CPP-Morn3 (222-237) peptide

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

A designed peptide that regulates two types of post-translational modifications of p53 with anti-cancer effect, based on the identification of a Morn3-mediated protein complex that confers composite modifications on p53. The findings highlight a strategy for targeting composite protein modifications with one molecule.

• Liang, L., Wang, H., Shi, H., Li, Z., Yao, H., Bu, Z., u2026 Xu, J. (2018). A Designed Peptide Targets Two Types of Modifications of p53 with Anti-cancer Activity. Cell Chemical Biology, 25(6), 761u2013774.e5. doi:10.1016/j.chembiol.2018.03.010
• Tan, J., Cheong, H., Park, Y.S., Kim, H., Zhang, M., Moon, C., and Huang, Y. (2014).Cell-penetrating peptide-mediated topical delivery of bio-macromolecular drugs. Curr. Pharm. Biotechnol. 15, 231u2013239.

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.