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  • Title: Heterologous expression and purification of dermaseptin S4 fusion in Escherichia coli and recovery of biological activity.
    Author: Song D, Chen Y, Li X, Zhu M, Gu Q.
    Journal: Prep Biochem Biotechnol; 2014; 44(6):598-607. PubMed ID: 24499364.
    Abstract:
    Heterologous expression of dermaseptin S4 (DS4), which has cytolytic activity in vitro against a broad spectrum of pathogenic microorganisms, was examined in Escherichia coli. The plasmid pGEX-4T-1, encoding DS4 fused with glutathione S-transferase (GST), was constructed and cloned into the E. coli strain BL21 (DE3). The fusion protein was overexpressed in this strain after induction with isopropyl-beta-D-thiogalactopyranoside (IPTG) and purified to homogeneity using GST affinity chromatography. To recover biologically active DS4, the purified fusion protein was cleaved using thrombin protease; the liberated DS4 was shown to be bactericidally active against an indicator strain. Since it is less expensive to obtain such a peptide biologically, in this study, we report for the first time a method to express purify DS4 in E. coli using a GST fusion system.
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