PMID:
Molecules. 2019 Oct 31 ;24(21). Epub 2019 Oct 31. PMID: 31683604
Abstract Title:
Angiotensin-I-Converting Enzyme Inhibitory Activity of Coumarins from.
Abstract:
The bioactivity of ten traditional Koreanspecies were screened by angiotensin-converting enzyme (ACE) assay in vitro. Among the crude extracts, the methanol extract ofwhole plants exhibited potent inhibitory effects against ACE. In addition, the ACE inhibitory activity of coumarins-,-was evaluated, along with two phenolic acids (,) obtained from.. Among profound coumarins,-were determined to manifest marked inhibitory activity against ACE with ICvalues of 4.68-20.04µM. Compounds,, anddisplayed competitive inhibition against ACE. Molecular docking studies confirmed that coumarins inhibited ACE via many hydrogen bond and hydrophobic interactions with catalytic residues and zinc ion of C- and N-domain ACE that blocked the catalytic activity of ACE. The results derived from these computational and in vitro experiments give additional scientific support to the anecdotal use ofin traditional medicine to treat cardiovascular diseases such as hypertension.
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