PERFORM Publications

Keyword search (4,163 papers available)

Title		Authors	PubMed ID
1	The enterobactin biosynthetic intermediate 2,3-dihydroxybenzoic acid is a competitive inhibitor of the Escherichia coli isochorismatase EntB	Bin X; Pawelek PD;	40400396 CHEMBIOCHEM
2	Evidence of isochorismate channeling between the Escherichia coli enterobactin biosynthetic enzymes EntC and EntB	Bin X; Pawelek PD;	39031458 CHEMBIOCHEM
3	New Megastigmane and Polyphenolic Components of Henna Leaves and Their Tumor-Specific Cytotoxicity on Human Oral Squamous Carcinoma Cell Lines	Orabi MAA; Orabi EA; Awadh AAA; Alshahrani MM; Abdel-Wahab BA; Sakagami H; Hatano T;	38001804 CHEMBIOCHEM
4	Structural determination and anticholinesterase assay of C-glycosidic ellagitannins from Lawsonia inermis leaves: A study supported by DFT calculations and molecular docking	Orabi MAA; Orabi EA; Abdel-Sattar ES; English AM; Hatano T; Elimam H;	36423882 CHEMBIOCHEM
5	Evidence of an intracellular interaction between the Escherichia coli enzymes EntC and EntB and identification of a potential electrostatic channeling surface	Ouellette S; Pakarian P; Bin X; Pawelek PD;	35952947 CHEMBIOCHEM
6	Identifying potential drug targets and candidate drugs for COVID-19: biological networks and structural modeling approaches	Selvaraj G; Kaliamurthi S; Peslherbe GH; Wei DQ;	33968364 CERMM
7	Angiotensin-I-Converting Enzyme Inhibitory Activity of Coumarins from Angelica decursiva.	Ali MY, Seong SH, Jung HA, Choi JS	31683604 CHEMBIOCHEM
8	Umbelliferone derivatives exert neuroprotective effects by inhibiting monoamine oxidase A, self-amyloidβ aggregation, and lipid peroxidation.	Seong SH, Ali MY, Jung HA, Choi JS	31557622 CHEMBIOCHEM
9	Virtual screening, docking, and dynamics of potential new inhibitors of dihydrofolate reductase from Yersinia pestis.	Bastos Lda C, de Souza FR, Guimarães AP, Sirouspour M, Cuya Guizado TR, Forgione P, Ramalho TC, França TC	26494420 CHEMISTRY
10	Mechanistic studies of new oximes reactivators of human butyryl cholinesterase inhibited by cyclosarin and sarin.	de Lima WE, Francisco A, da Cunha EF, Radic Z, Taylor P, França TC, Ramalho TC	27125569 CHEMISTRY
11	Flavanone glycosides inhibit β-site amyloid precursor protein cleaving enzyme 1 and cholinesterase and reduce Aβ aggregation in the amyloidogenic pathway.	Ali MY, Jannat S, Edraki N, Das S, Chang WK, Kim HC, Park SK, Chang MS	31194956 BIOLOGY

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
Publication:	Bioorganic chemistry
Keywords:	6-Formyl umbelliferone; Aβ; self-aggregation; Computational docking; Enzyme kinetics; MAO-A; Neuropsychiatric disorder;
PMID:	31557622	Category:	Bioorg Chem	Date Added:	2019-09-27
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]

BookR: School of Health Core Facilities Booking

"docking" Keyword-tagged Publications:

Search Publications

No results