Chemical synthesis and characterization of ShK toxin: a potent potassium channel inhibitor from a sea anemone
| Autor: | V.M. Mahnir, M. E. Byrnes, William R. Kem, W .A. Volberg, Ilya Khaytin, D.S. Krafte, William P. Gorczyca, I. Zaydenberg, Michael W. Pennington, R. Hill, J. de Chastonay |
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| Rok vydání: | 2009 |
| Předmět: |
Male
Protein Folding Potassium Channels Charybdotoxin Molecular Sequence Data Sequence Homology Clostridium difficile toxin A Peptide Sea anemone medicine.disease_cause Biochemistry Jurkat cells Rats Sprague-Dawley Cnidarian Venoms Potassium Channel Blockers medicine Animals Amino Acid Sequence Disulfides Chromatography High Pressure Liquid Elapid Venoms chemistry.chemical_classification Stichodactyla helianthus biology Chemistry Toxin Cell Membrane Brain Biological activity biology.organism_classification Potassium channel Rats Sea Anemones |
| Zdroj: | International Journal of Peptide and Protein Research. 46:354-358 |
| ISSN: | 0367-8377 |
| DOI: | 10.1111/j.1399-3011.1995.tb01068.x |
| Popis: | ShK-toxin, a 35 residue peptide isolated from the sea anemone Stichodactyla helianthus, was synthesized using an Fmoc strategy and successfully folded to the biologically active form containing three intramolecular disulfide bonds. The ability of synthetic ShK toxin to inhibit specific [125I]-dendrotoxin I binding to rat brain membranes slightly exceeded (was more potent than) that of the natural ShK toxin sample, but was comparable with previously reported data for ShK toxin. The peptide toxin inhibited [125I]-charybdotoxin binding to Jurkat T lymphocytes with an IC50 value of 32 pM. In addition, Jurkat T lymphocytes Kv1.3 potassium channels were inhibited with an IC50 value of 133 PM. Owing to their unique structure and high affinity for at least some potassium channels, ShK toxin and related sea anemone potassium channel toxins may become useful molecular probes for investigating potassium channels. © Munksgaard 1995. |
| Databáze: | OpenAIRE |
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