Journal
JOURNAL OF BIOTECHNOLOGY
Volume 128, Issue 1, Pages 184-193Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jbiotec.2006.09.014
Keywords
cone snail; conotoxin; mu LO-conotoxin family; fusion expression; recombinant protein; electrophysiology; voltage-sensitive sodium channel
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Conotoxins are a diverse array of small peptides mostly with multiple disulfide bridges. These peptides become an increasing significant source of neuro-pharmacological probes and drugs as a result of the high selectivity for ion channels and receptors. Usually, the analogue of natural conotoxins is produced by means of chemical synthesis. Here, we present a simple and fast strategy of producing disulfide-rich conotoxins via recombinant expression. By fused with thioredoxin and His tag, a novel O-superfamily conotoxin lt7a was successfully expressed in Escherichia coli and purified, resulting in a high yield of recombinant lt7a about 6 mg/l. The purity of target protein is up to 95% as identified by HPLC results. Whole cell patch-clamp recording revealed that the new conotoxin blocked voltage-sensitive sodium channels in rat dorsal root ganglion neurons, indicating it might be a novel mu O-conotoxin. (c) 2006 Elsevier B.V. All rights reserved.
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