T100-Mut peptide

T100-Mut peptide

• COA/MS/HPLC Report
• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

Myrisitic Acid-WKVRQRNKKVQQQESQTALVVNQRCLFA-OH

Myrisitic Acid-Trp-Lys-Val-Arg-Gln-Arg-Asn-Lys-Lys-Val-Gln-Gln-Gln-Glu-Ser-Gln-Thr-Ala-Leu-Val-Val-Asn-Gln-Arg-Cys-Leu-Phe-Ala-OH

28

95.8%

C₁₆₁H₂₇₁N₄₉O₄₂S

3597.23

Synthetic

Powder

T100-Mut is a cell permeable peptide which enhances the association of TRPA1 and TRPV1 and strongly inhibits TRPA1 associated pain. The design of T100-Mut originated from Tmem100, a 134-amino acid protein found in dorsal root ganglia (DRG), co-expressed with TRPA1 and TRPV1 with which it forms a complex. Tmem100 decreases the interaction between TRPA1 and TRPV1, whereas a Tmem100 mutant, Tmem100-3Q, exerts the opposite effect and enhances the association of TRPA1 and TRPV1 to inhibit TRPA1. T100-Mut contains the C-terminal sequence of Tmem100-3Q and mimicks the effect of full-length Tmem100-3Q, inhibiting TRPA1-mediated activity and pain in a TRPV1-dependent manner. T100-Mut is also effective in animal models of pain.

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

• Weng et al (2014) Tmem100 is a regulator of TRPA1-TRPV1 complex and contributes to persistent pain. Neuron 85(4) 833 PMID: 25640077

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.