Soluble expression, purification and functional identification of a disulfide-rich conotoxin derived from Conus litteratus
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...
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Veröffentlicht in: | Journal of biotechnology 2007-01, Vol.128 (1), p.184-193 |
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Sprache: | eng |
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Zusammenfassung: | 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 μO-conotoxin. |
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ISSN: | 0168-1656 1873-4863 |
DOI: | 10.1016/j.jbiotec.2006.09.014 |