DTP3 peptide

DTP3 peptide

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

Batch to batch variation of the purity

Ac-yrf-NH2

Ac-D-Tyr-D-Arg-D-Phe-NH2

3

95.68%

C₂₆H₃₅N₇O₅

525.6

1809784-29-9

86295191

Synthetic

Powder

DTP3 is designed to target the GADD45β/MKK7 complex. It binds to MKK7 and dissociates the GADD45β/MKK7 complex. By doing so, it activates the JNK signal. The activation of the JNK signal is a key event that leads to the induction of apoptosis in MM cells.
This peptide shows a high degree of selectivity. It has a preferential effect on cell lines with high GADD45β expression. In other words, it can selectively kill cancer cells that overexpress GADD45β, which is a characteristic of MM cells, while having minimal impact on normal cells.
DTP3 is highly active even at low nanomolar concentrations. It can effectively kill primary MM cells derived from MM patients. Compared to other drugs like bortezomib, it has a higher therapeutic index. This means that it can achieve a better balance between killing cancer cells and sparing normal cells, offering a more promising option for the treatment of MM and potentially other cancers where the NF-κB and GADD45β/MKK7 pathways play a significant role.

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

• Tornatore L, Sandomenico A, Raimondo D, Low C, Rocci A, Tralau-Stewart C, Capece D, D'Andrea D, Bua M, Boyle E, van Duin M, Zoppoli P, Jaxa-Chamiec A, Thotakura AK, Dyson J, Walker BA, Leonardi A, Chambery A, Driessen C, Sonneveld P, Morgan G, Palumbo A, Tramontano A, Rahemtulla A, Ruvo M, Franzoso G. Cancer-selective targeting of the NF-κB survival pathway with GADD45β/MKK7 inhibitors. Cancer Cell. 2014 Oct 13;26(4):495-508. doi: 10.1016/j.ccr.2014.07.027. Erratum in: Cancer Cell. 2014 Dec 8;26(6):938. doi: 10.1016/j.ccell.2014.11.021. PMID: 25314077; PMCID: PMC4197335.

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.