- Alomone Labs Kaliotoxin-1 inhibits KV1.3 channels heterologously expressed in Xenopus oocytes.Currents were elicited by application of voltage ramp from a holding potential of -80 mV to 50 mV in 100 msec, delivered every 10 seconds. A. Time course of channel activity (current amplitude at 0 mV), before (black) and during (green) application of 1 nM Kaliotoxin-1 (#STK-370). B. Top, illustration of the voltage ramp protocol. Bottom, example of superimposed current traces before (black) and during (green) application of 1 nM Kaliotoxin-1, taken from the experiment in A.
- Crest, M. et al. (1992) J. Biol. Chem. 267, 1640.
- Rodriguez de la Vega, R.C. and Possani, L.D. (2004) Toxicon 43, 865.
- Romi, R. et al. (1993) J. Biol. Chem. 268, 26302.
- Mourre, C. et al. (1999) J. Pharmcol. Exp. Ther. 291, 943.
- Grissmer, S. et. al. (1994) Mol. Pharmacol. 45, 1227.
- Hopkins, W.F. et al. (1996) Curr. Pharmaceut. Design. 2, 389.
- Tricaud, N. et al. (2000) Toxicon 38, 1749.
- Gairi, M. et al. (1997) J. of Peptide Sci. 3, 314.
- Korukottu , J. et al. (2008) PLoS ONE 3, e2359.
- Kourrich, S. et al. (2001) Behav. Brain Res. 120, 35.
Kaliotoxin-1 is a 38 amino acid long toxin, originally isolated from the venom of Androctonus mauretanicus mauretanicus scorpion and is classified as α-KTX 3.1 scorpion toxin family, having three disulfide bridges1,2.
Kaliotoxin-1 is a potent inhibitor of large conductance Ca2+-activated K+ channels (BKCa)3, and it also binds and inhibits Dendrotoxin-sensitive voltage-dependent K+ channels, mainly KV1.1 (KCNA1), KV1.2 (KCNA2) and KV1.3 (KCNA3) with a Kd of 1.5, 25 and 0.1 nM, respectively4-6. Its binding affinity to rat brain synaptosomes is 5-fold higher than that of Kaliotoxin-37.
The 3D structure of Kaliotoxin was determined by NMR spectroscopy and showed significant differences from structures established for other related scorpion toxins8,9.
In vivo application of Kaliotoxin was shown to facilitate cognitive processes such as learning in rats10.
Kaliotoxin-1 (#STK-370) is a highly pure, synthetic, and biologically active peptide toxin.