Cloning, expression, and pharmacological activity of BmK AS, an active peptide from scorpion Buthus martensii Karsch

Abstract

BmK AS is a beta 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.

Expression, purification and characterization of an analgesic peptide from Buthus martensii Karsch in Pichia pastoris

“…To date, recombinant expression of scorpion toxins by genetic engineering was almost achieved in E. coli (Zhang et al 2001;Fu et al 2004;Shao et al 2008). In spite of its easy culture and rapid cell growth, E. coli prokaryotic expression system has many disadvantages such as insolubility, incorrect refolding and low bioactivity of recombinant proteins.…”

Insights into Antimicrobial Peptides from Spiders and Scorpions

“…These include charybdotoxin, opiscorpine, and heteroscorpine [32–34]. In 2008, BmK AS was characterized to have four disulfide bonds [35]. Additional peptides with four disulfide bonds were subsequently identified.…”

Molecular cloning and functional identification of analgesic peptides from Buthus martensii Karsch

“…The recombinant BL21 (λDE3) cells, and positive clones were identified via clony PCR screening and confirmed by DNA sequencing with T7 primers. The construction procedure was performed as described elsewhere [11]. Take BmK 9 for example， the purification procedure of the recombinant peptides was indicated.…”