13602-53-4 Usage
Description
Angiotensin III (Ang III), also known as human angiotensin III, is a heptapeptide agonist that primarily targets the angiotensin 1 (AT1) and AT2 receptors. It exhibits a 30-fold higher affinity for AT2 receptors compared to AT1 receptors in HEK293 cells. Ang III plays a crucial role in the regulation of blood pressure, sodium excretion, and other physiological processes. It is the preferred agonist for renal AT2 receptors, which are responsible for sodium excretion into the urine. Ang III also has the ability to induce aldosterone synthesis and modulate sympathetic nerve activity, vasopressin release, and the baroreflex.
Uses
Used in Pharmaceutical Industry:
Angiotensin III, HUMAN is used as a therapeutic agent for the treatment of hypertension and related cardiovascular conditions. Its ability to modulate blood pressure and influence the renin-angiotensin system makes it a valuable compound in the development of new drugs targeting the AT1 and AT2 receptors.
Used in Research and Development:
Angiotensin III, HUMAN is used as a research tool for studying the mechanisms of blood pressure regulation, the renin-angiotensin system, and the role of AT1 and AT2 receptors in various physiological processes. It can also be employed in the development of novel drug delivery systems and the investigation of potential synergistic effects with other compounds.
Used in Diagnostic Applications:
Angiotensin III, HUMAN can be utilized in diagnostic tests to assess the activity of the renin-angiotensin system and the function of AT1 and AT2 receptors in patients with hypertension or other cardiovascular conditions. This can help in the identification of potential therapeutic targets and the development of personalized treatment strategies.
Used in Drug Delivery Systems:
To enhance the therapeutic potential of Angiotensin III, HUMAN, novel drug delivery systems can be developed to improve its bioavailability, targeting, and efficacy. These systems may include organic and metallic nanoparticles, liposomes, or other advanced delivery platforms designed to optimize the pharmacokinetic and pharmacodynamic properties of Ang III.
Check Digit Verification of cas no
The CAS Registry Mumber 13602-53-4 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,3,6,0 and 2 respectively; the second part has 2 digits, 5 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 13602-53:
(7*1)+(6*3)+(5*6)+(4*0)+(3*2)+(2*5)+(1*3)=74
74 % 10 = 4
So 13602-53-4 is a valid CAS Registry Number.
InChI:InChI=1/C46H66N12O9/c1-5-27(4)38(57-40(61)33(21-29-15-17-31(59)18-16-29)53-42(63)37(26(2)3)56-39(60)32(47)13-9-19-51-46(48)49)43(64)54-34(23-30-24-50-25-52-30)44(65)58-20-10-14-36(58)41(62)55-35(45(66)67)22-28-11-7-6-8-12-28/h6-8,11-12,15-18,24-27,32-38,59H,5,9-10,13-14,19-23,47H2,1-4H3,(H,50,52)(H,53,63)(H,54,64)(H,55,62)(H,56,60)(H,57,61)(H,66,67)(H4,48,49,51)/t27-,32-,33-,34-,35-,36-,37-,38-/m0/s1
13602-53-4Relevant articles and documents
Identification and characterization of novel inhibitors of mammalian aspartyl aminopeptidase
Chen, Yuanyuan,Tang, Hong,Seibel, William,Papoian, Ruben,Oh, Ki,Li, Xiaoyu,Zhang, Jianye,Golczak, Marcin,Palczewski, Krzysztof,Kiser, Philip D.
, p. 231 - 242 (2014/10/15)
Aspartyl aminopeptidase (DNPEP) has been implicated in the control of angiotensin signaling and endosome trafficking, but its precise biologic roles remain incompletely defined. We performed a high-throughput screen of ～25,000 small molecules to identify inhibitors of DNPEP for use as tools to study its biologic functions. Twenty-three confirmed hits inhibited DNPEP-catalyzed hydrolysis of angiotensin II with micromolar potency. A counter screen against glutamyl aminopeptidase (ENPEP), an enzyme with substrate specificity similar to that of DNPEP, identified eight DNPEP-selective inhibitors. Structure-activity relationships and modeling studies revealed structural features common to the identified inhibitors, including a metal-chelating group and a charged or polar moiety that could interact with portions of the enzyme active site. The compounds identified in this study should be valuable tools for elucidating DNPEP physiology. Copyright
Synthesis of peptides with the solid phase method. II. Octapeptide analogues of angiotensin II
Park,Choi,Rioux,Regoli
, p. 113 - 119 (2007/10/09)
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