Angiotensin II (3-8), human is a less effective agonist at the angiotensin AT1 receptor.
CAT No: R1201
CAS No:12676-15-2
Synonyms/Alias:Angiotensin IV;12676-15-2;23025-68-5;Angiotensin II (3-8), human;Human angiotensin IV;Nle-angiv;VAL-TYR-ILE-HIS-PRO-PHE;Ile3-angiotensin IV;Huamn angiotensin (3-8);1-De-asp-2-de-arg-5-ile-angiotensin II;(Ile5)-angiotensin II (3-8);(3-8)-5-Isoleucine-angiotensin II;Human angiotensin hexapeptide (3-8);(2S)-2-[[(2S)-1-[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-amino-3-methylbutanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-methylpentanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]pyrrolidine-2-carbonyl]amino]-3-phenylpropanoic acid;angiotensin II, des-Asp(1)-des-Arg(2)-Ile(5)-;(Des(Asp1,Arg2)-Ile5)angiotensin II;(Isoleucine5)-angiotensin II hexapeptide;3-L-isoleucine-Angiotensin IV;CHEMBL261120;5-Isoleucine-angiotensin II 3-8-hexapeptide;Angiotensin II, des-aspartyl(1)-des-arginyl(2)-isoleucine(5)-;Angiotensin IV, 3-L-isoleucine-;AT II (3-8);Angiotensin IV trifluoroacetate salt;Alanine, 3-phenyl-N-(1-(N-(N-(N-valyltyrosyl)isoleucyl)histidyl)prolyl)-;Angiotensin II, 1-de-L-aspartic acid-2-de-L-arginine-5-L-isoleucine-;Angiotensin II (3-8);Alanine, 3-phenyl-N-(1-(N-(N-(N-L-valyl-L-tyrosyl)-L-isoleucyl)-L-histidyl)-L-prolyl)-;(2S)-2-{[(2S)-1-[(2S)-2-[(2S,3S)-2-[(2S)-2-[(2S)-2-amino-3-methylbutanamido]-3-(4-hydroxyphenyl)propanamido]-3-methylpentanamido]-3-(1H-imidazol-5-yl)propanoyl]pyrrolidin-2-yl]formamido}-3-phenylpropanoic acid;Ang IV;MLS000069773;Angiotensin II, 1-des-asn-2-arg;(2S)-2-((((2S)-1-((2S)-2-(((2S,3S)-2-(((2S)-2-(((2S)-2-amino-1-hydroxy-3-methylbutylidene)amino)-1-hydroxy-3-(4-hydroxyphenyl)propylidene)amino)-1-hydroxy-3-methylpentylidene)amino)-3-(1H-imidazol-5-yl)propanoyl)pyrrolidin-2-yl)(hydroxy)methylidene)amino)-3-phenylpropanoate;(2S)-2-(((2S)-1-((2S)-2-((2S,3S)-2-((2S)-2-((2S)-2-amino-3-methylbutanamido)-3-(4-hydroxyphenyl)propanamido)-3-methylpentanamido)-3-(1H-imidazol-5-yl)propanoyl)pyrrolidin-2-yl)formamido)-3-phenylpropanoic acid;(2S)-2-({[(2S)-1-[(2S)-2-{[(2S,3S)-2-{[(2S)-2-{[(2S)-2-amino-1-hydroxy-3-methylbutylidene]amino}-1-hydroxy-3-(4-hydroxyphenyl)propylidene]amino}-1-hydroxy-3-methylpentylidene]amino}-3-(1H-imidazol-5-yl)propanoyl]pyrrolidin-2-yl](hydroxy)methylidene}amino)-3-phenylpropanoate;MFCD00167496;(A)II(3-8);cid_123814;GTPL5368;SCHEMBL4322236;BDBM85550;CHEBI:80127;DTXSID701347717;HMS2232C15;1-De-L-aspartic -2-de-L-arginine-5-L-isoleucineangiotensin II;HY-P1515;AKOS040758825;NCGC00167590-02;DA-50481;FA110283;SMR000058913;CAS_12676-15-2;CS-0044614;G83766;H-Val-Tyr-Ile-His-Pro-Phe-OH; H-VYIHPF-OH;Q66087802;Angiotensin I/II (3-8) (H-Val-Tyr-Ile-His-Pro-Phe-OH);1-De-L-aspartic-2-de-L-arginine-5-L-isoleucineangiotensin II;Angiotensin IV trifluoroacetate salt, >=95% (HPLC), powder;valyl-l-tyrosyl-l-isoleucyl-l-histidyl-l-prolyl-l-phenylalanin;(2S)-2-{[(2S)-1-[(2S)-2-[(2S,3S)-2-[(2S)-2-[(2S)-2-AMINO-3-METHYLBUTANAMIDO]-3-(4-HYDROXYPHENYL)PROPANAMIDO]-3-METHYLPENTANAMIDO]-3-(1H-IMIDAZOL-4-YL)PROPANOYL]PYRROLIDIN-2-YL]FORMAMIDO}-3-PHENYLPROPANOIC ACID;(S)-2-((S)-1-((S)-2-((2S,3S)-2-((S)-2-((S)-2-amino-3-methylbutanamido)-3-(4-hydroxyphenyl)propanamido)-3-methylpentanamido)-3-(1H-imidazol-4-yl)propanoyl)pyrrolidine-2-carboxamido)-3-phenylpropanoic acid;
Angiotensin II (3-8), human, is a biologically active peptide fragment derived from the C-terminal region of the full-length angiotensin II molecule. As a truncated hexapeptide, it retains key structural motifs that interact with components of the renin-angiotensin system, a central regulator of cardiovascular and renal physiology. Due to its defined sequence and bioactive properties, Angiotensin II (3-8) is widely utilized in research exploring peptide signaling, receptor specificity, and the functional dissection of angiotensin-mediated pathways. Its role as a selective fragment makes it a valuable tool for delineating the contribution of specific peptide domains to physiological and biochemical responses.
Peptide receptor characterization: Angiotensin II (3-8) is extensively employed in studies aimed at mapping the binding preferences and activation mechanisms of angiotensin receptors, particularly the AT1 and AT2 subtypes. By comparing the biological responses elicited by this hexapeptide fragment to those of the full-length parent peptide, researchers can discern the significance of terminal residues in receptor interaction and downstream signaling. Such comparative analyses provide critical insights into the structure-activity relationships that govern peptide-receptor dynamics, informing the rational design of novel ligands and antagonists.
Signal transduction research: As a functional peptide derivative, Angiotensin II (3-8) enables the targeted investigation of intracellular signaling cascades initiated by angiotensin peptides. Experimental use of this fragment allows for the selective activation or inhibition of specific pathways, facilitating the study of second messenger systems, kinase activation, and gene expression profiles in relevant cell types. This approach is instrumental in parsing out the discrete contributions of peptide fragments to complex signal transduction networks, advancing understanding of peptide hormone biology.
Enzymatic processing studies: The hexapeptide serves as a model substrate for examining the enzymatic processing of angiotensin peptides by proteases such as aminopeptidases and carboxypeptidases. Researchers utilize Angiotensin II (3-8) to probe the specificity, kinetics, and regulatory mechanisms of peptide cleavage events, which are critical for modulating bioactive peptide pools in physiological and pathological contexts. These studies contribute to a deeper understanding of peptide turnover and metabolic regulation within the renin-angiotensin system.
Analytical method development: In the context of bioanalytical chemistry, this peptide fragment is used as a standard or reference compound for the development and validation of quantitative assays, including liquid chromatography and mass spectrometry techniques. Its defined sequence and stability make it suitable for calibrating detection systems, optimizing separation protocols, and establishing assay sensitivity for angiotensin-related peptides in complex biological matrices. Such applications are essential for advancing peptide quantification in research and quality control settings.
Structure-function analysis: Angiotensin II (3-8) is a valuable probe for elucidating the relationship between peptide structure and biological activity. By systematically modifying or comparing this fragment with other angiotensin derivatives, investigators can identify critical residues and conformational features that influence receptor binding, signaling efficacy, and metabolic stability. These structure-function studies underpin the rational development of peptide-based tools and modulators, supporting innovation in both basic research and applied peptide science.
3. Urinary Metabolites Associated with Blood Pressure on a Low-or High-Sodium Die
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