Cloning, expression, and pharmacological activity of BmK AS, an active peptide from scorpion Buthus martensii Karsch
BmK AS is a β long-chain scorpion peptide from the venom of Buthus martensii Karsch (BmK). It was efficiently expressed as a soluble and functional peptide in Escherichia coli, and purified by metal chelating chromatography. About 4.2 mg/l purified recombinant BmK AS could be obtained. The recombinant BmK AS maintained a similar analgesic activity to the natural one in both the mouse-twisting test and hot-plate procedure. It also exhibited antimicrobial activity against both Gram-positive and Gram-negative bacteria. BmK AS is the first long-chain scorpion peptide reported to have antimicrobial activity, and is a valuable molecular scaffold for pharmacological research.
KeywordsAnalgesic activity Antimicrobial activity BmK AS Functional expression Homology model
Special thanks are due to Liaoning Education Department: education technology investigation supporting project (2004D222).
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