DRI-BCL10-P4 peptide

DRI-BCL10-P4 peptide

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

DRQIKIWFQNRRMKWKKeqlydllkGarkrsstr (lower case letters are on behalf of D-amino acid)

H-Asp-Arg-Gln-Ile-Lys-Ile-Trp-Phe-Gln-Asn-Arg-Arg-Met-Lys-Trp-Lys-Lys-D-Glu-D-Gln-D-Leu-D-Tyr-D-Asp-D-Leu-D-Leu-D-Lys-Gly-D-Ala-D-Arg-D-Lys-D-Arg-D-Ser-D-Ser-D-Thr-D-Arg-OH

34

95.2%

C₁₉₄H₃₂₀N₆₄O₄₉S

4365.06

Synthetic

Powder

DRI-BCL10-P4 is a BCL10 inhibitor peptide, interacted with BCL10, effectively disrupted BCL10 filament formation, selectively suppressed the growth of CB-SMOC-dependent cell lines (HBL1, TMD8 and SU-DHL4 cells), repressed NF-κB pathway activation in HBL1 and TMD8 cells but not in OCI-LY1 cells and induced apoptosis and cell cycle arrest of TMD8 and SU-DHL4 cells in a dose-dependent manner. DRI-BCL10-P4 suppressed the growth of BCL10-dependent DLBCL tumors in vivo. DRI-BCL10-P4 at 10 mg/kg significantly suppressed the growth of the BCL10-dependent cells (TMD8 and SU-DHL6 cell lines) but not the BCL10-independent tumor cells (OCI-LY1 cell line) in transplanted mouse models.

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

• Bao W, Sun C, Sun X, et al. Targeting BCL10 by small peptides for the treatment of B cell lymphoma. Theranostics. 2020;10(25):11622-11636. Published 2020 Sep 19. doi:10.7150/thno.47533

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.