Angiotensin I, human

In response to lowered blood pressure, the renin enzyme cleaves angiotensin-1 from angiotensin. Angiotensin-converting enzyme (ACE) removes a dipeptide to yield the physiologically active peptide angiotensin-2, the most potent pressor substance known, which helps regulate volume and mineral balance of body fluids.

Angiotensin I, human is a synthetic research peptide in the angiotensin peptide family. The renin-angiotensin system generates bioactive peptides by sequential proteolysis. Angiotensin I is converted by ACE to angiotensin II, while shorter metabolites such as angiotensin III and angiotensin IV have distinct receptor and enzymatic contexts. Exact residue numbering is therefore essential.

• ACE substrate and inhibition studies
• angiotensin receptor assays
• renin-angiotensin processing studies
• fragment structure-activity comparisons

The exact sequence, residue range, species, terminal state, and chemical modifications should be matched to the intended assay. Fragmentation or processing can materially alter receptor selectivity, potency, aggregation, or enzymatic behavior.

1. Angiotensin peptide processing literature