Evaluation of the inhibitory effects of eckol and dieckol isolated from edible brown alga Eisenia bicyclis on human monoamine oxidases A and B

• Published in: Archives of pharmacal research 2017, 40(4), , pp.480-491
• Main Authors: Jung, Hyun Ah, Roy, Anupom, Jung, Jee H., Choi, Jae Sue
• Format: Article
• Language: English
• Subjects: Benzofurans - chemistry; Benzofurans - isolation & purification; Benzofurans - pharmacology; Dioxins - chemistry; Dioxins - isolation & purification; Dioxins - pharmacology; Dose-Response Relationship, Drug; Humans; Medicine; Molecular Docking Simulation; Molecular Structure; Monoamine Oxidase - metabolism; Monoamine Oxidase Inhibitors - chemistry; Monoamine Oxidase Inhibitors - isolation & purification; Monoamine Oxidase Inhibitors - pharmacology; Phaeophyceae - chemistry; Pharmacology/Toxicology; Pharmacy; Research Article; Structure-Activity Relationship; 약학
• ISSN: 0253-6269; 1976-3786
• DOI: 10.1007/s12272-017-0904-3

Eckol and dieckol are important phlorotannins found in edible brown algae including Eisenia bicyclis, Ecklonia stolonifera, and others. Inhibition of monoamine oxidase (MAO) play an important role in the early management of Parkinson’s disease (PD). The aim of this study was to determine the effectiveness of eckol and dieckol isolated from the methanolic extract of E. bicyclis against PD by the inhibition of human MAO-A and MAO-B ( h MAO-A and h MAO-B). A sensitive enzyme-based chemiluminescent assay and kinetics methods were used to investigate enzyme inhibition and mode of inhibition. A molecular docking simulation was performed to clarify the binding characteristics of eckol and dieckol to h MAO-A and h MAO-B. The results suggested that methanolic extract of E. bicyclis and its isolated phlorotannins, eckol and dieckol, have potent inhibitory activity against h MAO-A and h MAO-B. The enzyme-based kinetics results demonstrated eckol mixed and non-competitive inhibition of h MAO-A and h MAO-B, respectively, while dieckol non-competitively inhibited both h MAOs. Molecular docking simulation predicted that eckol and dieckol exhibit higher binding affinity towards h MAO-A and h MAO-B through hydrogen bonding and hydrophobic interactions. These findings implicate eckol and dieckol as inhibitors of h MAOs that might be of potential value in the management of PD.