ArticleToxicon : official journal of the International Society on Toxinology2012
Expression and isotopic labelling of the potassium channel blocker ShK toxin as a thioredoxin fusion protein in bacteria.
Article in Toxicon : official journal of the International Society on Toxinology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 21 citations in OpenAlex.
- A bioengineered probiotic for the oral delivery of a peptide Kv1.3 channel blocker to treat rheumatoid arthritis.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Molecular and Functional Characterization of a Novel Kunitz-Type Toxin-like Peptide in the Giant Triton SnailMarine drugs · 2022Article
- Genomic Structure of Two Kv1.3 Channel Blockers from Scorpion Mesobuthus eupeus and Sea Anemone Stichodactyla haddoni and Construction of their Chimeric Peptide as a Novel Blocker.Biochemical genetics · 2022Article
- Conformational exchange in the potassium channel blocker ShK.Scientific reports · 2019Article
- Differences in ion channel phenotype and function between humans and animal models.Frontiers in bioscience (Landmark edition) · 2018Review
- Prolonged immunomodulation in inflammatory arthritis using the selective Kv1.3 channel blocker HsTX1[R14A] and its PEGylated analog.Clinical immunology (Orlando, Fla.) · 2017Article
- Preferential uptake of antioxidant carbon nanoparticles by T lymphocytes for immunomodulation.Scientific reports · 2016Article
- N-Terminally extended analogues of the K⁺ channel toxin from Stichodactyla helianthus as potent and selective blockers of the voltage-gated potassium channel Kv1.3.The FEBS journal · 2015Article
- Development of highly selective Kv1.3-blocking peptides based on the sea anemone peptide ShK.Marine drugs · 2015Article
- Conformational flexibility in the binding surface of the potassium channel blocker ShK.Chembiochem : a European journal of chemical biology · 2014Article
- Blocking KV1.3 channels inhibits Th2 lymphocyte function and treats a rat model of asthma.The Journal of biological chemistry · 2014Article
- A potent and Kv1.3-selective analogue of the scorpion toxin HsTX1 as a potential therapeutic for autoimmune diseases.Scientific reports · 2014Article
- A potent and selective peptide blocker of the Kv1.3 channel: prediction from free-energy simulations and experimental confirmation.PloS one · 2013Article
- Blocking KCa3.1 channels increases tumor cell killing by a subpopulation of human natural killer lymphocytes.PloS one · 2013Article
- A C-terminally amidated analogue of ShK is a potent and selective blocker of the voltage-gated potassium channel Kv1.3.FEBS letters · 2012Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
The polypeptide toxin ShK is a potent blocker of Kv1.3 potassium channels, which play a crucial role in the activation of human effector memory T-cells (T(EM)). Selective blockers constitute valuable therapeutic leads for the treatment of autoimmune diseases mediated by T(EM) cells, such as multiple sclerosis, rheumatoid arthritis, and type-1 diabetes. We have established a recombinant peptide expression system in order to generate isotopically-labelled ShK and various ShK analogues for in-depth biophysical and pharmacological studies. ShK was expressed as a thioredoxin fusion protein in Escherichia coli BL21 (DE3) cells and purified initially by Ni²⁺ iminodiacetic acid affinity chromatography. The fusion protein was cleaved with enterokinase and purified to homogeneity by reverse-phase HPLC. NMR spectra of ¹⁵N-labelled ShK were similar to those reported previously for the unlabelled synthetic peptide, confirming that recombinant ShK was correctly folded. Recombinant ShK blocked Kv1.3 channels with a K(d) of 25 pM and inhibited the proliferation of human and rat T lymphocytes with a preference for T(EM) cells, with similar potency to synthetic ShK in all assays. This expression system also enables the efficient production of ¹⁵N-labelled ShK for NMR studies of peptide dynamics and of the interaction of ShK with Kv1.3 channels.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.