Guanidinium toxins, as exemplified by saxitoxin (STX) are selective, nanomolar inhibitors of only a subset of the nine eukaryotic voltage-gated sodium channel subtypes (NaVs), despite the marked similarity in structure between members of this protein family. In an effort to understand the factors responsible for influencing toxin binding, we are employing novel toxin analogues in combination with protein mutagenesis to develop an accurate structural map of the toxin binding site. This information will inform the design of isoform-specific inhibitors of NaV function. Modified toxin syntheses together with results from protein mutagenesis and electrophysiology experiments will be presented.

Systematic approach for mapping the voltage-gated sodium channel pore using modified guanidinium toxins

248th National Meeting (2014)

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