Myr-tat-CBD3 peptide

Myr-tat-CBD3 peptide

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

Myrisitic Acid-YGRKKRRQRRRARSRLAELRGVPRGL-OH

Myrisitic Acid-Tyr-Gly-Arg-Lys-Lys-Arg-Arg-Gln-Arg-Arg-Arg-Ala-Arg-Ser-Arg-Leu-Ala-Glu-Leu-Arg-Gly-Val-Pro-Arg-Gly-Leu-OH

26

95.42%

C₁₄₈H₂₆₉N₅₉O₃₃

3403.08

Synthetic

Powder

Myr-tat-CBD3 is the N-terminal myristoylated version of TAT-CBD3 (PN-160), a peptide derived from the axonal collapsin response mediator protein 2 (CRMP-2). The myristoyl group allows insertion of myr-tat-CBD3 into membranes through hydrophobic interactions and myr-tat-CBD3 is membrane tethered, restricts the CaV2.2–CRMP2 interaction, blocks CaV2.2 trafficking, and strongly inhibits Ca2+ influx from primary sensory neurons. Intrathecal injection of myr-tat-CBD3 reduces carrageenan-induced inflammation and reverses paw incision–induced thermal and mechanical hypersensitivity without producing rewarding behaviour.

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

• Brittain et al (2011) Suppression of inflammatory and neuropathic pain by uncoupling CRMP-2 from the presynaptic Ca2+ channel complex. Nature Med. 17(7) 822 www.ncbi.nlm.nih.gov/pmc/articles/PMC3219927/
• Fischer et al (2014) Sustained relief of neuropathic pain by AAV-targeted expression of CBD3 peptide in rat dorsal root ganglion. Gene Ther. 21(1) 44 doi:10.1038/gt.2013.56
• François-Moutal eta al (2015) A membrane-delimited N-myristoylated CRMP2 peptide aptamer inhibits CaV2.2 trafficking and reverses inflammatory and postoperative pain behaviors. Pain 156(7) 1247 doi: 10.1097/j.pain.0000000000000147

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.