TAT-QFNP12 peptide

TAT-QFNP12 peptide

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

H-YGRKKRRQRRRVKKEAELDKYLE-OH

H-Tyr-Gly-Arg-Lys-Lys-Arg-Arg-Gln-Arg-Arg-Arg-Val-Lys-Lys-Glu-Ala-Glu-Leu-Asp-Lys-Tyr-Leu-Glu-OH

23

95.97%

C₁₃₀H₂₂₅N₄₇O₃₅

3006.46

Synthetic

Powder

TAT-QFNP12 is a peptide corresponding to the 302 to 313 amino acid domain of the protein phosphatase PPM1A, made cell permeable by the addition of TAT, and is a key fragment involved in the binding of PPM1A to the cytoplasmic protein NDRG2. TAT-QFNP12 blockade of the binding of NDRG2 with PPM1A allows PPM1A to enter the nucleus and dephosphorylate Smad2/3, preventing transcription and production of matrix metalloproteinase 9 (MMP-9). Unwanted increased levels of MMP-9 have an important part in blood-brain barrier (BBB) injury in subarachnoid haemorrhage (SAH) and can critically exacerbate poor prognosis. In mouse models of SAH, TAT-QFNP12 dose-dependently inhibits MMP-9 expression and Smad2/3 phosphorylation, and significantly reduces brain edema and neurological deficits, demonstrating that TAT-QFNP12 can protect the blood-brain barrier after SAH and alleviate secondary nerve injury.

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

• Feng et al (2022) Astrocytic NDRG2-PPM1A interaction exacerbates blood-brain barrier disruption after subarachnoid hemorrhage. Sci Adv. 8(39) eabq2423 PMID: 36179025

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.