector pRC. During fermentation, we studied and optimized essentialparameters including the type of host cells, medium, timing of induction, post-inductiontime and dissolved oxygen level. Using the suitable conditions in the fermentation, up to20 % ~ 23 % of the total cellular proteins is produced as the fusion protein, mostly in theform of inclusion bodies. After washing, on average about 5.27 g dried inclusion bodiescould be collected from 1 L broth and the purity of inclusion bodies reached 80 %.Cecropin X obtained by cleaving the fusion protein with cyanogen bromide showedremarkable tumorcidal activity against mouse Lewis lung carcinoma 3LL in vivo. View Full-Text
Keywords: Cecropin X; Escherichia coli; Inclusion body; Fermentation; Tumorcidal activities Cecropin X; Escherichia coli; Inclusion body; Fermentation; Tumorcidal activities
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Shen, Y.; Lao, X.G.; Chen, Y.; Zhang, H.Z.; Xu, X.X. High-level Expression of Cecropin X in Escherichia coli. Int. J. Mol. Sci. 2007, 8, 478-491.

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