R3V6 peptide

R3V6 peptide

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

Batch to batch variation of the purity

H-RRRVVVVVV-OH

H-Arg-Arg-Arg-Val-Val-Val-Val-Val-Val-OH

9

95.84%

C₄₈H₉₂N₁₈O₁₀

1081.35

Synthetic

Powder

R3V6 is a peptide that has been investigated for its potential in drug delivery, particularly in the context of pulmonary gene delivery. R3V6 has a hydrophobic V6 stretch and a hydrophilic R3 stretch. This unique structure allows it to form stable micelles in aqueous solution. The hydrophobic part of R3V6 can interact with other hydrophobic molecules, such as cholesterol-conjugated AMO155 (AMO155c), through hydrophobic interactions. R3V6 forms stable complexes with anti-microRNA oligonucleotides (AMOs) due to charge interactions between the arginine residues in R3V6 and the oligonucleotides. In animal experiments, R3V6 has shown higher pulmonary delivery efficiency compared to polyethylenimine (PEI) with a molecular weight of 25 kDa (PEI25k). However, the R3V6/AMO complexes it forms have a positive surface charge, which can be a drawback as positively charged substances are easily captured by mucins in the mucus layer of the lungs and cleared rapidly without reaching the lung epithelial cells. This limits its delivery efficiency. To overcome this, strategies such as incorporating amphiphilic drugs like glycyrrhizic acid (GA) have been explored to modify the surface charge and improve the delivery efficiency of the R3V6-based delivery system.

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

• Kang M, Zhuang C, Oh J, Lee M. Pulmonary Delivery of Anti-microRNA Oligonucleotide and Glycyrrhizic Acid Using Ternary Peptide Micelles for the Treatment of Acute Lung Injury. Biomater Res. 2024 Nov 8;28:0107. doi: 10.34133/bmr.0107. PMID: 39524248; PMCID: PMC11544319.

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.