SP94 peptide

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

Batch to batch variation of the purity

• SP94 is a peptide ligand with high specificity for hepatocellular carcinoma cells. It was discovered through phage display technology and has shown great potential in targeted drug delivery for liver cancer treatment.
• In vitro, SP94 binds to various hepatocellular carcinoma cell lines, indicating its broad recognition ability. In vivo, it homes specifically to tumor tissues in animal models, with minimal binding to normal visceral organs. This targeted delivery is further confirmed by competitive inhibition experiments. When conjugated with liposomal doxorubicin (SP94-LD), it significantly enhances the therapeutic efficacy against hepatocellular carcinoma xenografts. SP94-LD treatment leads to increased tumor apoptosis and decreased tumor angiogenesis, resulting in suppressed tumor growth compared to non-targeted treatments. Additionally, SP94-LD shows reduced hematologic toxicities, improving the overall safety profile. Overall, SP94 holds significant promise as a key component in targeted therapies for hepatocellular carcinoma.

• Lo A., Lin C. T. & Wu H. C. Hepatocellular carcinoma cell-specific peptide ligand for targeted drug delivery. Mol Cancer Ther 7, 579-589 (2008).
• Toita R. et al. A nanocarrier based on a genetically engineered protein cage to deliver doxorubicin to human hepatocellular carcinoma cells. Chem Commun (Camb) 49, 7442-7444 (2013).
• Toita R. et al. Development of human hepatocellular carcinoma cell-targeted protein cages. Bioconjug Chem 23, 1494-1501 (2012).

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.