PERFORM Publications

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Title		Authors	PubMed ID
1	The enterobactin biosynthetic intermediate 2,3-dihydroxybenzoic acid is a competitive inhibitor of the Escherichia coli isochorismatase EntB	Bin X; Pawelek PD;	40400396 CHEMBIOCHEM
2	New Megastigmane and Polyphenolic Components of Henna Leaves and Their Tumor-Specific Cytotoxicity on Human Oral Squamous Carcinoma Cell Lines	Orabi MAA; Orabi EA; Awadh AAA; Alshahrani MM; Abdel-Wahab BA; Sakagami H; Hatano T;	38001804 CHEMBIOCHEM
3	Structural determination and anticholinesterase assay of C-glycosidic ellagitannins from Lawsonia inermis leaves: A study supported by DFT calculations and molecular docking	Orabi MAA; Orabi EA; Abdel-Sattar ES; English AM; Hatano T; Elimam H;	36423882 CHEMBIOCHEM
4	Angiotensin-I-Converting Enzyme Inhibitory Activity of Coumarins from Angelica decursiva.	Ali MY, Seong SH, Jung HA, Choi JS	31683604 CHEMBIOCHEM
5	Flavanone glycosides inhibit β-site amyloid precursor protein cleaving enzyme 1 and cholinesterase and reduce Aβ aggregation in the amyloidogenic pathway.	Ali MY, Jannat S, Edraki N, Das S, Chang WK, Kim HC, Park SK, Chang MS	31194956 BIOLOGY

Title:	Angiotensin-I-Converting Enzyme Inhibitory Activity of Coumarins from Angelica decursiva.
Authors:	Ali MY, Seong SH, Jung HA, Choi JS
Link:	https://www.ncbi.nlm.nih.gov/pubmed/31683604?dopt=Abstract
DOI:	10.3390/molecules24213937
Publication:	Molecules (Basel, Switzerland)
Keywords:	Angelica decursiva; angiotensin-I-converting enzyme; antihypertension; coumarins; molecular docking;
PMID:	31683604	Category:	Molecules	Date Added:	2019-11-07
Dept Affiliation:	CHEMBIOCHEM 1 Department of Food and Life Science, Pukyong National University, Busan 48513, Korea. yousufbge@gmail.com. 2 Department of Chemistry and Biochemistry, Concordia University, Montreal, QC H4B 1R6, Canada. yousufbge@gmail.com. 3 Department of Biology, Faculty of Arts and Science, Concordia University, 7141 Sherbrooke St. W., Montreal, QC H4B 1R6, Canada. yousufbge@gmail.com. 4 Centre for Structural and Functional Genomic, Department of Biology, Faculty of Arts and Science, Concordia University, 7141 Sherbrooke St. W., Montreal, QC H4B 1R6, Canada. yousufbge@gmail.com. 5 Department of Food and Life Science, Pukyong National University, Busan 48513, Korea. seongsuhui@naver.com. 6 Department of Food Science and Human Nutrition, Jeonbuk National University, Jeonju 54896, Korea. jungha@jbnu.ac.kr. 7 Department of Food and Life Science, Pukyong National University, Busan 48513, Korea. choijs@pknu.ac.kr.

Description:

Angiotensin-I-Converting Enzyme Inhibitory Activity of Coumarins from Angelica decursiva.

Molecules. 2019 Oct 31;24(21):

Authors: Ali MY, Seong SH, Jung HA, Choi JS

Abstract

The bioactivity of ten traditional Korean Angelica species were screened by angiotensin-converting enzyme (ACE) assay in vitro. Among the crude extracts, the methanol extract of Angelica decursiva whole plants exhibited potent inhibitory effects against ACE. In addition, the ACE inhibitory activity of coumarins 1-5, 8-18 was evaluated, along with two phenolic acids (6, 7) obtained from A. decursiva. Among profound coumarins, 11-18 were determined to manifest marked inhibitory activity against ACE with IC50 values of 4.68-20.04 µM. Compounds 12, 13, and 15 displayed 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 of A. decursiva in traditional medicine to treat cardiovascular diseases such as hypertension.

PMID: 31683604 [PubMed - in process]

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