RV10 peptide

RV10 peptide

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

Batch to batch variation of the purity

H-MASLIYRQLL-OH

H-Met-Ala-Ser-Leu-Ile-Tyr-Arg-Gln-Leu-Leu-OH

10

95.3%

C₅₅H₉₄N₁₄O₁₄S

1207.48

Synthetic

Powder

RV10 peptide is a hydrophobic epitope derived from the VP8 subunit protein of rotavirus. It is a highly conserved linear B-cell epitope involved in human rotavirus neutralization. The physicochemical properties of the RV10 peptide, such as hydrophobicity and charge, can affect the expression, solubility, and stability of modular proteins. In a previous study, three different designs of the RV10 module were synthesized using synthetic biology strategies to generate stable modular capsomeres and virus-like particles (VLPs). The modularization of the murine polyomavirus VP1 with a single copy of RV10 flanked by long linkers and charged residues resulted in the expression of stable modular capsomeres. The introduction of longer flanking linkers may have alleviated structural perturbation of the capsomeres. The RV10 peptide can be used as a target for low-cost vaccine delivery against rotavirus and other target diseases.

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

• Tekewe A, Connors NK, Middelberg AP, Lua LH. Design strategies to address the effect of hydrophobic epitope on stability and in vitro assembly of modular virus-like particle. Protein Sci. 2016 Aug;25(8):1507-16. doi: 10.1002/pro.2953. Epub 2016 Jun 13. PMID: 27222486; PMCID: PMC4972206.

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.