Hainantoxin-IV

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Potent blocker of voltage-gated sodium channels

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). Hainantoxin-IV 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.

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Description

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%

ProTx-IProTx-IIProTx-II-Biotin
Huwentoxin-IHuwentoxin-IVGsAF-2
Hainantoxin-IIIJingzhaotoxin-IIIGsAF-1
Phrixotoxin-3μ-conotoxin-PIIIA

A positively charged surface patch is important for hainantoxin-IV binding to voltage-gated sodium channels

Structure--activity relationships of hainantoxin-IV and structure determination of active and inactive sodium channel blockers.

Isolation and characterization of hainantoxin-IV, a novel antagonist of tetrodotoxin-sensitive sodium channels from the Chinese bird spider Selenocosmia hainana.

Inhibition of neuronal tetrodotoxin-sensitive Na+ channels by two spider toxins: hainantoxin-III and hainantoxin-IV.

Determination of disulfide bridges of two spider toxins: Hainantoxin-III and Hainantoxin-IV

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    Hainantoxin-IV

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