ArticleToxins2014
Recombinant expression and functional characterization of martentoxin: a selective inhibitor for BK channel (α + β4).
Article in Toxins, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Purification and Comprehensive Characterization of Two Novel Acidic Glycoproteins from Scorpion with Therapeutic Potential.Applied biochemistry and biotechnology · 2026Article
- From venom peptides to neurotherapeutics: BmK defensins and short-chain peptides as modulators of ion channels.Frontiers in pharmacology · 2026Review
- Development of charybdotoxin Q18F variant as a selective peptide blocker of neuronal BK(α + β4) channel for the treatment of epileptic seizures.Protein science : a publication of the Protein Society · 2022Article
- Homology modeling and molecular docking simulation of martentoxin as a specific inhibitor of the BK channel.Annals of translational medicine · 2022Article
- The β4-Subunit of the Large-Conductance Potassium Ion Channel KCa1.1 Regulates Outflow Facility in Mice.Investigative ophthalmology & visual science · 2020Article
- Optimization of Scorpion Protein Extraction and Characterization of the Proteins' Functional Properties.Molecules (Basel, Switzerland) · 2019Article
- Anticonvulsant Effects of Dingxian Pill in Pentylenetetrazol-Kindled Rats.Evidence-based complementary and alternative medicine : eCAM · 2019Article
- Modulatory effects of bufalin, an active ingredient from toad venom on voltage-gated sodium channels.Molecular biology reports · 2018Article
- Large-Conductance Calcium-Activated Potassium Channels in Glomerulus: From Cell Signal Integration to Disease.Frontiers in physiology · 2016Review
- Peptide toxins and small-molecule blockers of BK channels.Acta pharmacologica Sinica · 2016Review
- Article
- Pharmacological consequences of the coexpression of BK channel α and auxiliary β subunits.Frontiers in physiology · 2014Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Martentoxin (MarTX), a 37-residue peptide purified from the venom of East-Asian scorpion (Buthus martensi Karsch), was capable of blocking large-conductance Ca2+-activated K+ (BK) channels. Here, we report an effective expression and purification approach for this toxin. The cDNA encoding martentoxin was expressed by the prokaryotic expression system pGEX-4T-3 which was added an enterokinase cleavage site by PCR. The fusion protein (GST-rMarTX) was digested by enterokinase to release hetero-expressed toxin and further purified via reverse-phase HPLC. The molecular weight of the hetero-expressed rMarTX was 4059.06 Da, which is identical to that of the natural peptide isolated from scorpion venom. Functional characterization through whole-cell patch clamp showed that rMarTX selectively and potently inhibited the currents of neuronal BK channels (α + β4) (IC50 = 186 nM), partly inhibited mKv1.3, but hardly having any significant effect on hKv4.2 and hKv3.1a even at 10 μM. Successful expression of martentoxin lays basis for further studies of structure-function relationship underlying martentoxin or other potassium-channel specific blockers.
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