Angiotensin amide is the octapeptide amide of bovine angiotensin II used to increase blood pressure by vasoconstriction.
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CAT No: 10-101-309
CAS No:53-73-6
Synonyms/Alias:Angiotensin amide;ANGIOTENSINAMIDE;53-73-6;Hypertensine;Ipertensina;Hypertensinamide;Angio tensinamida;Angiotensin II-amide;angiotensinamida;UNII-7WAL1X78KV;Angiotensin (Ciba) (VAN);Val-5-angiotensin II amide;Rainbow trout angiotensin II;5-Valyl-angiotensin II amide;Angiotensin amide [USAN:NF];5-Valine angiotensin II amide;5-Valine-angiotensin amide II;Angiotensin II amide 5-valine;Angiotensin II-5-valine amide;Angiotensinamidum [INN-Latin];Angiotensin amide, 5-L-valine-;Angio tensinamida [INN-Spanish];5-L-Valine-angiotensin II amide;Angiotensinamide [INN];5-Valine-angiotensin II-beta-amide;Angiotensin II, 1-L-asparagine-5-L-valine-;Angiotensin II amide, 5-L-valine-;EINECS 200-182-3;1-Asparagine-5-valine-angiotensin II;1-Asparaginyl-5-valyl-angiotensin II;NSC 107678;(Asn1,Val5)-Angiotensin II;(1-Asparagine-5-valine)-angiotensin II;1-L-Asparagine-5-L-valineangiotensin II;5-Valine-angiotensin II aspartic-beta-amide;Asn-Arg-Val-Tyr-Val-His-Pro-Phe;1-Asparatic acid-5-valine-angiotensin II amide;Angiotensin II aspartic-beta-amide, 5-L-valine;DTXSID401018923;1-Aspartic acid-beta-amide 5-valine-angiotensin II;NSC-107678;Angiotensinamide (INN);MFCD00167643;L-Asparaginyl-L-arginyl-L-valyl-L-tyrosyl-L-valyl-L-histidyl-L-prolyl-L-phenylalanin;(2S)-2-[[(2S)-1-[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-5-(diaminomethylideneamino)-2-[[(2S)-2,4-diamino-4-oxobutanoyl]amino]pentanoyl]amino]-3-methylbutanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-methylbutanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]pyrrolidine-2-carbonyl]amino]-3-phenylpropanoic acid;L-Phenylalanine, N-(1-(N-(N-(N-(N-(N2-L-asparaginyl-L-arginyl)-L-valyl)-L-tyrosyl)-L-valyl)-L-histidyl)-L-prolyl)-;Angiotensinamidum (INN-Latin);ANGIOTENSINAMIDE (MART.);ANGIOTENSINAMIDE [MART.];Angio tensinamida (INN-Spanish);Angiotensin (Ciba);Angiotensinamidum;L-asparaginyl-L-arginyl-L-valyl-L-tyrosyl-L-valyl-L-histidyl-L-prolyl-L-phenylalanine;Amide, Angiotensin;Angiotensin amide (USAN);ANGIOTENSIN AMIDE [USAN];angiotensine;5 Valine Angiotensin II Amide;5-Valine-Angiotensin II Amide;NSC107678;Amide, 5-Valine-Angiotensin II;(2S)-2-(((2S)-1-((2S)-2-(((2S)-2-(((2S)-2-(((2S)-2-(((2S)-5-(diaminomethylideneamino)-2-(((2S)-2,4-diamino-4-oxobutanoyl)amino)pentanoyl)amino)-3-methylbutanoyl)amino)-3-(4-hydroxyphenyl)propanoyl)amino)-3-methylbutanoyl)amino)-3-(1H-imidazol-5-yl)propanoyl)pyrrolidine-2-carbonyl)amino)-3-phenylpropanoic acid;1 Asparagine 5 valine Angiotensin II;1-Asparagine-5-valine Angiotensin II;Angiotensin II, 1-Asparagine-5-valine;H-Asn-Arg-Val-Tyr-Val-His-Pro-Phe-OH;SCHEMBL9324;7WAL1X78KV;ANGIOTENSIN AMIDE [MI];CHEMBL409803;ANGIOTENSINAMIDE [WHO-DD];C01CX06;CHEBI:135950;JYPVVOOBQVVUQV-CGHBYZBKSA-N;DTXCID601476937;HY-P2212;BDBM50228199;DB13517;DA-48713;FA109691;N-(1-(N-(N-(N-(N-(N(sup 2)-L-Asparaginyl-L-arginyl)-L-valyl)-L-tyrosyl)-L-valyl)-L-histidyl)-L-prolyl)-3-phenyl-L-alanine;CS-0113476;NS00041168;[Asn1, Val5]-Angiotensin II, >=97% (HPLC);Q4763296;(Asn1,Val5)-Angiotensin II (H-Asn-Arg-Val-Tyr-Val-His-Pro-Phe-OH);N-(1-(N-(N-(N-(N-(N2-L-ASPARAGINYL-L-ARGINYL)-L-VALYL)-L-TYROSYL)-L-VALYL)-L-HISTIDYL)-L-PROLYL)-3-PHENYL-L-ALANINE;
Chemical Name:(2S)-2-[[(2S)-1-[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-5-(diaminomethylideneamino)-2-[[(2S)-2,4-diamino-4-oxobutanoyl]amino]pentanoyl]amino]-3-methylbutanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-methylbutanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]pyrrolidine-2-carbonyl]amino]-3-phenylpropanoic acid
[Asn1,Val5]-Angiotensin II is a synthetic analog of the naturally occurring octapeptide angiotensin II, distinguished by specific amino acid substitutions at positions 1 and 5. These modifications impart unique biochemical properties that set it apart from the native peptide, influencing receptor binding affinity and downstream physiological responses. Due to its structural similarities and subtle differences, [Asn1,Val5]-Angiotensin II serves as a valuable tool for researchers seeking to dissect the intricate signaling pathways mediated by the renin-angiotensin system. Its well-defined sequence and robust stability under experimental conditions make it particularly suitable for a range of in vitro and in vivo studies, providing insights into peptide-receptor interactions, signal transduction, and the modulation of vascular function. The synthetic nature of this peptide enables precise control over experimental variables, making it indispensable for mechanistic studies in cardiovascular, renal, and neuroendocrine research.
Receptor Binding Studies: In receptor pharmacology, [Asn1,Val5]-Angiotensin II is frequently employed to explore the specificity and affinity of angiotensin II receptors, particularly AT1 and AT2 subtypes. Its altered sequence allows researchers to compare binding characteristics with the native peptide, facilitating the identification of critical residues involved in receptor interaction. By utilizing radiolabeled or fluorescently tagged versions of the analog, scientists can map binding sites, quantify binding kinetics, and evaluate competitive inhibition by novel antagonists or agonists. These studies are instrumental in understanding how structural modifications impact receptor selectivity, guiding the rational design of new therapeutic agents targeting the renin-angiotensin system.
Signal Transduction Analysis: The peptide analog is also widely used to investigate intracellular signaling cascades triggered by angiotensin II receptor activation. Researchers leverage [Asn1,Val5]-Angiotensin II to stimulate cultured cells or tissue preparations, monitoring downstream events such as calcium mobilization, protein kinase activation, and gene expression changes. By comparing the signaling profiles elicited by the analog versus the native peptide, it becomes possible to delineate the contribution of specific amino acid residues to receptor coupling and signal propagation. These analyses provide a deeper understanding of the molecular mechanisms governing cardiovascular and renal physiology.
Vascular Reactivity Experiments: In vascular biology, [Asn1,Val5]-Angiotensin II is utilized to assess its effects on blood vessel tone and reactivity. Isolated vessel preparations or perfused organ systems are exposed to the analog to evaluate contractile responses, relaxation dynamics, and interactions with endothelium-derived factors. Such studies help elucidate the role of angiotensin II analogs in modulating vascular resistance, contributing to foundational knowledge in hypertension and related disorders. The ability to compare responses to the modified and native peptides enables a nuanced understanding of structure-function relationships in vascular regulation.
Renal Physiology Research: The application of [Asn1,Val5]-Angiotensin II extends to the study of kidney function, where it is used to probe the peptide's role in regulating glomerular filtration, sodium reabsorption, and renal hemodynamics. Experimental models employing this analog allow for the dissection of signaling pathways involved in fluid and electrolyte balance, providing a platform for investigating the interplay between peptide structure and renal function. Insights gained from these studies inform the development of novel approaches to managing disorders of fluid homeostasis.
Neuroendocrine Investigations: In the context of neuroendocrine research, [Asn1,Val5]-Angiotensin II serves as a probe to examine its influence on hormone secretion, neuronal excitability, and central regulation of blood pressure. By applying the analog to neuronal cultures or brain slice preparations, researchers can assess changes in neurotransmitter release, electrophysiological properties, and gene expression patterns. These investigations contribute to a broader understanding of how angiotensin II analogs participate in the integration of neuroendocrine and cardiovascular functions, offering new perspectives on peptide signaling in the central nervous system. Through these diverse applications, [Asn1,Val5]-Angiotensin II continues to be a pivotal reagent in advancing fundamental and translational research across multiple scientific disciplines.
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