A series of cinnamic acid derivatives and their inhibitory activity on intestinal α-glucosidase

Adisakwattana, Sirichai; Chantarasinlapin, Praew; Thammarat, Haruthai; Yibchok-anun, Sirintorn

doi:10.1080/14756360902779326

Cited by 185 publications

(106 citation statements)

References 28 publications

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“…It was likely that the more phenolic group in cinnamoyl moiety, the more potent inhibition observed. This result was similar to previous report of intestinal a-glucosidase inhibition of hydroxylated cinnamic derivatives 6, 7 and 8 [10]. This trend was obviously found in 6a, whose inhibition against maltase was more potent than those of 7a (10 times) and 8a (4 times); while 8a showed only two times more potent than 7a (Table 2).…”

Section: A-glucose Inhibitory Activity and Dpph Radical Scavengingsupporting

confidence: 93%

Quercitylcinnamates, a new series of antidiabetic bioconjugates possessing α-glucosidase inhibition and antioxidant

Rattanangkool

Kittikhunnatham

Damsud

et al. 2013

European Journal of Medicinal Chemistry

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Section: A-glucose Inhibitory Activity and Dpph Radical Scavengingsupporting

confidence: 93%

Quercitylcinnamates, a new series of antidiabetic bioconjugates possessing α-glucosidase inhibition and antioxidant

Rattanangkool

Kittikhunnatham

Damsud

et al. 2013

European Journal of Medicinal Chemistry

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“…. Ferulic acid was also reported to inhibit intestinal α-glucosidase enzyme activity with an IC 50 value of 0.45 mM (Adisakwattana et al 2009). …”

Section: α-Amylase and α-Glucosidase Inhibition By Mango Peel Extractmentioning

confidence: 96%

Ethanol extract of mango (Mangifera indica L.) peel inhibits α-amylase and α-glucosidase activities, and ameliorates diabetes related biochemical parameters in streptozotocin (STZ)-induced diabetic rats

Gondi

Rao

2015

J Food Sci Technol

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Peel is a major by-product during processing of mango fruit into pulp. Recent report indicates that the whole peel powder ameliorated diabetes. In the present study, ethanolic extract of mango peel was analysed for its bioactive compounds, evaluated for α-amylase and α-glucosidase inhibitory properties, oral glucose tolerance test, antioxidant properties, plasma insulin level and biochemical parameters related to diabetes. In addition to gallic and protocatechuic acids, the extract also had chlorogenic and ferulic acids, which were not reported earlier in mango peel extracts. The peel extract inhibited α-amylase and α-glucosidase activities, with IC50 values of 4.0 and 3.5 μg/ml. Ethanolic extract of peel showed better glucose utilization in oral glucose tolerance test. Treatment of streptozotocin-induced diabetic rats with the extract decreased fasting blood glucose, fructosamine and glycated hemoglobin levels, and increased plasma insulin level. Peel extract treatment decreased malondialdehyde level, but increased the activities of antioxidant enzymes significantly in liver and kidney compared to diabetic rats. These beneficial effects were comparable to metformin, but better than gallic acid treated diabetic rats. The beneficial effects of peel extract may be through different mechanism like increased plasma insulin levels, decreased oxidative stress and inhibition of carbohydrate hydrolyzing enzyme activities by its bioactive compounds. Thus, results suggest that the peel extract can be a potential source of nutraceutical or can be used in functional foods and this is the first report on antidiabetic properties of mango peel extract.

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“…Inhibition Assay for Intestinal α-glucosidase and Pancreatic α-amylase Activity α-Glucosidase and pancreatic α-amylase inhibitory activities of cinnamon extract were assayed according to our previous paper [18]. Acarbose was used as a positive control for this assay.…”

Section: Hplc Analysismentioning

confidence: 99%

Inhibitory Activity of Cinnamon Bark Species and their Combination Effect with Acarbose against Intestinal α-glucosidase and Pancreatic α-amylase

Adisakwattana

Lerdsuwankij

Poputtachai

et al. 2011

Plant Foods Hum Nutr

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162

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Inhibition of α-glucosidase and pancreatic α-amylase is one of the therapeutic approaches for delaying carbohydrate digestion, resulting in reduced postprandial glucose. The aim of this study was to evaluate the phytochemical analysis and the inhibitory effect of various cinnamon bark species against intestinal α-glucosidase and pancreatic α-amylase. The results showed that the content of total phenolic, flavonoid, and condensed tannin ranged from 0.17 to 0.21 g gallic acid equivalent/g extract, from 48.85 to 65.52 mg quercetin equivalent/g extract, and from 0.12 to 0.15 g catechin equivalent/g extract, respectively. The HPLC fingerprints of each cinnamon species were established. Among cinnamon species, Thai cinnamon extract was the most potent inhibitor against the intestinal maltase with the IC(50) values of 0.58 ± 0.01 mg/ml. The findings also showed that Ceylon cinnamon was the most effective intestinal sucrase and pancreatic α-amylase inhibitor with the IC(50) values of 0.42 ± 0.02 and 1.23 ± 0.02 mg/ml, respectively. In addition, cinnamon extracts produced additive inhibition against intestinal α-glucosidase and pancreatic α-amylase when combined with acarbose. These results suggest that cinnamon bark extracts may be potentially useful for the control of postprandial glucose in diabetic patients through inhibition of intestinal α-glucosidase and pancreatic α-amylase.

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A series of cinnamic acid derivatives and their inhibitory activity on intestinal α-glucosidase

Cited by 185 publications

References 28 publications

Quercitylcinnamates, a new series of antidiabetic bioconjugates possessing α-glucosidase inhibition and antioxidant

Quercitylcinnamates, a new series of antidiabetic bioconjugates possessing α-glucosidase inhibition and antioxidant

Ethanol extract of mango (Mangifera indica L.) peel inhibits α-amylase and α-glucosidase activities, and ameliorates diabetes related biochemical parameters in streptozotocin (STZ)-induced diabetic rats

Inhibitory Activity of Cinnamon Bark Species and their Combination Effect with Acarbose against Intestinal α-glucosidase and Pancreatic α-amylase

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