| 货号 | 15313-1g |
| 描述 | Angiotensin-converting enzyme (ACE) removes the C-terminal dipeptide from angiotensin I to form angiotensin II, a powerful vasoconstrictor. ACE is a key regulator of the renin-angiotensin system and an important drug target for the treatment of hypertension, congestive heart failure, and heart attacks, and also in preventing renal and retinal complications in diabetes.1 As the first nonpeptidic ACE inhibitor to be developed (IC50 = 6.3 nM), captopril was discovered based on bradykinin-potentiating peptides isolated from the venom of B. Jararaca, a pit viper native to Brazil.2,3 It does not exhibit a domain preference for binding either the C- or N-terminal active sites of the somatic form of ACE, which may account for some of captopril’s negative side effects.4 Captopril is also a competitive and reversible inhibitor of leukotriene (LTA4) hydrolase, which results in the disruption of LTB4 synthesis at an IC50 value of 14 μM.5 |
| 别名 | SA 333;SQ 14,225; |
| 供应商 | Cayman |
| 应用文献 | |
| 1.Zaman, M.A.,Oparil, S. and Calhoun, D.A. Drugs targeting the renin-angiotensin-aldosterone system. Nature Reviews.Drug Discovery 1, 621-636 (2002). 2.Redelinghuys, P.,Nchinda, A.T. and Sturrock, E.D. Development of domain-selective angiotensin I-converting enzyme inhibitors. Annals of the New York Academy of Sciences 1056, 160-175 (2005). 3.Cushman, D.W. and Ondetti, M.A. Design of angiotensin converting enzyme inhibitors. Nature Medicine 5(10), 1110-1113 (1999). 4.Dalkas, G.A.,Marchand, D.,Galleyrand, J.C., et al. Study of a lipophilic captopril analogue binding to angiotensin I converting enzyme. J.Pept.Sci. 16(2), 91-97 (2010). 5.Orning, L.,Krivi, G.,Bild, G., et al. Inhibition of leukotriene A4 hydrolase/aminopeptidase by captopril. The Journal of Biological Chemisty 266(25), 16507-16511 (1991). | |
| 运输条件 | Room temperature in continental US; may vary elsewhere |
| 存放说明 | -20 |
| 纯度 | ≥98% |
| 计算分子量 | 217.3 |
| 分子式 | C9H15NO3S |
| CAS号 | 62571-86-2 |
| 稳定性 | ≥ 2 years |
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