Angiotensin (1-5) peptide

• COA/MS/HPLC Report
• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

Angiotensin (1-5) is a peptide fragment derived from the enzymatic processing of angiotensin I. Angiotensin I, a decapeptide, is cleaved by the angiotensin-converting enzyme (ACE), a peptidyl dipeptide hydrolase, which removes a C-terminal histidyl-leucine dipeptide to form the octapeptide angiotensin II. This conversion is a key step in the renin-angiotensin system. The enzyme exhibits broad specificity, hydrolyzing peptide bonds in various substrates, and requires chloride ions as a cofactor for optimal activity with certain peptides. ACE is widely distributed, with high concentrations found on vascular endothelial surfaces, particularly in the lung, and in renal proximal tubule epithelial cells.

The formation of angiotensin (1-5) involves further proteolytic cleavage of angiotensin I or II. While the provided text focuses on the conversion to angiotensin II, related enzymatic pathways can yield shorter fragments like angiotensin (1-5). This peptide is part of a cascade where sequential enzymatic actions modulate bioactive peptide profiles. The converting enzyme itself is a zinc-metallopeptidase, often membrane-bound, and its activity influences the balance between vasoactive peptides in circulation and local tissues.

• Erdös EG. Conversion of angiotensin I to angiotensin II. Am J Med. 1976 May 31;60(6):749-59. doi: 10.1016/0002-9343(76)90889-5. PMID: 190881.

Trifluoroacetic acid (TFA) is a common counterion from the purification process using High-Performance Liquid Chromatography (HPLC). The presence of TFA can affect the peptide's net weight, appearance, and solubility.

Impact on Net Weight: The TFA salt contributes to the total mass of the product. In most cases, the peptide content constitutes >80% of the total weight, with TFA accounting for the remainder.

Solubility: TFA salts generally enhance the solubility of peptides in aqueous solutions.

In Biological Assays: For most standard in vitro assays, the residual TFA levels do not cause interference. However, for highly sensitive cellular or biochemical studies, please be aware of its presence.