rytvela peptide

rytvela peptide

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

Batch to batch variation of the purity

H-RYTVELA-OH, All amino acids are D isomers

H-Arg-Tyr-Thr-Val-Glu-Leu-Ala-OH, All amino acids are D isomers

7

95.8%

C₃₈H₆₂N₁₀O₁₂

850.95

Synthetic

Powder

rytvela is an all D peptide derived from an extracellular loop region of the interleukin-1 receptor accessory protein (IL-1RAcP), which acts as an allosteric negative modulator of the interleukin-1 receptor (IL-1R). In vitro, rytvela is specific, potent and effective and blocks human thymocyte proliferation with an IC50 of 1 nM, Rytvela does not significantly inhibit NF-κB, but instead it selectively inhibits the IL-1R downstream stress associated protein kinases/transcription factor c-jun and Rho GTPase/Rho-associated coiled coil containing protein kinase signaling pathways. In vivo rytvela is active in models of hyperthermia and inflammatory bowel disease and topically in contact dermatitis.

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

• Quiniou et al (2008) Development of a novel noncompetitive antagonist of IL-1 receptor. J Immunol. 180(10) 6977 PMID: 18453620
• Dabouz (2020) An allosteric interleukin-1 receptor modulator mitigates inflammation and photoreceptor toxicity in a model of retinal degeneration. J Neuroinflammation. 17(1) 359 PMID: 33246504
• Takahashi (2021) Direct administration of the non-competitive interleukin-1 receptor antagonist rytvela transiently reduced intrauterine inflammation in an extremely preterm sheep model of chorioamnionitis. PLoS One 16(9) e0257847 PMID: 34559862

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.