Abstract
μ-Conotoxins are highly basic peptides which block the ion conduction pathway of voltage-gated sodium (NaV) channels by a combination of steric and electrostatic actions. Toxins, which block NaV channels at site one (saxitoxin derivatives, tetrodotoxin, and μ-conotoxins), show a similar voltage dependence of binding (apparent valence, zδ∼0.6) despite a wide range of nominal net charges (−1 to +7), suggesting a common mechanism underlying the voltage dependence. For PIIIA, single-channel studies using lipid bilayers reveal three different positions, R12, R14 and K17, at which neutral substitutions enable varying amplitudes of current to flow through toxin-bound channels.
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