CES peptide (Cyclic)

CES peptide (Cyclic)

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

Batch to batch variation of the purity

Ac-CESPLLSEC-NH2 (disulfide bond: Cys1-Cys9)

Ac-Cys-Glu-Ser-Pro-Leu-Leu-Ser-Glu-Cys-NH2 (disulfide bond: Cys1-Cys9)

9

95.49%

C₃₉H₆₃N₉O₁₆S₂

978.09

Synthetic

Powder

CES (CESPLLSEC) is a synthetic cyclic peptide stabilized by a disulfide bond engineered for selective targeting of glioblastoma. Its cyclic structure enhances stability and binding specificity, enabling recognition of aberrantly exposed SNAP25 isoforms on glioblastoma cell surfaces—a protein typically confined to intracellular compartments. This tumor-selective interaction, demonstrated in preclinical models, drives preferential accumulation in glioblastoma tissues. The peptide’s design combines hydrophobic and polar residues to optimize membrane engagement and target affinity. As a precision oncology tool, CES can potentially provide therapeutic delivery or diagnostic imaging in glioblastoma, leveraging its ability to exploit tumor-specific protein dysregulation. Further studies are needed to validate clinical efficacy.

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

• Arias, Alberto G.; Tovar-Martinez, Laura; Asciutto, Eliana K.; Mann, Aman; Põšnograjeva, Kristina; Gracia, Lorena Simón; et al. (2024). A Cyclic Peptide Targets Glioblastoma by Binding to Aberrantly Exposed SNAP25. ACS Publications. Collection. https://doi.org/10.1021/acs.molpharmaceut.4c00958

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.