Angiotensin II (5-8), human is an endogenous C-terminal fragment of the peptide vasoconstrictor angiotensin II. Angiotensin II binds the AT II type 1 (AT1) receptor, stimulating GPCRs in vascular smooth muscle cells and increasing intracellular Ca2+ levels. Angiotensin II also acts at the Na+/H+ exchanger in the proximal tubules of the kidney.
CAT No: R1202
CAS No:34233-50-6
Synonyms/Alias:Angiotensin I/II (5-8);34233-50-6;Angiotensin II (5-8), human;Angiotensin (5-8);(2S)-2-[[(2S)-1-[(2S)-2-[[(2S,3S)-2-amino-3-methylpentanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]pyrrolidine-2-carbonyl]amino]-3-phenylpropanoic acid;CTK1B7855;MFCD00167499;Angiotensin-(5-8);DTXSID40430963;CHEBI:144396;HY-P1769;Angiotensin I/II (5-8) TFA salt;FA109100;MS-29518;CS-0095581;C20972;G12438;Angiotensin I/II (5-8) (H-Ile-His-Pro-Phe-OH);H-Ile-His-Pro-Phe-OH TFA salt; H-IHPF-OH TFA salt;
Angiotensin II (5-8), human, is a synthetic peptide fragment derived from the C-terminal region of the native human angiotensin II octapeptide. Comprising the last four amino acids of the full-length hormone, this tetrapeptide retains a portion of the bioactive sequence crucial for receptor interaction studies, enzymatic processing investigations, and peptide mapping. Its defined structure and origin from the renin-angiotensin system make it an important tool for dissecting peptide-receptor interactions, substrate specificity of peptidases, and downstream signaling pathways in cardiovascular and renal research. As a research-use-only reagent, Angiotensin II (5-8), human, enables precise experimental manipulation within a variety of peptide-focused scientific contexts.
Peptide-receptor interaction studies: The fragment serves as a valuable probe to investigate the minimal structural requirements for binding to angiotensin receptors, particularly the AT1 and AT2 subtypes. By comparing the biological activity and binding affinity of the tetrapeptide relative to the full-length angiotensin II, researchers can elucidate which amino acid residues are essential for receptor recognition and activation. Such studies provide insight into the structure-activity relationship within the renin-angiotensin system and contribute to the rational design of receptor agonists or antagonists.
Enzymatic cleavage and substrate specificity assays: Angiotensin II (5-8), human, is frequently employed as a substrate to characterize the activity of peptidases such as aminopeptidases, carboxypeptidases, and angiotensinases. Its defined sequence allows for detailed analysis of enzymatic cleavage patterns, kinetic parameters, and the identification of enzyme inhibitors or modulators. These assays are fundamental for understanding peptide metabolism and the regulation of bioactive peptide levels in physiological and pathophysiological states.
Peptide mapping and analytical method development: The tetrapeptide is an effective standard for developing and validating chromatographic and mass spectrometric techniques used in peptide analysis. Its well-characterized structure and physicochemical properties facilitate the optimization of separation protocols, detection sensitivity, and quantification accuracy in complex biological samples. Analytical laboratories leverage this peptide fragment to ensure robustness and reproducibility in peptide profiling workflows.
Signal transduction research: As a truncated analogue of angiotensin II, the peptide enables researchers to dissect downstream signaling pathways activated by partial receptor engagement or by-products of angiotensin II degradation. By monitoring cellular responses to the tetrapeptide, such as changes in second messenger levels or gene expression profiles, investigators can differentiate between full agonist, partial agonist, or antagonist effects and gain a deeper understanding of receptor-mediated signal transduction mechanisms.
Peptide synthesis and modification studies: Angiotensin II (5-8), human, is also utilized as a model substrate for exploring novel synthetic methodologies, post-synthetic modifications, and peptide stability assessments. Its manageable length and well-defined sequence make it suitable for evaluating coupling efficiencies, protecting group strategies, and the impact of chemical modifications on peptide conformation and function. These studies are essential for advancing peptide chemistry and for the development of custom peptide-based tools for biomedical research.
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