Transferrin Receptor Targeting Peptide T12

Transferrin Receptor Targeting Peptide T12

• COA/MS/HPLC Report
• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

H-THRPPMWSPVWP-OH

H-Thr-His-Arg-Pro-Pro-Met-Trp-Ser-Pro-Val-Trp-Pro-OH

12

95.2%

C₇₁H₉₉N₁₉O₁₅S

1490.72

Synthetic

Powder

Transferrin receptor (TfR), is a transmembrane glycoprotein involved in cellular iron trafficking after interaction with its native iron-rich ligand, transferrin (Tf). Of the two TfR subtypes, theTfR2 is abundantly expressed in glioblastomas and their associated vasculature. Using the M13-phage screening on chicken embryo fibroblasts constitutively expressing the human transferrin receptor (hTfR), peptides T7 (HAIYPRH) and T12 (THRPPMWSPVWP) were discovered. Both peptides have been widely used to target several cancer types overexpressing transferrin receptors (TfR1 and TfR2), including liver, prostate, breast, pancreatic cancers, and many others. T12 showed higher affinity, in nanomolar range, towards the target and appeared more promising than the T7 peptide. However, T12 failed to show enhanced transport of conjugated compounds across the BBB.

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

• Wängler, C. et al. Mol Imaging Biol doi: 10.1007/s11307-010-0329-6, (2010).

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.