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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:Umbelliferone derivatives exert neuroprotective effects by inhibiting monoamine oxidase A, self-amyloidβ aggregation, and lipid peroxidation.
Authors:Seong SH,  Ali MY,  Jung HA,  Choi JS
Link:https://www.ncbi.nlm.nih.gov/pubmed/31557622?dopt=Abstract
DOI:10.1016/j.bioorg.2019.103293
Category:Bioorg Chem
PMID:31557622
Dept Affiliation: CHEMBIOCHEM
1 Department of Food and Life Science, Pukyong National University, Busan 48513, Republic of Korea.
2 Department of Chemistry and Biochemistry, Faculty of Arts and Science, Concordia University, 7141 Sherbrooke St. W., Montreal, Quebec, Canada; Centre for Structural and Functional Genomic, Department of Biology, Faculty of Arts and Science, Concordia University, 7141, Sherbrooke St. W., Montreal, Quebec, Canada.
3 Department of Food Science and Human Nutrition, Chonbuk National University, Jeonju 54896, Republic of Korea. Electronic address: jungha@jbnu.ac.kr.
4 Department of Food and Life Science, Pukyong National University, Busan 48513, Republic of Korea. Electronic address: choijs@pknu.ac.kr.

Description:

Umbelliferone derivatives exert neuroprotective effects by inhibiting monoamine oxidase A, self-amyloidß aggregation, and lipid peroxidation.

Bioorg Chem. 2019 Sep 18;92:103293

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

Abstract

Umbelliferone has been demonstrated to have a wide range of biological activities. However, the effect of incorporating a formyl moiety in the umbelliferone scaffold has not been investigated. In this paper, we investigated the inhibitory activity of six coumarins, namely umbelliferone (1), 6-formyl umbelliferone (2), 8-formyl umbelliferone (3), umbelliferone-6-carboxylic acid (4), esculetin (5), and scopoletin (6) against human monoamine oxidases (hMAOs), self-amyloid ß (Aß) aggregation, and lipid peroxidation. We found that all compounds had high selectivity for hMAO-A in comparison with hMAO-B. Among the compounds, 2 exhibited the highest hMAO inhibitory activity with an IC50 value of 3.23?µM for hMAO-A and 15.31?µM for hMAO-B. Enzyme kinetic analysis showed that 2 and 3 were competitive hMAO inhibitors. In silico hydrated molecular docking simulations revealed that the coumarins interacted with substrate-binding site residues of the enzymes and the isoalloxazine ring of FAD. In addition, formyl coumarins 2 and 3 significantly inhibited lipid peroxidation in rat brain homogenates and self-Aß25-35 aggregation compared to other derivatives. These represent the first experimental and modelling data for hMAO-A/B inhibition by umbelliferone derivatives. Together, the data suggest that introduction of a formyl moiety in the 7-hydroxycoumarin scaffold, especially at the 6 position, plays an important role in the inhibition of hMAOs, Aß self-aggregation, and lipid peroxidation. Umbelliferone derivative 2 is a promising therapeutic lead scaffold for developing anti-neuropsychiatric disorder drugs that function via selective hMAO-A inhibition.

PMID: 31557622 [PubMed - as supplied by publisher]