TKKTLRT peptide

TKKTLRT peptide

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

Batch to batch variation of the purity

H-TKKTLRT-OH

H-Thr-Lys-Lys-Thr-Leu-Arg-Thr-OH

7

95.45%

C₃₆H₇₀N₁₂O₁₁

847.01

Synthetic

Powder

TKKTLRT is a heptapeptide that belongs to the collagen-binding domain (CBD) family. CBDs are polypeptides that can bind specifically with collagens, which are structural proteins found in various tissues including tumors. The TKKTLRT peptide was designed based on the cleavage site of collagenase enzyme present in type I alpha 2 chain of collagen. It has been shown to have good tissue penetration and binding affinity towards exposed collagens within tumor tissues. When conjugated with therapeutic molecules such as antibodies or fusion proteins, TKKTLRT acts as a homing device for these molecules by targeting them specifically towards tumor cells through its interaction with exposed collagens within the tumor microenvironment. Studies have demonstrated that using TKKTLRT-conjugated therapeutics results in improved retention and efficacy at target sites while reducing off-target effects on normal cells compared to unmodified therapeutics.

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

• Liu J, Meng Z, Xu T, Kuerban K, Wang S, Zhang X, et al. A SIRPαFc Fusion Protein Conjugated With the Collagen-Binding Domain for Targeted Immunotherapy of Non-Small Cell Lung Cancer. Front Immunol. 2022

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.