NT1–20 peptide

NT1–20 peptide

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

H-GRKKRRQRRRCMELKTEEEEVGGVQPVSIQA-OH

H-Gly-Arg-Lys-Lys-Arg-Arg-Gln-Arg-Arg-Arg-Cys-Met-Glu-Leu-Lys-Thr-Glu-Glu-Glu-Glu-Val-Gly-Gly-Val-Gln-Pro-Val-Ser-Ile-Gln-Ala-OH

31

95.57%

C₁₅₀H₂₆₅N₅₅O₄₇S₂

3655.16

Synthetic

Powder

NT1–20 is a tatylated membrane penetrating peptide derived from the N-terminus of the acid sensing ion channel 1a (ASIC1a), which can block ASIC1a binding receptor interacting protein kinase 1 (RIPK1) to its C terminus. ASIC1a mediates necroptosis via recruiting RIPK1, independent of its ion-conducting function, and though this mechanism NT1-20 can protect neurons against acidosis induced necroptosis in vitro. NT1-20 can also reduce neuronal damage in mouse models of ischemic stroke.

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

• Wang et al (2020) Disruption of auto-inhibition underlies conformational signaling of ASIC1a to induce neuronal necroptosis. Nat Commun. 11(1) 475 PMID: 31980622

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.