SML3140
GsMTx4 trifluoroacetate
≥95% (HPLC)
Synonym(s):
1-amino-Cy5-glucose, Cyanine-based 1-amino-1-deoxy-β-glucose conjugate, Cy5-linked 1amino-glucose, GCLEFWWKCNPNDDKCCRPKLKCSKLFKLCNFSF-NH2 trifluoroacetate(Disulfide: 2-17, 9-23, 16-30), Gly-Cys-Leu-Glu-Phe-Trp-Trp-Lys-Cys-Asn-Pro-Asn-Asp-Asp-Lys-Cys-Cys-Arg-Pro-Lys-Leu-Lys-Cys-Ser-Lys-Leu-Phe-Lys-Leu-Cys-Asn-Phe-Ser-Phe-NH2 trifluoroacetate (Disulfide: 2-17, 9-23, 16-30), Grammostola Mechanotoxin #4 trifluoroacetate, GsMTx-4 trifluoroacetate, L-GsMTx trifluoroacetate
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General description
Grammostola mechanotoxin #4 (GsMTx4), a gating modifier peptide, is obtained from spider venom. This 34-amino-acid peptide is a small (3-5 kD) amphipathic molecule built on a conserved inhibitory cysteine-knot (ICK) backbone. The structure of GsMTx4 has a belt of charged residues surrounding a hydrophobic patch. GsMTx4 acts as an inhibitor of cationic mechanosensitive channels (MSCs) belonging to the Piezoand transient receptor potential (TRP) channel families. It is different from other spider venom peptides because it can inhibit these channels regardless of their shape, and both its L- and D-forms can have this effect. GsMTx4 has a unique structure and carries a positive charge due to its six lysine residues which can affect membrane binding. This peptide has become a valuable tool in research to identify the roles of excitatory MSCs in normal physiology and pathology. It can also inhibit stretch-activated big potassium channels (SAKcaC). The presence of positively charged residues in GsMTx4 is thought to play a role in peptide channel-lipid interaction. It can effectively reduce arrhythmias by inhibiting stretch-activated channels (SACs) in the heart. GsMTx4 also serves as an inhibitor of histone acetylation inhibitor I-BET 762 and Piezo 1 inhibitor.
Application
GsMTx4 trifluoroacetate has been used in drug treatment as a supplement in cell culture medium to treat mouse hippocampal neurons to block cationic MSCs in cortical neurons. It has also been used as a specific inhibitor to incubate cementoblasts to study its effects on the response of cementoblasts to investigate if cementum repair was impaired by compression.
Biochem/physiol Actions
GsMTx4 (Grammostola Mechanotoxin #4) is a tarantula venom-derived 34-mer amphipathic cysteine knot peptide that exerts its cationic mechanosensitive channels (MSCs; stretch-gated ion channels or SACs) modulatory activity by changing local membrane properties near the channels. GsMTx4 negatively regulates TRPC1/5/6 and Piexo1/2, while potentiating TREK-1 and TRPA1 activity. In addition, GsMTx4 can either hamper (2-4 μM) or facilitate (12-20 μM) the gating of prokaryotic E. coli cytoplasmic membrane MscS and MscK in a biphasic manner. GsMTx4 is also reported to inhibit Nav1.1 (SCN1A), Nav1.2 (SCN2A), Nav1.3 (SCN3A), Nav1.4 (SCN4A), Nav1.5 (SCN5A), Nav1.6 (SCN8A), Nav1.7 (SCN9A), hERG1/2/3 (KCNH2/6/7), but not hKV1.1 (KCNA1) or hKV1.4 (KCNA4).
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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A Fabian et al.
Pflugers Archiv : European journal of physiology, 457(2), 475-484 (2008-06-11)
Cell migration depends on the generation of structural asymmetry and on different steps: protrusion and adhesion at the front and traction and detachment at the rear part of the cell. The activity of Ca(2+) channels coordinate these steps by arranging
T M Suchyna et al.
The Journal of general physiology, 115(5), 583-598 (2000-04-25)
We have identified a 35 amino acid peptide toxin of the inhibitor cysteine knot family that blocks cationic stretch-activated ion channels. The toxin, denoted GsMTx-4, was isolated from the venom of the spider Grammostola spatulata and has <50% homology to
Annette C Hurst et al.
European biophysics journal : EBJ, 38(4), 415-425 (2009-01-10)
The spider peptide GsMTx4, at saturating concentration of 5 muM, is an effective and specific inhibitor for stretch-activated mechanosensitive (MS) channels found in a variety of eukaryotic cells. Although the structure of the peptide has been solved, the mode of
Elisa Redaelli et al.
The Journal of biological chemistry, 285(6), 4130-4142 (2009-12-04)
Venom-derived peptide modulators of ion channel gating are regarded as essential tools for understanding the molecular motions that occur during the opening and closing of ion channels. In this study, we present the characterization of five spider toxins on 12
Chilman Bae et al.
Biochemistry, 50(29), 6295-6300 (2011-06-24)
Cells can respond to mechanical stress by gating mechanosensitive ion channels (MSCs). The cloning of Piezo1, a eukaryotic cation selective MSC, defines a new system for studying mechanical transduction at the cellular level. Because Piezo1 has electrophysiological properties similar to
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