Animal toxins acting on ion channels of excitable cells are principally highly potent short
peptides that are present in limited amounts in the venoms of various unrelated species …

Potassium (K+) channels are a widespread superfamily of integral membrane proteins that
mediate selective transport of K+ ions through the cell membrane. They have been found in …

Proteomic analysis of the scorpion venom Scorpio maurus palmatus was performed using
reverse-phase HPLC separation followed by mass spectrometry determination. Sixty five …

OSK1 (α-KTx3. 7) is a 38-residue toxin cross-linked by three disulphide bridges that was
initially isolated from the venom of the Asian scorpion Orthochirus scrobiculosus. OSK1 and …

Scorpion toxins have been central to the investigation and understanding of the
physiological role of potassium (K+) channels and their expansive function in membrane …

Maurotoxin, a 34-amino acid toxin from Scorpio maurus scorpion venom, was examined for
its ability to inhibit cloned human SK (SK1, SK2, and SK3), IK1, and Slo1 calcium-activated …

The present study was conducted to explore the following hypotheses:(i) do scorpions
(Scorpio maurus palmatus) from different biotopes exhibit intraspecific diversity in their …

Pi1 is a 35-residue scorpion toxin cross-linked by four disulphide bridges that acts potently
on both small-conductance Ca2+-activated (SK) and voltage-gated (Kv) K+ channel …

The discovery of new drugs that selectively block or modulate ion channels has great
potential to provide new treatments for a host of conditions. One promising avenue revolves …

Scorpion venoms are a rich source of K+ channel-blocking peptides. For the most part, they
are structurally related small disulfide-rich proteins containing a conserved pattern of six …