Pentacyclic triterpenes as α-glucosidase and α-amylase inhibitors: Structure-activity relationships and the synergism with acarbose

Zhang, Bowei; Xing, Yan; Chen, Wen; Yu, Xiao; Sun, Wenlong; Xiu, Zhilong

doi:10.1016/j.bmcl.2017.09.027

Cited by 93 publications

(44 citation statements)

References 33 publications

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“…Previous studies have shown α-amylase inhibitory activity by various terpenes such as ursolic, corosolic, and oleanolic acids. The IC 50 values of these terpenes were in the range of 22.6-94.1 µM, which correlates to the present study [38]. Similarly, Zhang et al (2017) observed significant inhibition of α-amylase by pentacyclic triterpenes consisting of the ursane skeleton [38].…”

Section: α-Amylase and α-Glucosidase Inhibition Studiessupporting

confidence: 90%

“…The IC 50 values of these terpenes were in the range of 22.6-94.1 µM, which correlates to the present study [38]. Similarly, Zhang et al (2017) observed significant inhibition of α-amylase by pentacyclic triterpenes consisting of the ursane skeleton [38]. The presence of the ursane ring in 3-oxolupenal and katononic acid might be responsible for the observed anti-amylase activity.…”

Section: α-Amylase and α-Glucosidase Inhibition Studiessupporting

confidence: 89%

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Alpha-Amylase and Alpha-Glucosidase Enzyme Inhibition and Antioxidant Potential of 3-Oxolupenal and Katononic Acid Isolated from Nuxia oppositifolia

et al. 2019

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Nuxia oppositifolia is traditionally used in diabetes treatment in many Arabian countries; however, scientific evidence is lacking. Hence, the present study explored the antidiabetic and antioxidant activities of the plant extracts and their purified compounds. The methanolic crude extract of N. oppositifolia was partitioned using a two-solvent system. The n-hexane fraction was purified by silica gel column chromatography to yield several compounds including katononic acid and 3-oxolupenal. Antidiabetic activities were assessed by α-amylase and α-glucosidase enzyme inhibition. Antioxidant capacities were examined by 2,2-diphenyl-1-picrylhydrazyl (DPPH) and 2,2′-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) scavenging assays. Further, the interaction between enzymes (α-amylase and α-glucosidase) and ligands (3-oxolupenal and katononic acid) was followed by fluorescence quenching and molecular docking studies. 3-oxolupenal and katononic acid showed IC50 values of 46.2 μg/mL (101.6 µM) and 52.4 μg/mL (119.3 µM), respectively against the amylase inhibition. 3-oxolupenal (62.3 µg/mL or 141.9 μM) exhibited more potent inhibition against α-glucosidases compared to katononic acid (88.6 µg/mL or 194.8 μM). In terms of antioxidant activity, the relatively polar crude extract and n-butanol fraction showed the greatest DPPH and ABTS scavenging activity. However, the antioxidant activities of the purified compounds were in the low to moderate range. Molecular docking studies confirmed that 3-oxolupenal and katononic acid interacted strongly with the active site residues of both α-amylase and α-glucosidase. Fluorescence quenching results also suggest that 3-oxolupenal and katononic acid have a good affinity towards both α-amylase and α-glucosidase enzymes. This study provides preliminary data for the plant’s use in the treatment of type 2 diabetes mellitus.

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Section: α-Amylase and α-Glucosidase Inhibition Studiessupporting

confidence: 90%

Section: α-Amylase and α-Glucosidase Inhibition Studiessupporting

confidence: 89%

Alpha-Amylase and Alpha-Glucosidase Enzyme Inhibition and Antioxidant Potential of 3-Oxolupenal and Katononic Acid Isolated from Nuxia oppositifolia

et al. 2019

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“…A previous study reported that asiatic acid, corosolic acid, and maslinic acid inhibited α-glucosidase from Saccharomyces cerevisiae at 30.03±0.41, 3.53±0.27, and 5.52±0.19 µg/mL, respectively, 22) which were calculated to be 61, 7.5, and 12 µM, respectively. In another study, the IC 50 values of asiatic acid and corosolic acid on yeast α-glucosidase were found to be 100.2±0.2 and 17.2±0.9 µM, respectively.…”

Section: Discussionmentioning

confidence: 93%

Asiatic Acid, Corosolic Acid, and Maslinic Acid Interfere with Intracellular Trafficking and <i>N</i>-Linked Glycosylation of Intercellular Adhesion Molecule-1

Baba

Hiramatsu

Suradej

et al. 2018

Biological & Pharmaceutical Bulletin

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The pentacyclic triterpenoid ursolic acid was previously shown to inhibit the intracellular trafficking of intercellular adhesion molecule-1 (ICAM-1) from the endoplasmic reticulum (ER) to the Golgi apparatus. In the present study, we further investigated the biological activities of three pentacyclic triterpenoids closely related to ursolic acid on the interleukin 1α-induced expression and intracellular trafficking of ICAM-1. In human lung adenocarcinoma A549 cells, asiatic acid, corosolic acid, and maslinic acid interfered with the intracellular transport of ICAM-1 to the cell surface. Endoglycosidase H-sensitive glycans were linked to ICAM-1 in asiatic acid-, corosolic acid-, and maslinic acid-treated cells. Unlike corosolic acid, asiatic acid and maslinic acid increased the amount of the ICAM-1 protein. Moreover, asiatic acid increased the colocalization of ICAM-1 with calnexin (an ER marker), but not GM130 (a cis-Golgi marker). Asiatic acid, corosolic acid, and maslinic acid inhibited yeast α-glucosidase activity, but not Jack bean α-mannosidase activity. These results indicate that asiatic acid, corosolic acid, and maslinic acid interfere with the intracellular transport of ICAM-1 to the cell surface and cause the accumulation of ICAM-1 linked to endoglycosidase H-sensitive glycans.

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“…found that CRA enhanced glucose intake in L6 myotubes and enabled glucose transporter isoform 4 translocation in CHO/ h IR cells . Some researchers determined the inhibiting activity of nine pentacyclic triterpenes on α ‐glucosidase and α ‐amylase, and found that CRA had the strongest inhibition effect against α ‐glucosidase and the examined IC 50 value was (1.72 ± 0.09) × 10 −5 mol L −1 . Although various evidence has indicated that CRA can exert a significant suppression effect on α ‐glucosidase, its inhibitory mechanism is still uncertain, which restricts functional research into CRA as a novel natural α ‐glucosidase inhibitor.…”

Section: Introductionmentioning

confidence: 99%

Inhibitory effect of corosolic acid on α‐glucosidase: kinetics, interaction mechanism, and molecular simulation

Pan

et al. 2019

J Sci Food Agric

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BACKGROUND The suppression of α‐glucosidase activity to retard glucose absorption is an important therapy for type‐2 diabetes. Corosolic acid (CRA) is a potential antidiabetic component in many plant‐based foods and herbs. In this study, the interplay mechanism between α‐glucosidase and corosolic acid was investigated by several methods, including three‐dimensional fluorescence spectra, circular dichroism spectra, and molecular simulation. RESULTS Corosolic acid significantly inhibited α‐glucosidase reversibly in an uncompetitive manner and its IC50 value was 1.35 × 10−5 mol L−1. A combination of CRA with myricetin exerted a weak synergy against α‐glucosidase. The intrinsic fluorescence of α‐glucosidase was quenched via a static quenching course and the binding constant was 3.47 × 103 L mol−1 at 298 K. The binding of CRA to α‐glucosidase was mainly driven by hydrophobic forces and resulted in a partial extension of the protein polypeptide chain with a loss of α‐helix content. The molecular simulation illustrated that CRA bound to the entrance part of the active center of α‐glucosidase and interacted with the amino acid residues Ser157, Arg442, Phe303, Arg315, Tyr158, and Gln353, which could hinder the release of substrate and catalytic reaction product, eventually suppressing the catalytic activity of α‐glucosidase. CONCLUSIONS These results may suggest new insights into corosolic acid from food sources as a potential α‐glucosidase inhibitor that could better control diabetes. © 2019 Society of Chemical Industry

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Pentacyclic triterpenes as α-glucosidase and α-amylase inhibitors: Structure-activity relationships and the synergism with acarbose

Cited by 93 publications

References 33 publications

Alpha-Amylase and Alpha-Glucosidase Enzyme Inhibition and Antioxidant Potential of 3-Oxolupenal and Katononic Acid Isolated from Nuxia oppositifolia

Alpha-Amylase and Alpha-Glucosidase Enzyme Inhibition and Antioxidant Potential of 3-Oxolupenal and Katononic Acid Isolated from Nuxia oppositifolia

Asiatic Acid, Corosolic Acid, and Maslinic Acid Interfere with Intracellular Trafficking and <i>N</i>-Linked Glycosylation of Intercellular Adhesion Molecule-1

Inhibitory effect of corosolic acid on α‐glucosidase: kinetics, interaction mechanism, and molecular simulation

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