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Flavanone glycosides inhibit β-site amyloid precursor protein cleaving enzyme 1 and cholinesterase and reduce Aβ aggregation in the amyloidogenic pathway.

Author(s): Ali MY, Jannat S, Edraki N, Das S, Chang WK, Kim HC, Park SK, Chang MS

Chem Biol Interact. 2019 Jun 10;: Authors: Ali MY, Jannat S, Edraki N, Das S, Chang WK, Kim HC, Park SK, Chang MS

Article GUID: 31194956

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

Inhibition of β-site amyloid precursor protein cleaving enzyme 1 and cholinesterases by pterosins via a specific structure-activity relationship with a strong BBB permeability.

Author(s): Jannat S, Balupuri A, Ali MY, Hong SS, Choi CW, Choi YH, Ku JM, Kim WJ, Leem JY, Kim JE, Shrestha AC, Ham HN, Lee KH, Kim DM, Kang NS, Park GH

Exp Mol Med. 2019 02 12;51(2):12 Authors: Jannat S, Balupuri A, Ali MY, Hong SS, Choi CW, Choi YH, Ku JM, Kim WJ, Leem JY, Kim JE, Shrestha AC, Ham HN, Lee KH, Kim DM, Kang NS, Park GH

Article GUID: 30755593

Didymin, a dietary citrus flavonoid exhibits anti-diabetic complications and promotes glucose uptake through the activation of PI3K/Akt signaling pathway in insulin-resistant HepG2 cells.

Author(s): Ali MY, Zaib S, Rahman MM, Jannat S, Iqbal J, Park SK, Chang MS

Chem Biol Interact. 2019 May 25;305:180-194 Authors: Ali MY, Zaib S, Rahman MM, Jannat S, Iqbal J, Park SK, Chang MS

Article GUID: 30928401


Title:Kinetics and molecular docking of dihydroxanthyletin-type coumarins from Angelica decursiva that inhibit cholinesterase and BACE1.
Authors:Ali MYSeong SHJung HAJannat SChoi 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]