Voltage-gated sodium channels are targets for toxins from the venom of the spider Heriaeus melloteei |
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Authors: | A. S. Nikolsky B. Billen A. A. Vassilevski S. Yu. Filkin J. Tytgat E. V. Grishin |
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Affiliation: | 1. Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya, 16/10, Moscow, 117997, Russia 2. Laboratory of Toxicology, University of Leuven, Campus Gasthuisberg, O&N 2, P.O. Box 922, Herestraat 49, 3000, Leuven, Belgium
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Abstract: | Three novel peptides were isolated from the venom of the spider Heriaeus melloteei (Thomisidae) and characterized. The peptides named Hm-1, 2 and 3 blocked voltage-gated Na+ channels at concentrations in the order of 100 nM. Activity of the purified peptides was investigated in Na+ channel isoforms of mammals and insects. Hm-1 and 2 appeared to act as pore blockers, whereas Hm-3 modulated the channel activation process. The toxins described exhibit minor similarity with other known peptides and may therefore constitute new groups of Na+ channel ligands. |
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