TAT-Y127WT peptide

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

The TAT-Y127WT peptide, chemically identified as YGRKKRRQRRR-itqvYgfyd-FITC, represents a significant advancement in the study of idiopathic pulmonary fibrosis (IPF) treatment. This peptide acts as an inhibitor of protein phosphatase 2 A (PP2A), a factor implicated in the pathogenesis of IPF, particularly in relation to endothelial-mesenchymal transition (EndMT), a process involved in the development of this condition.

Recent studies have highlighted the role of PP2A in promoting EndMT, suggesting that inhibiting this enzyme could offer therapeutic benefits. TAT-Y127WT has been designed and synthesized specifically to investigate and validate the role of PP2A in pulmonary fibrosis. In experimental models, particularly those involving bleomycin (BLM)-induced pulmonary fibrosis in mice, TAT-Y127WT has demonstrated protective effects. It has been shown to effectively reduce lung injury and fibrosis. Additionally, mechanistic studies have indicated that TAT-Y127WT can alleviate EndMT following BLM induction.

Its efficacy in experimental models positions it as a promising candidate for new anti-fibrotic therapies aimed at treating IPF patients

• Yu J, Deng Y, Han M. Blocking protein phosphatase 2A with a peptide protects mice against bleomycin-induced pulmonary fibrosis. Exp Lung Res. 2020 Sep;46(7):234-242. doi: 10.1080/01902148.2020.1774823. Epub 2020 Jun 25. PMID: 32584210.

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.