552-58-9Relevant academic research and scientific papers
TNF-α inhibition elicited by mansoins A and B, heterotrimeric flavonoids isolated from mansoa hirsuta
Campana, Priscilla R. V.,Coleman, Christina M.,Teixeira, Mauro M.,Ferreira, Daneel,Braga, Fern?o C.
, p. 824 - 830 (2014)
Mansoins A (1) and B (2) isolated from the fruits of Mansoa hirsuta represent new glucosylated heterotrimeric flavonoids with a flavanone core linked to two 1,3-diarylpropane C6-C3-C6 units. Their structures and absolute c
Optimization of the biosynthesis of b-ring ortho-hydroxy lated flavonoids using the 4-hydroxyphenylacetate 3-hydroxylase complex (Hpabc) of escherichia coli
Chen, Yang,Gao, Liping,Gui, Lin,Guo, Lina,Lei, Ting,Li, Yan,Ma, Xiubing,Ruan, Haixiang,Wang, Longji,Wang, Yunsheng,Xia, Tao
, (2021/05/31)
Flavonoids are important plant metabolites that exhibit a wide range of physiological and pharmaceutical functions. Because of their wide biological activities, such as anti-inflammatory, antioxidant, antiaging and anticancer, they have been widely used in foods, nutraceutical and pharmaceuticals industries. Here, the hydroxylase complex HpaBC was selected for the efficient in vivo production of ortho-hydroxylated flavonoids. Several HpaBC expression vectors were constructed, and the corresponding products were successfully detected by feeding naringenin to vector-carrying strains. However, when HpaC was linked with an S-Tag on the C terminus, the enzyme activity was significantly affected. The optimal culture conditions were determined, including a substrate concentration of 80 mg·L?1, an induction temperature of 28?C, an M9 medium, and a substrate delay time of 6 h after IPTG induction. Finally, the efficiency of eriodictyol conversion from P2&3-carrying strains fed naringin was up to 57.67 ± 3.36%. The same strategy was used to produce catechin and caf-feic acid, and the highest conversion efficiencies were 35.2 ± 3.14 and 32.93 ± 2.01%, respectively. In this paper, the catalytic activity of HpaBC on dihydrokaempferol and kaempferol was demonstrated for the first time. This study demonstrates a feasible method for efficiently synthesizing in vivo B-ring dihydroxylated flavonoids, such as catechins, flavanols, dihydroflavonols and flavonols, in a bacterial expression system.
Semi-synthesis method of eriodictyol
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Paragraph 0028; 0030-0046, (2021/05/29)
The invention relates to the field of chemical synthesis, and particularly relates to a semi-synthesis method of eriodictyol, and aims to solve the problems that raw materials are difficult to obtain, the process is complicated, the cost is high and the yield is low in the synthesis process of the eriodictyol at present. The technical scheme adopted by the invention is as follows: the semi-synthesis method of eriodictyol comprises the steps of 1) mixing neohesperidin and hydrobromic acid in a mass ratio of 1: (5-8), heating after mixing, monitoring a liquid phase until the purity of eriodictyol reaches 89-91% or above, and stopping reaction to obtain a reaction liquid; 2) adding water into the reaction liquid for cooling, and performing suction filtration to obtain a wet crude eriodictyol product; 3) adding ethanol into the wet crude eriodictyol product, and adding activated carbon for decoloration; and 4) after the decoloration is completed, removing the activated carbon, concentrating the ethanol solution dissolved with eriodictyol, standing for crystallization, and carrying out suction filtration and drying to obtain an eriodictyol refined product.
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.
Convenient synthesis of flavanone derivatives via oxa-Michael addition using catalytic amount of aqueous cesium fluoride
Miura, Motofumi,Shigematsu, Karin,Toriyama, Masaharu,Motohashi, Shigeyasu
, (2021/10/25)
A total of 36 flavanones, which included polycyclic aromatic and heterocyclic rings, were readily synthesized via oxa-Michael addition from the corresponding hydroxychalcones with a catalytic amount of aqueous cesium fluoride solution under mild conditions. This method could be applied to the scalable synthesis of eriodictyol as a known potent inhibitor of the SARS-CoV-2 spike protein.
Regioselective O-glycosylation of flavonoids by fungi Beauveria bassiana, Absidia coerulea and Absidia glauca
Sordon, Sandra,Pop?oński, Jaros?aw,Tronina, Tomasz,Huszcza, Ewa
, (2019/02/13)
In the present study, the species: Beauveria bassiana, Absidia coerulea and Absidia glauca were used in biotransformation of flavones (chrysin, apigenin, luteolin, diosmetin) and flavanones (pinocembrin, naringenin, eriodictyol, hesperetin). The Beauveria bassiana AM 278 strain catalyzed the methylglucose attachment reactions to the flavonoid molecule at positions C7 and C3′. The application of the Absidia genus (A. coerulea AM 93, A. glauca AM 177) as the biocatalyst resulted in the formation of glucosides with a sugar molecule present at C7 and C3′ positions of flavonoids skeleton. Nine of obtained products have not been previously reported in the literature.
New Glycosides of Eriodictyol from Dracocephalum palmatum
Olennikov,Chirikova,Kim, Eungyoung,Kim, Sang Woo,Zul’fugarov
, p. 860 - 863 (2018/09/25)
Two new glycosides of eriodictyol were isolated from the aerial part of Dracocephalum palmatum and identified using UV, NMR, and CD spectroscopy and mass spectrometry as (S)-eriodictyol-7-O-(6′′-O-malonyl)-β-Dglucopyranoside (pyracanthoside-6′′ -O-malonat
Enhanced antioxidant activity, antibacterial activity and hypoglycemic effect of luteolin by complexation with manganese(II) and its inhibition kinetics on xanthine oxidase
Dong, Hao,Yang, Xiaocui,He, Jiapeng,Cai, Sheng,Xiao, Kaijun,Zhu, Liang
, p. 53385 - 53395 (2017/12/02)
The present study aims to improve the biological activities of luteolin by complexation with manganese(ii). UV-visible spectroscopy, infrared spectroscopy, thermogravimetric analysis and elemental analysis were adopted to assess the relevant interaction of luteolin and manganese(ii) ions and the chelation sites. The antioxidant activity, hypoglycemic effect and antimicrobial activity of luteolin-manganese(ii) complex with respect to its parent luteolin and the inhibition effect of which on xanthine oxidase were investigated and compared. The spectroscopic data indicated that luteolin reacts with manganese(ii) cations through the chelation sites of 5-hydroxy and 4-carbonyl in two luteolin molecules. Antioxidant and antibacterial activity were enhanced after the complexation of manganese(ii) cations with luteolin. An inhibition effect assay found that luteolin and luteolin-manganese(ii) complex reversibly inhibited xanthine oxidase in a competitive manner. Luteolin-manganese(ii) complex had a more remarkable hypoglycemic effect than luteolin by increasing the glucose consumption in liver tissue.
Selective and efficient oxidative modifications of flavonoids with 2-iodoxybenzoic acid (IBX)
Barontini, Maurizio,Bernini, Roberta,Crisante, Fernanda,Fabrizi, Giancarlo
experimental part, p. 6047 - 6053 (2010/09/11)
2-Iodoxybenzoic acid (IBX), a mild and efficient hypervalent iodine oxidant, has been utilised in different reaction conditions to perform several efficient oxidative modifications of flavonoids. Fine-tuning of the reaction conditions allowed remarkably selective modifications of these compounds. At room temperature, IBX proved to be an excellent reagent for a highly regioselective aromatic hydroxylation of monohydroxylated flavanones and flavones, generating the corresponding catecholic derivatives showing high antioxidant activity. At 90 °C, IBX efficiently dehydrogenated a large panel of methoxylated flavanones to their corresponding flavones exhibiting anticancer activity. IBX polystyrene has also been utilised to increase the recovery of highly polar compounds. Following the first oxidation, the reagent was recovered and reused in several runs without loss of efficiency and selectivity. The first example of an application of IBX polystyrene in a dehydrogenation reaction has been described.
Directed evolution of the Actinomycete Cytochrome P450 MoxA (CYP105) for enhanced activity
Kabumoto, Hiroki,Miyazaki, Kentaro,Arisawa, Akira
experimental part, p. 1922 - 1927 (2010/07/02)
Actinomycete cytochrome P450 from Nonomuraea recticatena NBRC 14525 (P450moxA) catalyzes the hydroxylation of a broad range of substrates, including fatty acids, steroids, and various aromatic compounds. Hence, the enzyme is potentially useful in medicinal applications, but the activity is insufficient for practical use. Here we applied directed evolution to enhance the activity. A random mutagenesis library was screened using 7-ethoxycoumarin as a substrate to retrieve 17 variants showing 2-fold activities. Twenty-five amino acid substitutions were found in the variants, of which five mutations were identified to have the largest effects (Q87W, T115A, H132L, R191W, and G294D). These mutations additively increased the activity; the quintet mutant had 20-times the activity of the wildtype. These five single mutations also increased in activity toward structurally distinct substrates (diclofenac and naringe- nin). Based on the three-dimensional structure of the enzyme, we discerned that mutations in the substrate recognition site improved the activity, which was substrate dependent; mutations apart from the active site improved the activity as well as the substrates did.
