Angiotensin I, human

Product Name: Angiotensin I, human

Sequence One Letter Code: DRVYIHPFHL

Sequence Three Letter Code: H-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-OH

Cas No: 484-42-4

Chemical Formula:C62H89N17O14

Molecular Weight: 1296.6

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: Cardiovascular Disease Research

SMILES: CC[C@H](C)[C@@H](C(=O)N[C@@H](CC1=CN=CN1)C(=O)N2CCC[C@H]2C(=O)N[C@@H](CC3=CC=CC=C3)C(=O)N[C@@H](CC4=CN=CN4)C(=O)N[C@@H](CC(C)C)C(=O)O)NC(=O)[C@H](CC5=CC=C(C=C5)O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC(=O)O)N

IUPAC: (2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-1-[(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-carboxypropanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-3-methylbutanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-methylpentanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]pyrrolidine-2-carbonyl]amino]-3-phenylpropanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-4-methylpentanoic acid

INCHIKEY: ORWYRWWVDCYOMK-HBZPZAIKSA-N

INCHI:

InChI=1S/C62H89N17O14/c1-7-35(6)51(78-56(87)44(25-37-17-19-40(80)20-18-37)74-58(89)50(34(4)5)77-53(84)42(15-11-21-68-62(64)65)71-52(83)41(63)28-49(81)82)59(90)75-46(27-39-30-67-32-70-39)60(91)79-22-12-16-48(79)57(88)73-43(24-36-13-9-8-10-14-36)54(85)72-45(26-38-29-66-31-69-38)55(86)76-47(61(92)93)23-33(2)3/h8-10,13-14,17-20,29-35,41-48,50-51,80H,7,11-12,15-16,21-28,63H2,1-6H3,(H,66,69)(H,67,70)(H,71,83)(H,72,85)(H,73,88)(H,74,89)(H,75,90)(H,76,86)(H,77,84)(H,78,87)(H,81,82)(H,92,93)(H4,64,65,68)/t35-,41-,42-,43-,44-,45-,46-,47-,48-,50-,51-/m0/s1

Source / Species: human

Conjugation: Unconjugated

Code Nacres: NA.26

Application: Human Angiotensin I (Ang I) is a decapeptide precursor in the renin–angiotensin system, conserved across multiple species. Although biologically inactive, it serves as the substrate for enzymatic conversion into angiotensin II, a potent regulator of blood pressure and fluid balance. This conversion is primarily mediated by angiotensin-converting enzyme (ACE), with additional contribution from enzymes such as chymase. Human chymase efficiently cleaves Ang I at the Phe8–His9 bond to generate angiotensin II, highlighting alternative pathways in cardiovascular regulation. Ang I is widely used in research on enzymatic activity, cardiovascular physiology, and peptide processing, supporting studies of hypertension, vascular function, and renin–angiotensin system dynamics.

Current Research: Human Angiotensin I (Ang I) is a 10-amino-acid (decapeptide) that serves as a central intermediate in the renin–angiotensin system (RAS), a critical hormonal cascade regulating blood pressure, fluid balance, and vascular function. Although Ang I itself is biologically inactive, it plays an essential role as the substrate for enzymatic conversion into angiotensin II (Ang II), one of the most potent vasoactive peptides in human physiology. Due to its central position in this pathway, Ang I is widely used in research focused on cardiovascular biology, enzymatic processing, and peptide metabolism. The Renin–Angiotensin System Overview The renin–angiotensin system is a tightly regulated pathway that maintains hemodynamic stability and electrolyte balance. It is initiated by the enzyme renin, which cleaves angiotensinogen (a liver-derived protein) to produce Ang I. Ang I then serves as the immediate precursor for Ang II through enzymatic processing. The overall cascade includes: Renin: Converts angiotensinogen to Ang I Angiotensin-converting enzyme (ACE): Converts Ang I to Ang II Angiotensin II: Exerts physiological effects such as vasoconstriction and aldosterone release While Ang I does not directly affect vascular tone or hormone secretion, its conversion into Ang II is essential for activating downstream responses. Enzymatic Conversion to Angiotensin II The primary pathway for Ang II generation involves ACE, which cleaves Ang I by removing two C-terminal amino acids. This conversion produces Ang II, an octapeptide with strong biological activity. However, alternative enzymatic pathways also contribute to Ang II production. Notably, chymase, a serine protease found in various tissues, can convert Ang I directly into Ang II by cleaving at the Phe8–His9 bond. This pathway is particularly significant in certain tissues, such as the heart and vasculature, where chymase activity may complement or even dominate over ACE-mediated conversion. The existence of multiple enzymatic routes highlights the complex regulation of Ang II production and its importance in cardiovascular physiology. Role of Angiotensin II in Physiological Regulation Although Ang I itself is inactive, its conversion product, Ang II, plays a major role in: Vasoconstriction, increasing blood pressure Stimulation of aldosterone secretion, promoting sodium and water retention Regulation of renal function Modulation of sympathetic nervous system activity Because Ang I is the direct precursor of Ang II, studying its conversion provides critical insight into how these physiological processes are controlled. Applications in Cardiovascular and Enzymatic Research Human Angiotensin I is widely used as a substrate peptide in biochemical and physiological studies. Its well-defined sequence and central role in the RAS make it an ideal tool for investigating enzyme activity and pathway dynamics. Common research applications include: ACE activity assays to evaluate enzymatic conversion efficiency Chymase and alternative pathway studies Screening of enzyme inhibitors targeting RAS components Kinetic analysis of peptide cleavage mechanisms Investigation of tissue-specific Ang II generation pathways These studies are essential for understanding how different enzymes contribute to Ang II production under normal and pathological conditions. Relevance to Hypertension and Cardiovascular Disease The renin–angiotensin system is a major focus in research on hypertension, heart failure, and vascular disease. Dysregulation of Ang II production can lead to excessive vasoconstriction, fluid retention, and increased cardiovascular risk. By serving as a substrate for Ang II generation, Ang I is frequently used in studies examining: Mechanisms of blood pressure regulation Pathways contributing to cardiovascular remodeling Effects of pharmacological inhibitors (e.g., ACE inhibitors) Balance between ACE-dependent and ACE-independent pathways Understanding how Ang I is processed in different tissues helps clarify the complexity of RAS regulation and its role in disease. A Fundamental Tool for Studying RAS Dynamics Human Angiotensin I is a foundational reagent in research on peptide processing and cardiovascular physiology. Although it lacks intrinsic biological activity, its role as a precursor to Ang II makes it indispensable for studying enzymatic conversion, pathway regulation, and therapeutic targets within the renin–angiotensin system. By enabling detailed investigation of ACE, chymase, and related enzymes, Ang I continues to support advances in understanding blood pressure control, vascular biology, and the molecular mechanisms underlying cardiovascular disease.