RGDFF peptide

RGDFF peptide

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

Batch to batch variation of the purity

H-RGDFF-OH

H-Arg-Gly-Asp-Phe-Phe-OH

5

95.43%

C₃₀H₄₀N₈O₈

640.68

Synthetic

Powder

RGDFF is an amphiphilic pentapeptide which could be coassemble with the thiol-activated H2S donors (CL2/3) into nanocarriers for targeted therapy of non-small-cell lung cancer. The coassembly approach simply solved the solubility issue of CL2/3 by the introduction of electron-donating groups (phenyl rings) to slow down the H2S release while dramatically improving their biocompatible interface, circulation time, slow release of H2S, and tumor targeting.

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

• Chen H, Guan X, Liu Q, Yang L, Guo J, Gao F, Qi Y, Wu X, Zhang F, Tian X. Co-assembled Nanocarriers of De Novo Thiol-Activated Hydrogen Sulfide Donors with an RGDFF Pentapeptide for Targeted Therapy of Non-Small-Cell Lung Cancer. ACS Appl Mater Interfaces. 2022 Dec 7;14(48):53475-53490. doi: 10.1021/acsami.2c14570. Epub 2022 Nov 22. PMID: 36413755.

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.