Planta Medica Letters 2016; 3(01): e17-e19
DOI: 10.1055/s-0042-102460
Letter
Georg Thieme Verlag KG Stuttgart · New York

Miconidin Acetate and Primin as Potent 5-Lipoxygenase Inhibitors from Brazilian Eugenia hiemalis (Myrtaceae)

Gabriele Andressa Zatelli
1  Laboratory of Natural Products, Department of Pharmaceutical Sciences, Federal University of Santa Catarina, Florianopolis, Brazil
,
Veronika Temml
2  Institute of Pharmacy/Pharmacognosy, Institute of Pharmacy and Center for Molecular Biosciences Innsbruck (CMBI), Innsbruck, Austria
,
Zsofia Kutil
3  Laboratory of Plant Biotechnologies, Institute of Experimental Botany AS CR, v. v. i., Prague, Czech Republic
,
Premysl Landa
3  Laboratory of Plant Biotechnologies, Institute of Experimental Botany AS CR, v. v. i., Prague, Czech Republic
,
Tomas Vanek
3  Laboratory of Plant Biotechnologies, Institute of Experimental Botany AS CR, v. v. i., Prague, Czech Republic
,
Daniela Schuster
4  Computer-Aided Molecular Design Group, Institute of Pharmaceutical Chemistry, and Center for Molecular Biosciences Innsbruck (CMBI), Innsbruck, Austria
,
Miriam Falkenberg
1  Laboratory of Natural Products, Department of Pharmaceutical Sciences, Federal University of Santa Catarina, Florianopolis, Brazil
› Author Affiliations
Further Information

Publication History

received 24 September 2015
revised 24 December 2015

accepted 24 January 2016

Publication Date:
14 March 2016 (online)

Abstract

This paper describes the isolation and identification of primin and miconidin acetate as metabolites from the flower bud extract of Eugenia hiemalis as well as the anti-inflammatory activity of miconidin acetate by inhibition of 5-lipoxygenase. Miconidin acetate inhibited leukotriene B4 formation catalyzed by the human recombinant enzyme (IC50 = 0.3 ± 0.17 µM) more than primin (IC50 = 1.4 ± 0.6 µM) and zileuton (IC50 = 1.1 ± 0.7 µM). Miconidin acetate (20 µM) inhibited LTB4 formation to an extent of 59 ± 12 % in vitro using a cell-based assay, comparable to the positive control zileuton (69 ± 12 % inhibition at a concentration of 10 µM). The binding modes of miconidin acetate were further evaluated in silico by molecular docking to the human 5-lipoxygenase crystal structure. The hydroxyl group was predicted to form a hydrogen bond with the terminal Ile676, while the pentyl moiety occupied the hydrophobic substrate channel. The obtained results show that flower buds of E. hiemalis are an interesting source of anti-inflammatory compounds, mainly of miconidin acetate.

Supporting Information