α-Glucosidase inhibition and antihyperglycemic activity of prenylated xanthones from Garcinia mangostana

Ryu, Hyung Won; Cho, Jung Keun; Long, Marcus J. C.; Yuk, Heung Joo; Kim, Young Soo; Jung, Sunin; Kim, Young Suk; Lee, Byong Won; Park, Ki Hun

doi:10.1016/j.phytochem.2011.08.007

Cited by 152 publications

(125 citation statements)

References 22 publications

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“…The residue was separated by ion-exchange chromatography to give 1 (166 mg, 83%), an enantiomer of 1,6-dideoxynojirimycin (ent-1,6-dDNJ): Enzyme inhibition experiments. α-Glucosidase was assayed according to standard procedures by following the hydrolysis of nitrophenyl glycosides [Ryu et al, 2011] via monitoring formation of p-nitrophenol spectrometrically at 405 nm. The reaction mixture consisted of the enzyme solution (0.02 units α-glucosidase, 50 μL), substrate (1 mM p-nitrophenyl-α-D-glucopyranoside, 50 μL) in 50 mM potassium phosphate buffer (pH 6.8) and test sample in 5% DMSO (10 μL).…”

Section: Methodsmentioning

confidence: 99%

“…The above-mentioned enzymes were from Sigma. All enzyme activities were determined using the appropriate substrates (p-nitrophenyl-α-L-rhamnopyranoside, p-nitrophenyl-α-D-glucopyranoside, p-nitrophenyl-β-D-glucopyranoside, o-nitrophenyl-α-D-mannopyranoside, p-nitrophenyl-α-Dgalactopyranoside, and starch) at the optimum pH of each enzyme [Ryu et al, 2011]. The inhibitory effects of the tested compounds were expressed as the concentrations that inhibited 50% of the enzyme activity (IC 50 ).…”

Section: Methodsmentioning

confidence: 99%

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Piperidine azasugars displaying competitive α-rhamnosidase inhibition and their kinetic mechanism

Cho

Rengasamy

Curtis‐Long

et al. 2011

J Korean Soc Appl Biol Chem

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Azasugars derived from L-alanine and L-serine were screened for inhibitory activity against α-rhamnosidase. The enantiomers of 1,6-dideoxynojirimycin (ent-1,6-dDNJ) (1) and (2S,3R)-2-(hydroxymethyl)piperidin-3-ol (5) showed highly specific and potent inhibition against α-rhamnosidase with K i values of 4.2 and 16.6 μM, respectively. Structure of the best inhibitor features the same stereochemical configuration as L-rhamnose at C2, C3, and C4 centers. In kinetic studies, both compounds exhibited competitive inhibition behavior. Compound 1 manifested simple reversible slow-binding inhibition with the following kinetic parameters: k 3 = 1.17 nM −1 min −1 , k 4 = 5.96 ×10 −3 min −1 , and K i app =5.1 mM.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Piperidine azasugars displaying competitive α-rhamnosidase inhibition and their kinetic mechanism

Cho

Rengasamy

Curtis‐Long

et al. 2011

J Korean Soc Appl Biol Chem

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“…The S. cerevisiae a-glucosidase inhibitory activity was assayed according to standard procedures by following the hydrolysis of nitrophenyl glycosides (Ryu et al 2011). Briefly, the reaction mixture consisted of the enzyme solution (0.02 units a-glucosidase, 50 lL), substrate (1 mM p-nitrophenyl-a-D-glucopyranoside, 50 lL) in 50 mM potassium phosphate buffer (pH 6.8), and test compound in 5 % DMSO (10 lL).…”

Section: Extraction and Isolationmentioning

confidence: 99%

Anti-hyperglycemic activity of polyphenols isolated from barnyard millet (Echinochloa utilis L.) and their role inhibiting α-glucosidase

Seo¹,

Eun²,

Lee

et al. 2015

J Korean Soc Appl Biol Chem

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The extracts and chemical compounds isolated from barnyard millet (Echinochloa utilis) grains were investigated as part of a search for naturally derived antihyperglycemic medicinal plants. Among the five different solvent extracts, the ethyl acetate extract showed the lowest IC 50 value against Saccharomyces cerevisiae a-glucosidase (70.2 lg/mL). Chromatography yielded eight phenolic compounds that may have been responsible for this effect. Among them, N-p-coumaroyl serotonin (1, CS), feruloyl serotonin (2, FS), and luteolin (5) potently inhibited aglucosidase with IC 50 values of 1.3-17.8 lM compared with those of deoxynojirimycin (DNJ, IC 50 = 2.5 ± 0.1 -lM) and acarbose (IC 50 = 255.1 ± 15.6 lM). Additionally, for the first time, we found that CS and FS were significantly inhibited mammalian rat intestinal sucrase (IC 50 of 3.0 and 8.2 lM) and reduced glucose content (73 and 52 % at 0.1 mg/wells) in Caco-2 (human intestinal epithelial) cells. Furthermore, oral glucose tolerance test revealed improved glucose tolerance following treatment with the barnyard millet grains extract by retarding the postprandial rise in blood glucose in vivo. These results suggest that barnyard millet grain can be used as a natural functional medicine to prevent and alleviate type-2 diabetes.

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“…Some plants of Garcinia species have been studied scientifically and are known to have activity as an antidiabetic, among others Garcinia brevipedicellata [5], Garcinia mangostana [6], Garcinia nobilis [7], and Garcinia hanburyi [8]. The bioactive compounds that play a role in the α-glucosidase inhibitor from each of these plants that brevipsidones D, prenylated xanthones, xanthones, and polyprenylated xanthones [5][6][7][8].…”

Section: Introductionmentioning

confidence: 99%

“…The bioactive compounds that play a role in the α-glucosidase inhibitor from each of these plants that brevipsidones D, prenylated xanthones, xanthones, and polyprenylated xanthones [5][6][7][8].…”

Section: Introductionmentioning

confidence: 99%

COMPARISON OF INHIBITORY ACTIVITY AGAINST THE Α-Glucosidase ENZYMES IN THE EXTRACTS AND FRACTIONS FROM LEAVES OF THE GARCINIA KYDIA ROXBURGH

Martha

Elya

Hanafi

2017

Asian J Pharm Clin Res

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Objective: Garcinia kydia Roxb. is a species of the genus Garcinia, is based chemotaxonomic has various bioactive compounds that have been isolated by a variety of pharmacological activities, one of the activities that are being developed that inhibition of α-glucosidase. However, α-glucosidase inhibitory activity in the extracts and fraction from leaves of the G. kydia Roxb. has not been reported. In this study, seeks to evaluate of α-glucosidase inhibitory activity against extracts and fractions of potentially. Methods:The α-glucosidase inhibitory activity test conducted by in vitro using the enzymatic reaction is measured of quantity with a microplate reader and identifies the compound from the active fraction with normal-phase thin layer chromatography. Results:The ethyl acetate and methanol extract have the potential to inhibit the α-glucosidase with the percent inhibition at a concentration of 500 µg/ml of 83% and 59%, respectively. The active fraction of the ethyl acetate extracts (FEA8) with percentage inhibition at concentrations of 100 µg/ml and inhibitory concentration (IC 50 ) values of 80% and 2.79 μg/ml, respectively, and active fraction of the methanol extracts (FMT3) with percent inhibition at concentrations of 100 µg/ml and IC 50 values of 71% and 8.43 μg/ml, respectively. Conclusion: G. kydiaRoxb. evident has the potential to inhibit the α-glucosidase. Flavonoid and phenolic compounds that suspected of acts as α-glucosidase inhibitory activity. Thus, the research will continue the process of isolating the active compound so that it can be developed as natural therapeutic agents in the control of glucose.

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α-Glucosidase inhibition and antihyperglycemic activity of prenylated xanthones from Garcinia mangostana

Cited by 152 publications

References 22 publications

Piperidine azasugars displaying competitive α-rhamnosidase inhibition and their kinetic mechanism

Piperidine azasugars displaying competitive α-rhamnosidase inhibition and their kinetic mechanism

Anti-hyperglycemic activity of polyphenols isolated from barnyard millet (Echinochloa utilis L.) and their role inhibiting α-glucosidase

COMPARISON OF INHIBITORY ACTIVITY AGAINST THE Α-Glucosidase ENZYMES IN THE EXTRACTS AND FRACTIONS FROM LEAVES OF THE GARCINIA KYDIA ROXBURGH

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