RVG15 peptide

RVG15 peptide

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

H-YTIWCDIFTDSRQKR-OH

H-Tyr-Thr-Ile-Trp-Cys-Asp-Ile-Phe-Thr-Asp-Ser-Arg-Gln-Lys-Arg-OH

15

95.24%

C₈₆H₁₃₀N₂₄O₂₅S

1932.15

Synthetic

Powder

RVG15 is a derivative peptide of the rabies virus glycoprotein (RVG). It is known for its ability to bind specifically to the nicotinic acetylcholine receptor (nAChR), which is widely overexpressed on the blood-brain barrier (BBB) and glioma cells. This property of RVG15 is utilized to facilitate the delivery of drugs across the BBB, thereby enhancing their accumulation in brain tumors like glioma.

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

• Xin X, Liu W, Zhang ZA, Han Y, Qi LL, Zhang YY, Zhang XT, Duan HX, Chen LQ, Jin MJ, Wang QM, Gao ZG, Huang W. Efficient Anti-Glioma Therapy Through the Brain-Targeted RVG15-Modified Liposomes Loading Paclitaxel-Cholesterol Complex. Int J Nanomedicine. 2021 Aug 24;16:5755-5776. doi: 10.2147/IJN.S318266. PMID: 34471351; PMCID: PMC8403987.

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.