Two dipeptides with anticoagulant activity have been isolated from scorpion venom [21]. This study shows for the first time the ability of short venom peptides to slow down blood coagulation. Using molecular dynamics simulation of complexes between scorpion toxins and the Kv1.2 channel resulted in the identification of hydrophobic patches, hydrogen-bonds, and salt bridges as the three essential forces mediating the interactions between this channel and the toxins. This discovery might help design highly selective Kv1.2-channel inhibitors [22].
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