Angiotensin II peptide

Angiotensin II peptide

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

Batch to batch variation of the purity

DRVYIHPF

H-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-OH

8

95.4%

C₅₀H₇₁N₁₃O₁₂

1046.19

4474-91-3

Synthetic

Powder

Angiotensin II is the major biologically active component of the renin-angiotensin system. Its activities include the regulation of blood pressure, salt and water balance, and vascular tonus. Ang II stimulates various enzymes as NADPH oxidase.Ang II is often used as a model compound in the development and evaluation of analytical methods for peptides and proteins (e.g. MS).

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

• A.W.A.Hahn et al., J. Cardiovasc. Pharmacol., 22 (Suppl.5), S37 (1993)
• M.de Gasparo et al., Pharmacol. Rev., 52, 415 (2000)

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.