Scorpine, a small cationic
peptide from the
venom of Pandinus imperator, which has been shown to have anti-bacterial and anti-plasmodial activities, has potential important applications in the pharmaceutical industries. However, the isolation of
scorpine from natural sources is inefficient and time-consuming. Here, we first report the expression and purification of recombinant
scorpine in Escherichia coli, using small
ubiquitin-related modifier (SUMO) fusion partner. The fusion
protein was expressed in soluble form in E. coli, and expression was verified by SDS-PAGE and western blotting analysis. The fusion
protein was purified to 90% purity by
nickel-nitrilotriacetic acid (Ni2+-NTA) resin chromatography. After the SUMO-
scorpine fusion
protein was cleaved by the SUMO
protease, the cleaved sample was reapplied to a Ni2+-NTA column.
Tricine/SDS-PAGE gel results indicated that
Scorpine had been purified successfully to more than 95% purity. The recombinantly expressed
Scorpine showed anti-bacterial activity against two standard bacteria including Staphylococcus aureus ATCC 29213 and Acinetobacter baumannii ATCC 19606, and clinically isolated bacteria including S. aureus S, S. aureus R, A. baumannii S, and A. baumannii R. It also produced 100% reduction in Plasmodium falciparum
parasitemia in vitro. Thus, the expression strategy presented in this study allowed convenient high yield and easy purification of recombinant
Scorpine for
pharmaceutical applications in the future.