tatM2NX peptide

tatM2NX peptide

• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

H-YGRKKRRQRRRGSREPGEMLPRKLKRVLRQEFWV-OH

H-Tyr-Gly-Arg-Lys-Lys-Arg-Arg-Gln-Arg-Arg-Arg-Gly-Ser-Arg-Glu-Pro-Gly-Glu-Met-Leu-Pro-Arg-Lys-Leu-Lys-Arg-Val-Leu-Arg-Gln-Glu-Phe-Trp-Val-OH

34

95.46%

C₁₉₀H₃₂₃N₇₁O₄₅S

4354.09

Synthetic

Powder

tatM2NX is a peptide generated by fusing part of the C-terminus of transient receptor potential melastin 2 (TRPM2) channels, corresponding more than 90% with the Nudix domain (M2NX), with the tat inducer of HIV. tatM2NX is a TRPM2 antagonist which prevents ligand binding and TRPM2 activation, and inhibits over 90% of human TRPM2 channel currents at concentrations as low as 2 μM. tatM2NX is an antagonist with an IC50 of 396 nM and is neuroprotective in animal models of focal and global ischemia.

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. For more details, please refer to the manual:Handling and Storage of Synthetic Peptides

• Shimizu et al (2016) Extended therapeutic window of a novel peptide inhibitor of TRPM2 channels following focal cerebral ischemia. Exp Neurol. 283(Pt A) 151 PMID: 27317297
• Cruz-Torres et al (2020) Characterization and Optimization of the Novel Transient Receptor Potential Melastatin 2 Antagonist tatM2NX. Mol Pharmacol. 97(2) 102 PMID: 31772034

Trifluoroacetic acid (TFA) has a significant impact on peptides due to its role in the peptide synthesis process.

TFA is essential for the protonation of peptides that lack basic amino acids such as Arginine (Arg), Histidine (His), and Lysine (Lys), or ones that have blocked N-termini. As a result, peptides often contain TFA salts in the final product.

TFA residues, when present in custom peptides, can cause unpredictable fluctuations in experimental data. At a nanomolar (nM) level, TFA can influence cell experiments, hindering cell growth at low concentrations (as low as 10 nM) and promoting it at higher doses (0.5–7.0 mM). It can also serve as an allosteric regulator on the GlyR of glycine receptors, thereby increasing receptor activity at lower glycine concentrations.

In an in vivo setting, TFA can trifluoroacetylate amino groups in proteins and phospholipids, inducing potentially unwanted antibody responses. Moreover, TFA can impact structure studies as it affects spectrum absorption.