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

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

  • Arch Pharm Res. 2017 Apr;40(4):480-491. doi: 10.1007/s12272-017-0904-3.
Hyun Ah Jung 1 Anupom Roy 2 Jee H Jung 3 Jae Sue Choi 4
Affiliations

Affiliations

  • 1 Department of Food Science and Human Nutrition, Chonbuk National University, Jeonju, 561-756, Republic of Korea.
  • 2 Department of Food and Life Science, Pukyong National University, Busan, 608-737, Republic of Korea.
  • 3 College of Pharmacy, Pusan National University, Busan, 609-735, Republic of Korea.
  • 4 Department of Food and Life Science, Pukyong National University, Busan, 608-737, Republic of Korea. [email protected].
Abstract

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 (hMAO-A and hMAO-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 hMAO-A and hMAO-B. The results suggested that methanolic extract of E. bicyclis and its isolated phlorotannins, eckol and dieckol, have potent inhibitory activity against hMAO-A and hMAO-B. The enzyme-based kinetics results demonstrated eckol mixed and non-competitive inhibition of hMAO-A and hMAO-B, respectively, while dieckol non-competitively inhibited both hMAOs. Molecular docking simulation predicted that eckol and dieckol exhibit higher binding affinity towards hMAO-A and hMAO-B through hydrogen bonding and hydrophobic interactions. These findings implicate eckol and dieckol as inhibitors of hMAOs that might be of potential value in the management of PD.

Keywords

Dieckol; Eckol; Eisenia bicyclis; Enzyme kinetic; MAO inhibitor; Molecular docking.

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