[Sar1, Ile8]-Angiotensin II is a peptide that has multiple effects on vascular smooth muscle, including contraction of normal arteries and hypertrophy or hyperplasia of cultured cells or diseased vessels.
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CAT No: R1131
CAS No:37827-06-8
Synonyms/Alias:Sar-Arg-Val-Tyr-Ile-His-Pro-Ile;67724-27-0;Angiotensin II [Sar1 Ile8];(Sar1,Ile8)-Angiotensin II;[Sar1,Ile8]-ANGIOTENSIN II;37827-06-8;[Sar1, Ile8]-Angiotensin II;2-[[1-[2-[[2-[[2-[[2-[[5-(diaminomethylideneamino)-2-[[2-(methylamino)acetyl]amino]pentanoyl]amino]-3-methylbutanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-methylpentanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]pyrrolidine-2-carbonyl]amino]-3-methylpentanoic acid;DTXSID80553928;PAN-4016-V;AKOS040759172;DA-69294;N-Methylglycyl-N~5~-(diaminomethylidene)ornithylvalyltyrosylisoleucylhistidylprolylisoleucine;2-{[1-(2-{2-[2-(2-{5-carbamimidamido-2-[2-(methylamino)acetamido]pentanamido}-3-methylbutanamido)-3-(4-hydroxyphenyl)propanamido]-3-methylpentanamido}-3-(1H-imidazol-4-yl)propanoyl)pyrrolidin-2-yl]formamido}-3-methylpentanoic acid;
[Sar1, Ile8]-Angiotensin II is a synthetic peptide analog of the endogenous octapeptide hormone angiotensin II, featuring substitutions at positions 1 and 8 with sarcosine and isoleucine, respectively. This modified peptide is widely recognized for its utility in probing the structure-activity relationships of angiotensin II receptors and dissecting the molecular mechanisms underlying the renin-angiotensin system. By altering the N-terminal and C-terminal residues, [Sar1, Ile8]-Angiotensin II exhibits distinct receptor binding characteristics and altered resistance to enzymatic degradation, making it a valuable research tool for studies in cardiovascular physiology, receptor pharmacology, and peptide signaling pathways.
Receptor Pharmacology: In receptor binding assays and functional studies, [Sar1, Ile8]-Angiotensin II serves as a potent agonist for angiotensin II type 1 (AT1) and type 2 (AT2) receptors. Its unique substitutions confer modified affinity and efficacy profiles, enabling researchers to differentiate receptor subtypes and investigate ligand-receptor interactions at a molecular level. The peptide is frequently employed to map binding sites, evaluate receptor selectivity, and quantify downstream signaling responses in various cell-based and membrane preparations.
Signal Transduction Studies: The analog is instrumental in dissecting the intracellular signaling cascades activated by angiotensin II receptor engagement. Its stability and receptor specificity facilitate the analysis of G protein-coupled receptor (GPCR) activation, second messenger generation, and kinase phosphorylation events. By comparing the signaling outcomes of [Sar1, Ile8]-Angiotensin II with those of native angiotensin II, scientists can elucidate the contributions of individual amino acid residues to receptor activation and effector coupling.
Peptide Structure-Activity Relationship (SAR) Research: Incorporation of sarcosine at position 1 and isoleucine at position 8 allows for systematic SAR investigations. The analog is utilized to determine how N- and C-terminal modifications impact receptor recognition, peptide conformation, and biological activity. Such studies are critical for the rational design of novel peptide ligands with tailored pharmacological profiles, and for understanding the structural determinants of peptide hormone function.
Enzymatic Stability Assessments: Due to its modified termini, [Sar1, Ile8]-Angiotensin II demonstrates increased resistance to proteolytic enzymes compared to the native peptide. This property is exploited in experiments aimed at evaluating peptide degradation pathways, enzyme specificity, and the influence of peptide stability on biological activity. The analog provides a robust model for studying the metabolic fate of peptide hormones and for developing strategies to enhance peptide durability in physiological environments.
In vivo and ex vivo Functional Models: The peptide's altered pharmacokinetic and pharmacodynamic properties make it suitable for use in animal models and isolated tissue preparations to assess cardiovascular, renal, and endocrine responses mediated by angiotensin II receptors. Its application extends to the evaluation of blood pressure regulation, vascular contractility, and fluid-electrolyte balance, offering insights into the physiological roles of the renin-angiotensin system. These functional studies are foundational for advancing peptide-based research and supporting the development of receptor-targeted modulators.
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