Sarilesin peptide

Sarilesin peptide

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

Batch to batch variation of the purity

XRVYIHPI, X is sarcosine

Sar-Arg-Val-Tyr-Ile-His-Pro-Ile-OH

7

95.42%

C₄₆H₇₃N₁₃O₁₀

968.17

Synthetic

Powder

Sarilesin, also known as [Sar1,Ile8]-angiotensin II, is a specific antagonist at angiotensin receptors. Sarilesin has multiple effects on vascular smooth muscle, including contraction of normal arteries and hypertrophy or hyperplasia of cultured cells or diseased vessels. Sarilesin activates both the NADPH and NADH oxidases, and stimulates superoxide anion formation in vascular smooth muscle cells.

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

• Obermüller et al (1991) Distribution of angiotensin II receptor subtypes in rat brain nuclei. Neurosci. Lett. 132(1) 11 PMID: 1787912
• Matsoukas et al (1993) Synthesis and biological activities of angiotensin II, Sarilesin, and Sarmesin analogues containing Aze or Pip at position 7. J. Med. Chem. 1993 36(7) 904 PMID: 8464045

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.