T7 peptide (TFA removed)

T7 peptide (TFA removed)

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

Batch to batch variation of the purity

H-HAIYPRH-OH

H-His-Ala-Ile-Tyr-Pro-Arg-His-OH

7

98.43%

C₄₁H₆₀N₁₄O₉

893

Synthetic

Powder

T7 (HAIYPRH) peptide, a phage display-selected peptide, exhibited high binding affinity to transferrin receptor (TfR) overexpressed on tumor cells. The binding site of T7 to TfR is distinct from that of Tf, thus avoiding competitive inhibition by endogenous Tf. Moreover, endogenous Tf could facilitate the internalization of T7. T7 demonstrated potential ability as an active targeting ligand for the delivery of agents to TfR-overexpressed tumor cells.

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

• Lee JH, Engler JA, Collawn JF, Moore BA, Receptor mediated uptake of peptides that bind the human transferrin receptor, Eur J Biochem. 268 (2001) 2004-2012.
• Oh S, Kim BJ, Singh NP, Lai H, Sasaki T, Synthesis and anti-cancer activity of covalent conjugates of artemisinin and a transferrin-receptor targeting peptide, Cancer Lett. 274 (2009) 33-39.

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.