µ-conotoxin-GIIIB – Ion Channels and Transporters

µ-conotoxin GIIIB is a 22 amino acid conopeptide originally isolated from the venom of the piscivorous marine snail Conus geographus. µ-conotoxin GIIIB adopts a compact structure consisting of a distorted 310-helix and a small ß-hairpin. µ-conotoxin GIIIB is stabilized by three disulphide bridges and is highly enriched in lysine and arginine residues, forming potential sites of interaction with Na channels. An unusual feature is the presence of three hydroxyproline residues. µ-conotoxin GIIIB is a useful probe to discriminate between neuronal and muscle sodium channels as it exhibits at least a 1000-fold specificity for muscle versus nerve sodium channels. µ-Conotoxin GIIIB selectively blocks Nav1.4 voltage-dependent sodium channels, which are predominantly expressed in muscle, with an affinity close to 20 nM. µ-Conotoxin GIIIB appears to physically occlude the channel pore by binding on site I of the Na+ channel.

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