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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
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: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]