scholarly journals Southeast Asian Medicinal Plants with Angiotensin Converting Enzyme (ACE) Inhibition Properties

2020 ◽  
Vol 12 (6) ◽  
pp. 1429-1439
Author(s):  
T. A. Faiz T. Anuar ◽  
Azlini Ismail
Molecules ◽  
2021 ◽  
Vol 26 (22) ◽  
pp. 6971
Author(s):  
Syeda Tehreem ◽  
Saeedur Rahman ◽  
Muhammad Salman Bhatti ◽  
Reaz Uddin ◽  
Muhammad Noman Khan ◽  
...  

Angiotensin converting enzyme (ACE) plays a crucial role in regulating blood pressure in the human body. Identification of potential ACE inhibitors from medicinal plants supported the idea of repurposing these medicinal plants against hypertension. A method based on ultra-performance liquid chromatography (UPLC) coupled with a diode array detector (DAD) was used for the rapid screening of plant extracts and purified compounds to determine their ACE inhibitory activity. Hippuryl-histidiyl-leucine (HHL) was used as a substrate, which is converted into hippuric acid (HA) by the action of ACE. A calibration curve of the substrate HHL was developed with the linear regression 0.999. The limits of detection and quantification of this method were found to be 0.134 and 0.4061 mM, respectively. Different parameters of ACE inhibitory assay were optimized, including concentration, incubation time and temperature. The ACE inhibition potential of Adhatoda vasica (methanolic-aqueous extract) and its isolated pyrroquinazoline alkaloids, vasicinol (1), vasicine (2) and vasicinone (3) was evaluated. Compounds 1–3 were characterized by various spectroscopic techniques. The IC50 values of vasicinol (1), vasicine (2) and vasicinone (3) were found to be 6.45, 2.60 and 13.49 mM, respectively. Molecular docking studies of compounds 1–3 were also performed. Among these compounds, vasicinol (1) binds as effectively as captopril, a standard drug of ACE inhibition.


1993 ◽  
Vol 17 (1) ◽  
pp. 40-47 ◽  
Author(s):  
V. Gross ◽  
E. Treher ◽  
K. Haag ◽  
W. Neis ◽  
U. Wiegand ◽  
...  

1993 ◽  
Vol 264 (5) ◽  
pp. H1493-H1497 ◽  
Author(s):  
M. Grafe ◽  
C. Bossaller ◽  
K. Graf ◽  
W. Auch-Schwelk ◽  
C. R. Baumgarten ◽  
...  

The degradation of bradykinin by angiotensin-converting-enzyme (ACE) activity in cultured human endothelial cells was studied by direct measurement of bradykinin and by its effect on the release of endothelium-derived relaxing factors. The half-life of exogenous bradykinin (10,000 pg/ml) was calculated from the decay of the bradykinin concentration as 46 +/- 2 min in cell monolayers, 133 +/- 15 min in conditioned medium, and 24 +/- 2 min in homogenates. Most of the bradykinin-degrading activity in cell monolayers could be inhibited in a concentration-dependent manner by the ACE inhibitors lisinopril, ramiprilat, and captopril. Bradykinin-degrading activity was released into the culture medium containing one-fourth of the bradykinin-degrading activity found in the presence of cell monolayers. In cell homogenates higher unspecific bradykinin-degrading activities were present. The functional consequence of bradykinin degradation was demonstrated by the potentiating effect of ramiprilat on the generation of endothelium-derived relaxing factors nitric oxide and prostacyclin from endothelial cells. The study supports the concept of increased vasodilatory effects of bradykinin during ACE inhibition.


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