GsMTx4

Selective blocker of mechanosensitive ion channels

GsMTx4 (GsMTx-4, M-theraphotoxin-Gr1a) has been isolated from the venom of the spider Grammostola rosea. This cationic hydrophobic polypeptide blocks selectively the gating of cation selective channels and mechanosensitive ion channels such as TRPC1 or TRPC6, without having any effect on whole-cell voltage-sensitive currents. This toxin acts by perturbing the interface between the channel and the lipid bilayer without necessarily being in physical contact with the channel. GsMTx4 also demonstrated to active TRPA1 channel at 1µM concentration and to inhibit Piezo1 currents.

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Product code: N/A. Categories: , . Tags: , , .

AA sequence: Gly-Cys2-Leu-Glu-Phe-Trp-Trp-Lys-Cys9-Asn-Pro-Asn-Asp-Asp-Lys-Cys16-Cys17-Arg-Pro-Lys-Leu-Lys-Cys23-Ser-Lys-Leu-Phe-Lys-Leu-Cys30-Asn-Phe-Ser-Phe-NH2
Disulfide bonds: Cys2-Cys17, Cys9-Cys23 and Cys16-Cys30
Length (AA): 34
Formula: C185H273N49O45S6
Molecular Weight: 4095.2 Da
Appearance: White lyophilized solid
Solubility: water and saline buffer
CAS number:
Source: Synthetic
Purity rate: > 97 %

  • NMB-1: selective blocker of SA mechanosensitive ion channels
Citations
Synergy between Piezo1 and Piezo2 channels confers high-strain mechanosensitivity to articular cartilage

The Mechanosensitive Ion Channel Piezo1 Is Inhibited by the Peptide GsMTx4

Molecular dynamics simulations of a stretch-activated channel inhibitor GsMTx4 with lipid membranes: two binding modes and effects of lipid structure

Localization of the voltage-sensor toxin receptor on KvAP

cDNA sequence and in vitro folding of GsMTx4, a specific peptide inhibitor of mechanosensitive channels

Solution structure of peptide toxins that block mechanosensitive ion channels

Identification of a peptide toxin from Grammostola spatulata spider venom that blocks cation-selective stretch-activated channels