Peptide toxins are potent and selective compounds that can act on ion channels in plasma membrane of excitable cells.1 These high specificity and affinity compounds, often with diverse and selective pharmacologies, are used as pharmacological probes to study and characterize various receptor proteins involved in ion-channel function.1 These toxin peptides generally consist of a relatively small number of structural frameworks that are particularly suited to addressing the crucial issues of potency and stability.1 Multiple disulfide bonds constitute essential structural elements in many of these bioactive peptides, which are generated by proteolytic processing of prefolded protein precursors and then released from the cells in the bioactive form into the extracellular medium to exert their physiological function.
Ca2+ Channel Blockers
ω-Conotoxin GVIA
ω-Conotoxin MVIIC
ω-Conotoxin MVIIA
Imperatoxin A (IpTxa)
Ryanodine receptor agonist
K+ Channel Blockers
Iberiotoxin (IbTX)
Charybdotoxin
[Glu32]-Charybdotoxin
Apamin
Mast Cell Degranulating Peptide, MCD
Cl-Channel Blocker
Chlorotoxin (Cltx)
Other Ion Channel Blockers
Conantokin G
Sarafotoxin 6C
[Lys4]-Sarafotoxin 6c
Beauvericin
Company Info
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For more information, visit www.anaspec.com
Reference:
1. Lewis, RJ. and ML. Garcia, Nat. Rev. Drug Discov. 2, 790 (2003).
