Yeast and mammalian α-glucosidase inhibitory constituents from Himalayan rhubarb Rheum emodi Wall.ex Meisson

Babu, K. Suresh; Tiwari, Ashok Kumar; Srinivas, P.; Ali, Amtul Z.; Raju, B. China; Rao, J. Madhusudana

doi:10.1016/j.bmcl.2004.04.062

Cited by 123 publications

(23 citation statements)

References 11 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The assay was conducted as described previously [27,28] with some modifications. This assay uses p-nitrophenyl-α-D-glucopyranoside (pNPG) as the substrate, which is hydrolyzed by α-glucosidase to release p-nitrophenol.…”

Section: α-Glucosidase Inhibition Assaymentioning

confidence: 99%

Total Phenolics, Antioxidant Activity and Anti-Diabetic Capacities of Selected Iraqi Medicinal Plants

Molan¹,

Mahdy²

2016

AJLSR

View full text Add to dashboard Cite

Introduction: In Iraq, medicinal plants have not received much attention in terms of quantifying their antioxidant and other biological/pharmacological activities so the objective of the present study was to assess the antioxidant activity of selected medicinal plants grown in Iraq and relate it to their total phenolic contents and their inhibitory effect on carbohydrate-hydrolyzing enzymes. Methods: Antioxidant activity was assessed by ferric reducing antioxidant power (FRAP) and oxygen reactive absorbance capacity (ORAC) methods. The possible inhibitory effect on carbohydrate-hydrolyzing enzymes was also investigated. Results: In almost all the parameters used, the aqueous extracts from Mentha piperita showed significantly higher (P < 0.0001) activities than other plants. Antioxidant activity was significantly correlated (P < 0.0001) with TPC among all the plants studied. In addition, the plant extracts showed strong inhibition against pancreatic α-amylase and yeast α-glucosidase. Only Cyperus rotundus and Prosopis farcta have been used traditionally for the treatment of diabetes in Iraq. Conclusions:In conclusion, to the best of our knowledge, the remaining four plants and herbs (Glycyrrhiza glabra, H. Sabdariffa, Matricaria chamomilla, and M. piperita) have no records in the literature for their antidiabetic effects. Consequently, this study identifies these four medicinal plants as novel inhibitors of key enzymes (α-glucosidase and α-amylase) relevant for type 2 diabetes that showed even higher activity than the currently being used for the treatment of diabetes by the Iraqi herbalists.

show abstract

Section: α-Glucosidase Inhibition Assaymentioning

confidence: 99%

Total Phenolics, Antioxidant Activity and Anti-Diabetic Capacities of Selected Iraqi Medicinal Plants

Molan¹,

Mahdy²

2016

AJLSR

View full text Add to dashboard Cite

show abstract

“…The enzyme, which belongs to Glycoside Hydrolases family 13, has common specific structural features such as the catalytic ( / ) 8 -barrel domain, which acts specifically on -1,4-and -1,6-O-glucosidic linkages [2][3][4][5]. YAGH has been extensively used to identify its inhibitors from traditional medicine plants [6,7] and food items [8] and these inhibitors from plants and foods have shown potential biological function, such as antihyperglycemic potential [9], antioxidant ability [10], etc. It is also useful to enrich the chemical library that is used in screening assays with molecules that are likely to have biological activities by selecting YAGH as the target protein [11,12].…”

Section: Introductionmentioning

confidence: 99%

Inhibition Kinetics of Flavonoids on Yeast α-Glucosidase Merged with Docking Simulations

2010

PPL

View full text Add to dashboard Cite

Flavonoids, also called vitamin P, are widely distributed in plants fulfilling many functions. Yeast α-glucosidase (YAGH; EC 3.2.1.20), as extensively used target protein for screening bioactive compounds from medicine plants, was selected to explore the possible mechanisms of multiple biological function of flavonoids. The results in this study indicated that flavonoids, as mixed-type inhibitors, quenched the intrinsic fluorescence of YAGH by a mixed fluorescence quenching mechanism. The interaction information between flavonoids and YAGH was analyzed using a flexible docking method (AutoDock) and showed that 3', 4' dihydroxyl groups of B ring and 3-OH of C ring played a more important role in the inhibition activity than other hydroxyl groups, because the 3', 4' dihydroxyl groups of B ring directly interacted with the active-site residues of YAGH to inhibit enzyme activity and 3-OH of C ring seemed to be necessary to maintain the proper binding orientation of flavonoid molecules, thereby making the hydroxyl groups of B ring interact with active-site residues tightly in the hydrophobic pocket of YAGH. The results supply a basis for understanding the mechanisms of multiple biological functions of flavonoids.

show abstract

“…Natural and synthetic inhibitors of alpha-glucosidase have been identified11,24–27, but their inhibitory effect depended greatly to the enzyme's origin. Major differences have been observed between yeast and mammalian alpha-glucosidase activity28, whereas in a recent report the results of hydrolyzing activity of small intestinal disaccharidases from rats showed that experiments evaluating inhibitors on rat intestinal enzymes could substitute for evaluations using human enzymes29.…”

Section: Discussionmentioning

confidence: 99%

Peptide modulators of alpha‐glucosidase

Roškar

Molek

Vodnik

et al. 2015

J of Diabetes Invest

View full text Add to dashboard Cite

Aims/IntroductionAcute glucose fluctuations during the postprandial period pose great risk for cardiovascular complications and thus represent an important therapeutic approach in type 2 diabetes. In the present study, screening of peptide libraries was used to select peptides with an affinity towards mammalian intestinal alpha-glucosidase as potential leads in antidiabetic agent development.Materials and MethodsThree phage-displayed peptide libraries were used in independent selections with different elution strategies to isolate target-binding peptides. Selected peptides displayed on phage were tested to compete for an enzyme-binding site with known competitive inhibitors, acarbose and voglibose. The four best performing peptides were synthesized. Their binding to the mammalian alpha-glucosidase and their effect on enzyme activity were evaluated.ResultsTwo linear and two cyclic heptapeptides with high affinity towards intestinal alpha-glucosidase were selected. Phage-displayed as well as synthetic peptides bind into or to the vicinity of the active site on the enzyme. Both cyclic peptides inhibited enzyme activity, whereas both linear peptides increased enzyme activity.ConclusionsAlthough natural substrates of glycosidase are polysaccharides, in the present study we successfully isolated novel peptide modulators of alpha-glucosidase. Modulatory activity of selected peptides could be further optimized through peptidomimetic design. They represent promising leads for development of efficient alpha-glucosidase inhibitors.

show abstract

Yeast and mammalian α-glucosidase inhibitory constituents from Himalayan rhubarb Rheum emodi Wall.ex Meisson

Cited by 123 publications

References 11 publications

Total Phenolics, Antioxidant Activity and Anti-Diabetic Capacities of Selected Iraqi Medicinal Plants

Total Phenolics, Antioxidant Activity and Anti-Diabetic Capacities of Selected Iraqi Medicinal Plants

Inhibition Kinetics of Flavonoids on Yeast α-Glucosidase Merged with Docking Simulations

Peptide modulators of alpha‐glucosidase

Contact Info

Product

Resources

About

Yeast and mammalian α-glucosidase inhibitory constituents from Himalayan rhubarb Rheum emodi Wall.ex Meisson

Cited by 123 publications

References 11 publications

Total Phenolics, Antioxidant Activity and Anti-Diabetic Capacities of Selected Iraqi Medicinal Plants

Total Phenolics, Antioxidant Activity and Anti-Diabetic Capacities of Selected Iraqi Medicinal Plants

Inhibition Kinetics of Flavonoids on Yeast &#945;-Glucosidase Merged with Docking Simulations

Peptide modulators of alpha‐glucosidase

Contact Info

Product

Resources

About

Inhibition Kinetics of Flavonoids on Yeast α-Glucosidase Merged with Docking Simulations