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

Author(s): Ali MY, Seong SH, Jung HA, Choi JS

Molecules. 2019 Oct 31;24(21): Authors: Ali MY, Seong SH, Jung HA, Choi JS

Article GUID: 31683604
Umbelliferone derivatives exert neuroprotective effects by inhibiting monoamine oxidase A, self-amyloidβ aggregation, and lipid peroxidation.

Author(s): Seong SH, Ali MY, Jung HA, Choi JS

Bioorg Chem. 2019 Sep 18;92:103293 Authors: Seong SH, Ali MY, Jung HA, Choi JS

Article GUID: 31557622
Kinetics and molecular docking of dihydroxanthyletin-type coumarins from Angelica decursiva that inhibit cholinesterase and BACE1.

Author(s): Ali MY, Seong SH, Jung HA, Jannat S, Choi JS

Arch Pharm Res. 2018 Jul;41(7):753-764 Authors: Ali MY, Seong SH, Jung HA, Jannat S, Choi JS

Article GUID: 30047040
Title:Kinetics and molecular docking of dihydroxanthyletin-type coumarins from Angelica decursiva that inhibit cholinesterase and BACE1.
Authors:Ali MY,  Seong SH,  Jung HA,  Jannat S,  Choi JS
Link:https://www.ncbi.nlm.nih.gov/pubmed/30047040?dopt=Abstract
Category:Arch Pharm Res
PMID:30047040
Dept Affiliation: CHEMBIOCHEM
1 Department of Food and Life Science, Pukyong National University, Busan, 608-737, Republic of Korea.
2 Department of Chemistry and Biochemistry, Concordia University, Montreal, QC, Canada, H4B 1R6.
3 Department of Food Science and Human Nutrition, Chonbuk National University, Jeonju, 561-756, Republic of Korea. jungha@jbnu.ac.kr.
4 Department of Food and Life Science, Pukyong National University, Busan, 608-737, Republic of Korea. choijs@pknu.ac.kr.

Description:

Kinetics and molecular docking of dihydroxanthyletin-type coumarins from Angelica decursiva that inhibit cholinesterase and BACE1.

Arch Pharm Res. 2018 Jul;41(7):753-764

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

Abstract

In the present study, we investigated the anti-Alzheimer's disease (AD) potential of six dihydroxanthyletin-type coumarins, 4'-hydroxy Pd-C-III (1), decursidin (2), Pd-C-I (3), 4'-methoxy Pd-C-I (4), Pd-C-II (5), and Pd-C-III (6) from Angelica decursiva by evaluating their ability to inhibit acetylcholinesterase (AChE), butyrylcholinesterase (BChE) and ß-site amyloid precursor protein cleaving enzyme 1 (BACE1). Coumarins 1-6 exhibited dose-dependent inhibition of AChE, BChE, and BACE1. IC50 values were 1.0-4.01 µM for AChE, 5.78-13.91 µM for BChE, and 1.99-17.34 µM for BACE1. Kinetic studies revealed that 1 was noncompetitive inhibitor for AChE, while 2-6 were mixed-type inhibitors of AChE. Compounds 1, 5 and 6 had mixed-type inhibitory effects against BChE; 2 was a competitive inhibitor; and 3 and 4 were noncompetitive inhibitors. Against BACE1, compounds 1, 2, 3, 5 showed mixed-type inhibition and 4, 6 were noncompetitive inhibitors. Molecular docking simulation of the compounds demonstrated negative-binding energies indicating high proximity to the active site and tight binding to the enzyme. These data suggested that the compounds inhibited AChE, BChE, and BACE1, providing a preventive and therapeutic strategy for AD treatment.

PMID: 30047040 [PubMed - indexed for MEDLINE]