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AaH-II scorpion toxin

AaH-II was originally discovered from the venom of the scorpion Androctonus australis Hector and belongs to alpha-toxins. It is a 64 amino-acid peptide that comprises four disulfide bonds and structured according a beta1-alpha-beta2-beta3 scaffold. Iodinated AaH-II binds with a 3 nM affinity to axolemma from rat Central Nervous System (DeVries and Lazdunski, 1982). In frog myelinated nerve fibres, AaH-II prolongs the inactivation time constants of the inward Na+ current and induces a persistent current component (Benoit & Dubois, 1986). By these two effects combined, AaH-II causes prolonged action potentials and thereby decreased firing frequencies. These effects are susceptible to produce paralysis, cardiac arrhythmia and death, including in humans (Bosmans & Tytgat, 2007). Concerning the selectivity, the reported EC50 values for slowing channel inactivation are 3 nM for rat Nav1.2 and 2 nM for rat Nav1.4 channels (Alami et al., 2003). The EC50 value on Nav1.7 is 52 nM. At the functional level, AaH-II was shown to bind onto the voltage-sensor of domain IV to block fast inactivation by trapping a deactivated state. (Clairfeuille et al., 2019). Smartox now proposes the synthetic version of AaH-II.

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Disulfide bonds: C1-C8; C2-C5; C3-C6; C4-C7
Length (aa): 64
Formula: C313H457N89O95S8
Molecular Weight:  7243,18 Da
Appearance: white lyophilized solid
Solubility: water or saline buffer
CAS number: NA
Source: Synthetic
Purity rate: > 95 %

Structural basis of α-scorpion toxin action on Nav channels.

Voltage-gated sodium channel modulation by scorpion α-toxins

Characterization of Amm VIII

Properties of maintained sodium current induced by a toxin from Androctonus scorpion in frog node of Ranvier.
The binding of two classes of neurotoxins to axolemma of mammalian brain

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