Abstract
Venoms of snakes, scorpions, spiders, insects, sea anemones, and cone snails are complex mixtures of mostly peptides and small proteins that have evolved for prey capture and/or defense. These deadly animals have long fascinated scientists and the public. Early studies isolated lethal components in the search for cures and understanding of their mechanisms of action. Ion channels have emerged as targets for many venom peptides, providing researchers highly selective and potent molecular probes that have proved invaluable in unraveling ion channel structure and function. This minireview highlights molecular details of their toxin-receptor interactions and opportunities for development of peptide therapeutics.
Highlights
Ion channels are a diverse class of membrane proteins that play critical roles in cellular physiology, underlying such essential processes as neuronal signaling and muscle contractility [1]
Key ion channel targets of venom peptides include voltagegated potassium, sodium, and calcium channels and the ligandgated nicotinic acetylcholine receptors, where toxins acting at different binding sites have evolved across multiple phyla
Kϩ channels are four-domain membrane proteins that selectively transport Kϩ ions across the cell membrane, where they play a key role in regulating cell excitability [3] and non-excitable cell physiology
Summary
Kϩ channels are four-domain membrane proteins that selectively transport Kϩ ions across the cell membrane, where they play a key role in regulating cell excitability [3] and non-excitable cell physiology. The venoms of snakes, cone snails, spiders, anemones, and scorpions have provided researchers with potent subtype-selective pharmacological tools, including several with therapeutic potential [2] Many of these peptides possess a conserved functional dyad, comprising a Lys residue near a Tyr, Phe, or Leu, indicative of convergent evolution among many [6] but not all [7] Kϩ channel toxins. Snake—Isolated Ͼ20 years ago from African snakes (Dendroaspis sp.), dendrotoxins have proved remarkable tools to study Kϩ channel structure and function These peptides comprise 57– 60 aa and three disulfide bonds that stabilize a “Kunitz-type toxin” fold. The bacterial Kv channel isolated from VsTx1 [28] may allow a spider toxin-Kϩ channel co-crystal structure to be solved
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