Angiotensin I/II 1-6 contains the amino acids 1-6 and is converted from Angiotensin I/II peptide. Angiotensin I is formed by the action of renin on angiotensinogen. Angiotensin II is produced from angiotensin I. Angiotensin II has been investigated for the treatment, basic science, and diagnostic of Hypertension, Renin Angiotensin System, and Idiopathic Membranous Nephropathy.
CAT No: R1199
CAS No:47896-63-9
Synonyms/Alias:Angiotensin I/II 1-6;Angiotensin I/II (1-6);47896-63-9;(3S)-3-amino-4-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S,3S)-1-[[(1S)-1-carboxy-2-(1H-imidazol-5-yl)ethyl]amino]-3-methyl-1-oxopentan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-4-oxobutanoic acid;Angiotensin i/ii(1-6);Asp-Arg-Val-Tyr-Ile-His;HY-P1829;AKOS040764047;DA-61062;FA108793;TS-10414;CS-0096103;H-Asp-Arg-Val-Tyr-Ile-His-OH; H-DRVYIH-OH;(3S)-3-AMINO-3-{[(1S)-4-CARBAMIMIDAMIDO-1-{[(1S)-1-{[(1S)-1-{[(1S,2S)-1-{[(1S)-1-CARBOXY-2-(1H-IMIDAZOL-4-YL)ETHYL]CARBAMOYL}-2-METHYLBUTYL]CARBAMOYL}-2-(4-HYDROXYPHENYL)ETHYL]CARBAMOYL}-2-METHYLPROPYL]CARBAMOYL}BUTYL]CARBAMOYL}PROPANOIC ACID;
Angiotensin I/II 1-6 is a synthetic peptide fragment derived from the N-terminal sequence of both angiotensin I and angiotensin II, comprising the first six amino acids of these key regulators within the renin-angiotensin system. As a truncated peptide, it offers a unique tool for dissecting the structure-activity relationships of angiotensin peptides and provides insight into the functional domains responsible for receptor binding and downstream signaling. Its biochemical relevance extends to cardiovascular, renal, and endocrine research, where the modulation of angiotensin pathways is of central importance. The availability of this defined peptide fragment enables precise experimental manipulation and targeted investigation of peptide-mediated mechanisms in physiological and pathological contexts.
Receptor binding studies: Angiotensin I/II 1-6 is widely used in receptor binding assays to delineate the essential residues required for interaction with angiotensin receptors, particularly the AT1 and AT2 subtypes. By employing this fragment in competitive binding experiments, researchers can map binding affinities, identify critical contact points, and distinguish the minimal sequence necessary for receptor activation or inhibition. Such studies are fundamental for elucidating the molecular determinants of ligand-receptor specificity within the renin-angiotensin system.
Signal transduction research: The peptide fragment serves as a valuable probe for investigating the initiation and modulation of intracellular signaling cascades triggered by angiotensin receptor engagement. Utilizing angiotensin I/II 1-6 in cell-based assays allows for the assessment of its ability to activate or antagonize canonical pathways such as phospholipase C, MAPK, or calcium mobilization. These experiments help clarify how truncated peptides influence downstream physiological responses and contribute to the broader understanding of angiotensin signaling dynamics.
Peptide structure-activity relationship analysis: As a well-defined N-terminal segment, angiotensin I/II 1-6 is instrumental in systematic structure-activity relationship (SAR) studies. Researchers employ this peptide to compare biological activity profiles with those of longer or modified angiotensin analogs, thereby pinpointing the contributions of specific residues to functional potency and selectivity. SAR investigations using this fragment can inform the rational design of new peptide-based modulators with tailored properties for research and development applications.
Enzymatic processing and metabolism studies: The peptide is frequently utilized as a substrate in enzymatic assays to examine the activity, specificity, and kinetics of proteases involved in angiotensin metabolism, such as aminopeptidases and carboxypeptidases. By monitoring the degradation or modification of angiotensin I/II 1-6, scientists can characterize enzyme-substrate interactions, identify cleavage sites, and investigate the generation of bioactive peptide fragments. Such work provides critical insights into the regulation of peptide hormone turnover in physiological systems.
Analytical method development: Angiotensin I/II 1-6 is also applied as a reference standard or calibration peptide in the development and validation of analytical techniques, including high-performance liquid chromatography (HPLC), mass spectrometry, and immunoassays. Its defined sequence and physicochemical properties make it suitable for optimizing detection sensitivity, quantification accuracy, and assay reproducibility. These applications support rigorous quality control and enable reliable measurement of angiotensin-related peptides in diverse biological and experimental samples.
2. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes
3. Urinary Metabolites Associated with Blood Pressure on a Low-or High-Sodium Die
5. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
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