Scorpion venom contains a large variety of biologically active peptides. However, most of
these peptides have not been identified and characterized. Peptides with three disulfide bridges, existing
in the scorpion venom, have not been studied in detail and have been poorly characterized until
now. Here, we report the recombinant expression and functional characterization of two kinds of
venom peptides (BmKBTx and BmNaL-3SS2) with three disulfide bridges. This study adopted an
effective Escherichia coli system. The genes for BmKBTx and BmNaL-3SS2 were obtained by polymerase
chain reaction and cloned to the pSYPU-1b vector. After expression and purification, the
two recombinant proteins were subjected to an analgesic activity assay in mice and whole-cell patchclamp
recording of hNav1.7-CHO cell lines. Functional tests showed that BmKBTx and BmNaL-
3SS2 have analgesic activity in mice and can interact with the hNav1.7 subtype of the voltage-gated
sodium channel (VGSC). Scorpion venom is rich in bioactive proteins, but most of their functions
are unknown to us. This study has increased our knowledge of these novel disulfide-bridged peptides
(DBPs) and their biological activities.
Keywords: BmKBTx, BmNaL-3SS2, recombinant expression, analgesic activity, electrophysiology, hNav1.7, disulfide bridge.
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