Charybdotoxin blocks dendrotoxin-sensitive voltage-activated K+ channels.
Charybdotoxin, a short scorpion venom neurotoxin, which was thought to be specific for the blockade of Ca2+-activated K+ channels also blocks a class of voltage-sensitive K+ channels that are known to be the target of other peptide neurotoxins from snake and bee venoms such as dendrotoxin and MCD peptide. Charybdotoxin also inhibits 125I-dendrotoxin and 125I-MCD peptide binding to their receptors. All these effects are observed with an IC50 of about 30 nM.
Schweitz
H
H
Centre de Biochimie du Centre National de la Recherche Scientifique, Nice, France.
Stansfeld
C E
CE
Bidard
J N
JN
Fagni
L
L
Maes
P
P
Lazdunski
M
M
D000818:Animals; D002478:Cells, Cultured; D018999:Charybdotoxin; D004546:Elapid Venoms / Q000037:antagonists & inhibitors*; D004594:Electrophysiology; D009498:Neurotoxins / Q000633:toxicity*; D015221:Potassium Channels / Q000187:drug effects*; D051381:Rats; D012604:Scorpion Venoms / Q000633:toxicity*; D013574:Synaptosomes / Q000378:metabolism
D004546:Elapid Venoms; D009498:Neurotoxins; D015221:Potassium Channels; D012604:Scorpion Venoms; D018999:Charybdotoxin; C020273:dendrotoxin