17654-19-2Relevant articles and documents
Enantiomers of naringenin as pleiotropic, stereoselective inhibitors of cytochrome P450 isoforms
Lu, Wenjie Jessie,Ferlito, Valentina,Xu, Cong,Flockhart, David Alastair,Caccamese, Salvatore
, p. 891 - 896 (2011)
Interactions between naringenin and the cytochrome P450 (CYP) system have been of interest since the first demonstration that grapefruit juice reduced CYP3A activity. The effects of naringenin on other CYP isoforms have been less investigated. In addition
Chiral separation of novel iminonaringenin derivatives
Bouanini, Meriem,Belboukhari, Nasser,Menéndez, J. Carlos,Sekkoum, Khaled,Cheriti, Abdelkarim,Aboul-Enein, Hassan Y.
, p. 484 - 490 (2018)
A series of 4-iminonaringenin derivatives 2-6 have been prepared in good overall yields from a condensation reaction between naringenin and primary amines. The structures of all products were confirmed by ultraviolet, infrared, proton nuclear magnetic resonance, and carbon-13 nuclear magnetic resonance spectroscopic techniques. These derivatives were analyzed by high-performance liquid chromatography using polysaccharide-based chiral stationary phases, namely, Chiralpak IB and Chiralcel OD, using various mobile phases. 2-Propanol showed a high enantioselectivity for naringin and its derivatives using achiral column containing immobilized polysaccharides (Chiralpak IB).
Medicinal flowers. xxvii.1) New flavanone and chalcone glycosides, arenariumosides i, ii, iii, and iv, and tumor necrosis factor-α inhibitors from everlasting, flowers of helichrysum arenarium
Toshio Morikawa,Li-Bo Wang,Seikou Nakamura,Kiyofumi Ninomiya,Eri Yokoyama,Hisashi Matsuda,Osamu Muraoka,Li-Jun Wu,Yoshikawa, Masayuki
, p. 361 - 367 (2009)
The methanolic extract from the flowers of Helichrysum arenarium L. Moench was found to show inhibitory effect on tumor necrosis factor-α (TNF-α, 1 ng/ml)-induced cytotoxicity in L929 cells. From the methanolic extract, 50 constituents including four new
Discovery of Novel Bacterial Chalcone Isomerases by a Sequence-Structure-Function-Evolution Strategy for Enzymatic Synthesis of (S)-Flavanones
Bornscheuer, Uwe T.,Brückner, Stephan I.,Gei?ler, Torsten,Gross, Egon,Hartmann, Beate,Ley, Jakob P.,Meinert, Hannes,R?ttger, Carsten,Schuiten, Eva,Yi, Dong,Zirpel, Bastian
supporting information, p. 16874 - 16879 (2021/07/06)
Chalcone isomerase (CHI) is a key enzyme in the biosynthesis of flavonoids in plants. The first bacterial CHI (CHIera) was identified from Eubacterium ramulus, but its distribution, evolutionary source, substrate scope, and stereoselectivity are still unclear. Here, we describe the identification of 66 novel bacterial CHIs from Genbank using a novel Sequence-Structure-Function-Evolution (SSFE) strategy. These novel bacterial CHIs show diversity in substrate specificity towards various hydroxylated and methoxylated chalcones. The mutagenesis of CHIera according to the substrate binding models of these novel bacterial CHIs resulted in several variants with greatly improved activity towards these chalcones. Furthermore, the preparative scale conversion catalyzed by bacterial CHIs has been performed for five chalcones and revealed (S)-selectivity with up to 96 % ee, which provides an alternative biocatalytic route for the synthesis of (S)-flavanones in high yields.