Synthesis of furocoumarin-stilbene hybrids as potential multifunctional drugs against multiple biochemical targets associated with Alzheimer's disease

被引：24

作者：

Agbo, Emmanuel N. ^{[1
]}

Gildenhuys, Samantha ^{[2
]}

Choong, Yee Siew ^{[3
]}

Mphahlele, Malose J. ^{[1
]}

More, Garland K. ^{[2
]}

机构：

[1] Univ South Africa, Coll Sci Engn & Technol, Dept Chem, Private Bag X06, ZA-1710 Florida, South Africa

[2] Univ South Africa, Coll Agr & Environm Sci, Dept Life & Consumer Sci, Private Bag X06, ZA-1710 Florida, South Africa

[3] Univ Sains Malaysia, Inst Res Mol Med INFORMM, George Town 11800, Malaysia

来源：

BIOORGANIC CHEMISTRY | 2020年 / 101卷

基金：

新加坡国家研究基金会;

关键词：

Furocoumarin-stilbene hybrids; Cholinesterases; beta-secretase; Cyclooxygenase-2; lipoxygenase-5; Antioxidant effect; Molecular docking; COUMARIN DERIVATIVES; IN-VITRO; BIOLOGICAL EVALUATION; MOLECULAR DOCKING; DIRECTED LIGANDS; ACETYLCHOLINESTERASE; RESVERATROL; INHIBITION; CHOLINESTERASE; PTEROSTILBENE;

D O I：

10.1016/j.bioorg.2020.103997

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A series of furocoumarin-stilbene hybrids has been synthesized and evaluated in vitro for inhibitory effect against acetylcholinesterase (AChE), butyrylcholinestarase (BChE), D-secretase, cyclooxygenase-2 (COX-2), and lipox-ygenase-5 (LOX-5) activities including free radical-scavenging properties. Among these hybrids, 8-(3,5-di-methoxyphenyl)-4-(3,5-dimethoxystyryl)furochromen-2-one 4h exhibited significant anticholinesterase activity and inhibitory effect against beta-secretase, COX-2 and LOX-5 activities. 2,2-Diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity and an in vitro cell-based antioxidant activity assay involving lipopolysaccharide induced reactive oxygen species production revealed that 4h has capability of scavenging free radicals. Molecular docking into AChE, BChE, beta-secretase, COX-2 and LOX-5 active sites has also been performed.

引用

页数：13

共 62 条

[1] Synthesis and molecular docking studies of imines as α-glucosidase and α-amylase inhibitors [J].