Abstract
In the last three decades, numerous peptides isolated from scorpion venom have been identified as members of the KTx, or potassium channel-blocking group of toxins. This chapter provides an overview of the four families of KTx, named α, β, γ, and κ, discussing characteristic structural features and K+ channel selectivity of these peptides. Methods of KTx peptide identification and isolation, as well as techniques for the assessment of the efficacy of potassium channel blockade, are described. With the advancement of molecular biology, molecular dynamics simulations, and nuclear magnetic resonance (NMR) techniques, many details of the toxin-channel interaction have been clarified and models of different modes of toxin binding have emerged. A table summarizing all currently known 133 members of the KTx group of peptides is presented, including their systematic and common names, along with their affinities for the major target K+ channels, which may be in the low picomolar range. These peptides have provided vital information about the topology of the external pore region of K+ channels highlighting similarities and even minute differences. In addition to being valuable exploratory molecular tools, peptide blockers of K+ channels with high affinity and selectivity offer great potential for therapeutic use in a wide variety of diseases as was illustrated by several successful trials in animal models.
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Bartok, A., Panyi, G., Varga, Z. (2014). Potassium Channel-Blocking Peptide Toxins from Scorpion Venom. In: Gopalakrishnakone, P., Ferroni Schwartz, E., Possani, L., Rodríguez de la Vega, R. (eds) Scorpion Venoms. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-6647-1_30-1
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