Hainantoxin-IV

Toxin properties

Hainantoxin-IV (HNTX-IV) is a peptide that was originally isolated from the venom of the Chinese bird spider Ornithoctonus hainana Liang (Selenocosmia hainana Liang). It has been reported that this peptide is a potent antagonist of tetrodotoxin-sensitive (TTX-S) voltage-gated sodium channels (VGSCs). It binds to TTX-S with an IC₅₀value of 34 nM in adult rat dorsal root ganglion (DRG) neurons. Tetrodotoxin-resistant (TTX-R) voltage-gated sodium channels are not affected by hainantoxin IV. It probably interacts with the site 1 through a mechanism quite similar to that of TTX without affecting the activation and inactivation kinetics.

Product specifications

AA sequence: Glu-Cys²-Leu-Gly-Phe-Gly-Lys-Gly-Cys⁹-Asn-Pro-Ser-Asn-Asp-Gln-Cys¹⁶-Cys¹⁷-Lys-Ser-Ser-Asn-Leu-Val-Cys²⁴-Ser-Arg-Lys-His-Arg-Trp-Cys³¹-Lys-Tyr-Glu-Ile-NH2
(Disulfide bonds between Cys²-Cys¹⁷, Cys⁹-Cys²⁴, and Cys¹⁶-Cys³¹)
Length (aa): 35
Formula: C₁₆₆H₂₅₇N₅₃O₅₀S₆
Molecular Weight: 3987.6 Da
Appearance: White lyophilized solid
Solubility: water and saline buffer
CAS number: Not available
Source: Synthetic
Purity rate: > 97%

Prices & Quantities

Other quantities available upon request

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References

• Dongling Li, et al. (2004) Structure-Activity Relationships of Hainantoxin-IV and Structure Determination of Active and Inactive Sodium Channel Blockers, JBC Papers in Press. PubMed link
• Liu Z, et al. (2003) Isolation and characterization of hainantoxin-IV, a novel antagonist of tetrodotoxin-sensitive sodium channels from the Chinese bird spider Selenocosmia hainana, Cell Mol Life Sci. PubMed link
• Liu Y, et al. (2012) A positively charged surface patch is important for hainantoxin-IV binding to voltage-gated sodium channels. J Pept Sci. PubMed link
• Wang W., et al. (2009) Determination of disulfide bridges of two spider toxins: Hainantoxin-III and Hainantoxin-IV. J Venom Anim Toxins incl Trop Dis. PubMed link