GsMTx4
Product ID L8427-100UG 
Name GsMTx4 
Molecular formula C185H273N49O45S6
Description
A 35 amino-acids peptide with 3 disulfide bridges , synthetic, initially isolated from the venom of the Chilean rose tarantula Grammostola rosea, also known as Grammostola spatulata.
Biological activity

A selective blocker of mechanosensitive ion channels (MSCs).


This cationic hydrophobic peptide inhibits a lot of different channels and has an antimicrobial activity.

 

Ion Channel modulator :

GsMTx4 blocks mechanosensitive ion channels (MSCs, also named stretch-activated channels or SACs), without having effect on whole-cell voltage-sensitive currents. Acts by partitioning into the membrane and perturbing the interface between the channel and the lipid bilayer without necessarily being in physical contact with the channel. Inhibits atrial fibrillation as well as the membrane motor of outer hair cells at low doses. It is especially a selective blocker of Piezo1 channels, TRPC1 and TRPC6.

It has also a medium toxicity on a large spectra of sodium channels (Nav1.1/SCN1A, Nav1.2/SCN2A, Nav1.3/SCN3A, Nav1.4/SCN4A, Nav1.5/SCN5A, Nav1.6/SCN8A, Nav1.7/SCN9A), and also inhibits potassium channels Kv11.1/KCNH2 and Kv11.2/KCNH6. It does not inhibit potassium channels Kv1.1/KCNA1, Kv1.4/KCNA4 and Kv11.3/KCNH7.

GsMTx4 shown to activate TRPA1 channel.

This toxin also binds to the voltage sensor of voltage-gated potassium channels from the archaebacterium Aeropyrum pernix (KvAP) without affecting channel gating.

 

Antimicrobial activity :

GsMTx4 has demonstrated its antimicrobial properties against Gram+ bacteria B. subtilis, S. aureus and S.epidermidis, and against Gram- bacteria S. typhimurium, P. aeruginosa, and E. coli.

 

 Packaging and Prices

Packaging Price (€) Quantité Buy Now
1 Unité(s) 90.00

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5 Unité(s) 360.00

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For quotation of big quantities, please Contact us
 Product Technical Documents
Safety Data Sheet Available on request, please Contact us
Ref. SDS_L8427-100UG : unit price : free of charge
 Chemical and Physical Properties
Product code L8427-100UG  Molecular weight 4107.81 Da
Product name GsMTx4  Physical form White lyophilized solid
CAS No. 1209500-46-8 Melting point
RTECS NA Solubility water and saline buffer
UNIPROT Q7YT39 Optical Activity
PubChem SID    
PubChem CID 90488987    
Purity > 90 %    
Toxicity(LD50) No Data    
Chemical Name    
Storage & Reconstitution
Recommandations

Stable at room temperature, store preferably at 4°C


 
Savety Recommandations  
 Bibliographic References
Product code L8427-100UG 
Product name GsMTx4 

- 1. Anderson M, et al. (2013) Opposing effects of podocin on the gating of podocyte TRPC6 channels evoked by membrane stretch or diacylglycerol. Am J Physiol Cell Physiol.
2. Bae, C.,  et al. (2011) The Mechanosensitive Ion Channel Piezo1 Is Inhibited by the Peptide GsMTx4. Biochemistry.
3. Fang J., Iwasa K.H.(2006) Effects of tarantula toxin GsMTx4 on the membrane motor of outer hair cells. Neurosci. Lett. 404:213-216
4. Lee W, et al. (2015) Synergy between Piezo1 and Piezo2 channels confers high-strain mechanosensitivity to articular cartilage. PNAS.
5. Nishizawa M, Nishizawa K. (2007) Molecular dynamics simulations of a stretch-activated channel inhibitor GsMTx4 with lipid membranes: two binding modes and effects of lipid structure. Biophys J. 92:4233-4243
6. Ono S., Kimura T., Kubo T. (2011) Characterization of voltage-dependent calcium channel blocking peptides from the venom of the tarantula Grammostola rosea. Toxicon 58:265-276
7. Ostrow, K. L., et al. (2003) cDNA sequence and in vitro folding of GsMTx4, a specific peptide inhibitor of mechanosensitive channels. Toxicon 42:263-274.
8. Oswald, R. E., et al. (2002) Solution structure of peptide toxins that block mechanosensitive ion channels. J Biol Chem.
9. Ruta, V., and MacKinnon, R. (2004) Localization of the voltage-sensor toxin receptor on KvAP, Biochemistry.
10. Suchyna T.M., et al. (2000) Identification of a peptide toxin from Grammostola spatulata spider venom that blocks cation-selective stretch-activated channels. J Gen Physiol 115:583-598
11. Suchyna T.M. et al (2004) Bilayer-dependent inhibition of mechanosensitive channels by neuroactive peptide enantiomers. Nature 430:235-240.
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