Synthesis and biological evaluation of a novel baicalein glycoside as an anti-inflammatory agent

Kim, Kyun Ha; Park, Young-Don; Park, Heejin; Moon, Keumok; Ha, Ki‐Tae; Baek, Nam‐In; Park, Cheon-Seok; Joo, Myungsoo; Cha, Jaeho

doi:10.1016/j.ejphar.2014.10.013

Cited by 42 publications

(41 citation statements)

References 41 publications

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“…Although we did not quantify this parameter, it is clear from the HPLC behaviour (Fig. S1), extraction experiments with organic solvents (not shown) and the results of others (Kim et al, 2014) that the aqueous solubility of the parent compound was greatly enhanced by the glucosylation(s).…”

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confidence: 86%

“…They are the first reported phloretin glycosides that possess an ␣ sugar-aglycone linkage. Acceptors that previously have been shown to be glucosylated by Ams enzymes are sugars (Daudé et al, 2013;Schneider et al, 2010) and sugar alcohols (Daudé et al, 2013), hydroquinone (Seo et al, 2012), catechin (Cho et al, 2011), baicalein (Kim et al, 2014), arbutin (Seo et al, 2009), salicin ) and piceid . Therefore, the results described here establish, for the first time, the acceptance of unglycosylated as well as glycosylated chalcone-type compounds as substrates for Glc transfer by a non-Leloir glycosyltransferase.…”

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confidence: 96%

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Biotransformation of phloretin by amylosucrase yields three novel dihydrochalcone glucosides

Overwin

Wray

Höfer

2015

Journal of Biotechnology

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confidence: 86%

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confidence: 96%

Biotransformation of phloretin by amylosucrase yields three novel dihydrochalcone glucosides

Overwin

Wray

Höfer

2015

Journal of Biotechnology

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“…Kim et al (2014) reported the glucosylation of baicalein with this enzyme in 60 % yield. A comparison of the crystal structures of the Neisseria and Deinococcus enzymes (Guérin et al 2012;Mirza et al 2001) revealed significant differences at the acceptor subsites +1 and +2, which may increase ligand accessibility for the Deinococcus enzyme, compared to the Neisseria AS.…”

Section: Acceptance Of Flavones and Flavanes By Ams And Gtfrmentioning

confidence: 97%

“…Thus, enzymatic glycosylations are an increasingly interesting alternative. A number of enzymes, including cellulase, α-glucosidase (Gao et al 2000), α-amylase (Gao et al 2000;Noguchi et al 2008a), cyclodextrin glucanotransferase (Aramsangtienchai et al 2011;Funayama et al 1993), sucrose phosphorylase (Kitao et al 1993), glucansucrases (GSs) (Bertrand et al 2006;Meulenbeld et al 1999;Moon et al 2007;Woo et al 2012), amylosucrases (ASs) (Cho et al 2011;Kim et al 2014), a glycosidase variant (Yang et al 2007) and UDP-dependent glycosyltransferases (Kim et al 2015;Noguchi et al 2008b), have been tried for flavonoid glycosylation with varying success.…”

Section: Introductionmentioning

confidence: 99%

Flavonoid glucosylation by non-Leloir glycosyltransferases: formation of multiple derivatives of 3,5,7,3′,4′-pentahydroxyflavane stereoisomers

Overwin

Wray

Höfer

2015

Appl Microbiol Biotechnol

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Flavonoids are known to possess a multitude of biological activities. Therefore, diversification of the core structures is of considerable interest. One of nature's important tailoring reactions in the generation of bioactive compounds is glycosylation, which is able to influence numerous molecular properties. Here, we examined two non-Leloir glycosyltransferases that use sucrose as an inexpensive carbohydrate donor, glycosyltransferase R from Streptococcus oralis (GtfR) and amylosucrase from Neisseria polysaccharea (Ams), for the glucosylation of flavonoids. Flavones generally were poor substrates. Several inhibited Ams. In contrast, flavanes were well accepted by both enzymes. All glucose attachments occurred via α1 linkages. Comparison of the three available stereoisomers of 3,5,7,3',4'-pentahydroxyflavane revealed significant differences in glycoside formation between them as well as between the two enzymes. The latter were shown to possess largely complementary product ranges. Altogether, three of the four hydroxy substituents of the terminal flavonoid rings were glycosylated. Typically, Ams glucosylated the B ring at position 3', whereas GtfR glucosylated this ring at position 4' and/or the A ring at position 7. In several instances, short carbohydrate chains were attached to the aglycones. These contained α 1-4 linkages when formed by Ams, but α 1-3 bonds when generated by GtfR. The results show that both enzymes are useful catalysts for the glucodiversification of flavanes. In total, more than 16 products were formed, of which seven have previously not been described.

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“…Addition of a sugar moiety to the biologically active compounds by glycosylation can improve their biological activities as well as the low water solubility and low absorption rate in small intestine [6,7,9,20]. The β-glucosidase from hyperthermophilic bacterium Thermotoga neapolitana has been successfully used to attach the sugar moiety to the various biologically active compounds and the resultant glycosylated compounds enhanced solubility and biological half-life [4,8,16].…”

Section: Introductionmentioning

confidence: 99%

Optimization of Glycosyl Aesculin Synthesis by Thermotoga neapolitana β-Glucosidase Using Response-surface Methodology

Park¹,

Park²,

Cha³

2017

Journal of Life Science

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Glycosyl aesculin, a potent anti-inflammatory agent, was synthesized by transglycosylation reaction, catalyzed by Thermotoga neapolitana β-glucosidase, with aesculin as an acceptor. The key reaction parameters were optimized using response-surface methodology (RSM) and 2 μg of the enzyme. As shown by a statistical analysis, a second-order polynomial model fitted well to the data (p<0.05). The response surface curve for the interaction between aesculin and other parameters revealed that the aesculin concentration and reaction time were the primary factors that affected the yield of glycosyl aesculin. Among the tested factors, the optimum values for glycosyl aesculin production were as follows: aesculin concentration of 9.5 g/l, temperature of 84℃, reaction time of 81 min, and pH of 8.2. Under these conditions, 61.7% of glycosyl aesculin was obtained, with a predicted yield of 5.86 g/l.The maximum amount of glycosyl aesculin was 6.02 g/l. Good agreement between the predicted and experimental results confirmed the validity of the RSM. The optimization of reaction conditions by RSM resulted in a 1.6-fold increase in the production of glycosyl aesculin as compared to the yield before optimization. These results indicate that RSM can be effectively used for process optimization in the synthesis of a variety of biologically active glycosides using bacterial glycosidases.

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Synthesis and biological evaluation of a novel baicalein glycoside as an anti-inflammatory agent

Cited by 42 publications

References 41 publications

Biotransformation of phloretin by amylosucrase yields three novel dihydrochalcone glucosides

Biotransformation of phloretin by amylosucrase yields three novel dihydrochalcone glucosides

Flavonoid glucosylation by non-Leloir glycosyltransferases: formation of multiple derivatives of 3,5,7,3′,4′-pentahydroxyflavane stereoisomers

Optimization of Glycosyl Aesculin Synthesis by Thermotoga neapolitana β-Glucosidase Using Response-surface Methodology

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