TGF-β1-simulating CM peptide

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

Batch to batch variation of the purity

• LIANAK peptide, named CM, is an oligopeptide with significant potential in the field of cartilage regeneration.
• This peptide is a member of the cytomodulins family and has been reported to mimic certain bioactivities of TGF-β1. It contains fewer than 10 amino acids, which makes it cost-effective for synthesis and shows great promise in translational medicine and tissue engineering. Previous studies have shown that CM-encapsulated cream can improve tissue tensile strength, epithelization, collagen deposition, and angiogenesis in a rat skin wound model. However, the rapid diffusion of soluble CM peptides limits its effectiveness, highlighting the need for a suitable carrier. For example, it can be combined with the self-assembling peptide RAD to form a functionalized RAD-CM SAP. The resulting peptide mixture assembled into an interwoven nanofiber network, and the R/C hydrogel demonstrated good in vitro biocompatibility and chondrogenic bioactivity, as evidenced by increased expressions of chondrogenic genes and enhanced cartilage matrix secretion. Overall, LIANAK peptide offers a promising approach for cartilage repair and regeneration, although further research is needed to fully understand its mechanisms and optimize its performance.

• Ye W, Yang Z, Cao F, Li H, Zhao T, Zhang H, Zhang Z, Yang S, Zhu J, Liu Z, Zheng J, Liu H, Ma G, Guo Q, Wang X. Articular cartilage reconstruction with TGF-β1-simulating self-assembling peptide hydrogel-based composite scaffold. Acta Biomater. 2022 Jul 1;146:94-106. doi: 10.1016/j.actbio.2022.05.012. Epub 2022 May 10. PMID: 35552000.

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.