Zwitterionic glycosidase inhibitors: salacinol and related analogues

Mohan, Sankar; Pinto, B. Mario

doi:10.1016/j.carres.2007.05.014

Cited by 102 publications

(62 citation statements)

References 103 publications

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“…Based on our results, the preliminary SARs demonstrated that 28-O-monoglucosides (6-8) exhibited potent a-glucosidase and a-amylase inhibitory activities, which is consistent with the results reported by Luo and co-workers [30]. Furthermore, 3,28-O-bidesmosides (1)(2)(3)(4)(5) and positive control (acrbose) showed similar a-glucosidase and a-amylase inhibitory activities, and 3-O-monoglucosides (9)(10)(11)(12)(13)(14)(15)(16) showed no inhibitory activities against a-glucosidase. …”

Section: Biological Evaluationssupporting

confidence: 93%

Synthesis and Evaluation of a Series of Oleanolic Acid Saponins as α‐Glucosidase and α‐Amylase Inhibitors

Guo

et al. 2015

Archiv der Pharmazie

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Sixteen naturally occurring oleanolic acid saponins and their derivatives were synthesized in an efficient and practical strategy, and their inhibitory activities against α-glucosidase and α-amylase were evaluated in vitro. Among all the compounds, 28-O-monoglucoside 8 exhibited remarkably potent inhibitory activity against α-glucosidase with an IC50 value of 87.3 µM, which was fivefold stronger than that of the antidiabetic acarbose. Based on the preliminary structure-activity relationships, for 28-O-monoglucosides, the presence of a terminal α-l-rhamnopyranosyl residue enhanced the α-glucosidase and α-amylase inhibitory activities. Furthermore, for 3,28-O-bidesmosides, sugar-substituted moieties attached to the C-3 and C-28 positions of the oleanolic acid scaffold are helpful to increase the inhibitory activities against α-amylase and α-glucosidase.

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Section: Biological Evaluationssupporting

confidence: 93%

Synthesis and Evaluation of a Series of Oleanolic Acid Saponins as α‐Glucosidase and α‐Amylase Inhibitors

Guo

et al. 2015

Archiv der Pharmazie

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“…Previously, the compounds have been shown to be stronger inhibitors of ntMGAM, with K i values in the low-micromolar range (i.e. 0.03-0.19 M) compared with acarbose (1) (K i ϭ 62 Ϯ 13 M) (23)(24)(25)(26)(27)(28). In addition, the de-O-sulfonated compounds (6 -9) were either equivalent or better inhibitors than the parent sulfonated compounds (2-5) (14,29,54).…”

mentioning

confidence: 99%

Modulation of Starch Digestion for Slow Glucose Release through “Toggling” of Activities of Mucosal α-Glucosidases

Lee

Eskandari

Jones

et al. 2012

Journal of Biological Chemistry

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For digestion of starch, α‐amylase first hydrolyzes the starch structure to α‐limit dextrins (αLDx's). Complete hydrolysis to glucose then takes place through the combined action of mucosal maltase‐glucoamylase (MGAM) and sucrase‐isomaltase (SI), which have two subunits each (N‐ and C‐ terminal). In this study, we applied the concept of “toggling” through differential inhibition of subunits to examine control of glucogenesis from αLDx's with the aim of attaining slow glucose delivery to the body. Mammalian recombinant MGAM and SI subunits were individually reacted with αLDx's with varying concentrations of acarbose, a well known α‐glucosidase inhibitor. Released glucose amounts were analyzed for hydrolysis activity. Notably, results showed selective inhibitory effect on C‐terminal subunits by acarbose for starch digestion. Furthermore, Ki values of C‐terminal subunits were lower than human α‐amylases which can be applied that certain amount of acarbose had inhibitory effect on the hydrolysis of αLDx's by C‐terminal subunits but not on α‐amylase for moderating glucogenesis. This result supports the concept of controlling starch digestion rate for slow glucose release through the “toggling” of activities of the mucosal α‐glucosidases by selective enzyme inhibition. Conceivably this approach could be used to treat Type II diabetes by extending postprandial blood glucose delivery to the body, and may apply as well to other metabolic syndrome‐associated diseases and conditions. This research was supported from Whistler Center for Carbohydrate Research and USDA/AFRI.

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“…This sugar molecule is further absorbed by epithelial cells of intestine using sodium-dependent, carrier-mediated active transport pump [39]. Inhibition of these enzymes decreases the hydrolysis of complex carbohydrate units into simple sugar units and helps in the management of postprandial hyperglycemia thus diabetes mellitus [40,41]. In our in vitro study, the acetone fraction has exhibited remarkable alpha-glucosidase inhibition as compared to alpha-amylase.…”

Section: Discussionmentioning

confidence: 76%

In-Vitro Hypoglycemic Evaluation of Fractions of Hydro-Acoholic Extract of Heartwood of Tecomella Undulata Linn.

Garg¹,

Rohilla²,

Garg³

2017

Asian J Pharm Clin Res

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Objective: The objective of this study was to screen alpha-amylase and alpha-glucosidase inhibitors from the different fractions of crude hydroalcoholic extract of heartwood of Tecomella undulata Linn.Methods: Four fractions of crude hydroalcoholic extract of heartwood of plant were used for in-vitro inhibitory assays against digestive enzymes: Alpha-amylase and alpha-glucosidase. For assay, different concentrations (20,40, 60, 80, and 100 µg/ml) were used for all fractions. A standard protocol was used for preliminary phytochemical screening of different bioactive components present in all fractions. Results:The fractions have shown moderate to highest inhibitory activity against both enzymes. However, the strong inhibition was revealed by acetone fraction against alpha-amylase with very minimal inhibitory concentrations at inhibitory concentration 50% values when compared with a standard drug acarbose. Several medicinally active phytocomponents such as flavonoids, saponin, anthraquinones, tannins, triterpenoids, and phenols were observed in all studied fractions. Conclusion:The different fractions prepared from crude hydroalcoholic extract of heartwood of plant are capable of inhibiting alpha-amylase and alpha-glucosidase, and it can be concluded that heartwood of T. undulata Linn. is partially active against postprandial hyperglycemia, thus diabetes mellitus.

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Zwitterionic glycosidase inhibitors: salacinol and related analogues

Cited by 102 publications

References 103 publications

Synthesis and Evaluation of a Series of Oleanolic Acid Saponins as α‐Glucosidase and α‐Amylase Inhibitors

Synthesis and Evaluation of a Series of Oleanolic Acid Saponins as α‐Glucosidase and α‐Amylase Inhibitors

Modulation of Starch Digestion for Slow Glucose Release through “Toggling” of Activities of Mucosal α-Glucosidases

In-Vitro Hypoglycemic Evaluation of Fractions of Hydro-Acoholic Extract of Heartwood of Tecomella Undulata Linn.

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