Inhibition of Human\nSalivary and Pancreatic α‑Amylase\nby Resveratrol Oligomers

A key strategy to\nmitigate postprandial hyperglycemia involves\ninhibiting α-amylases, which commence the starch digestion process\nin the gut. This study examined the inhibitory effects of resveratrol\nand stilbenoid tetramers, vaticanol B, (−)-hopeaphenol, and\nvatalbinoside A on human salivary and pancreatic α-amylases\nexperimentally and through molecular docking studies. Vaticanol B\ndemonstrated the most potent inhibition with IC<sub>50</sub> values\nof 5.3 ± 0.3 μM for salivary and 6.1 ± 0.5 μM\nfor pancreatic α-amylase (compared to acarbose with IC<sub>50</sub> values of 1.2 ± 0.1 μM and 0.5 ± 0.0 μM, respectively).\nKinetic analysis suggested a competitive inhibition mode for vaticanol\nB. Resveratrol and vatalbinoside A were poor inhibitors of human α-amylases,\nwhile (−)-hopeaphenol exhibited moderate inhibition. Molecular\ndocking supported the inhibition data, and several aspects of the\nstructural configurations explained the stronger inhibition exerted\nby vaticanol B. Overall, vaticanol B shows promise as a natural alternative\nto acarbose for inhibiting α-amylase.

Publication Details

Journal
Figshare
Published
2024-11-06
DOI
https://doi.org/10.1021/acs.jmedchem.4c01042.s001
Primary Topic
Mycorrhizal Fungi and Plant Interactions
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article
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article

Inhibition of Human\nSalivary and Pancreatic α‑Amylase\nby Resveratrol Oligomers

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Mycorrhizal Fungi and Plant Interactions
article

Inhibition of Human\nSalivary and Pancreatic α‑Amylase\nby Resveratrol Oligomers

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Abstract

A key strategy to\nmitigate postprandial hyperglycemia involves\ninhibiting α-amylases, which commence the starch digestion process\nin the gut. This study examined the inhibitory effects of resveratrol\nand stilbenoid tetramers, vaticanol B, (−)-hopeaphenol, and\nvatalbinoside A on human salivary and pancreatic α-amylases\nexperimentally and through molecular docking studies. Vaticanol B\ndemonstrated the most potent inhibition with IC<sub>50</sub> values\nof 5.3 ± 0.3 μM for salivary and 6.1 ± 0.5 μM\nfor pancreatic α-amylase (compared to acarbose with IC<sub>50</sub> values of 1.2 ± 0.1 μM and 0.5 ± 0.0 μM, respectively).\nKinetic analysis suggested a competitive inhibition mode for vaticanol\nB. Resveratrol and vatalbinoside A were poor inhibitors of human α-amylases,\nwhile (−)-hopeaphenol exhibited moderate inhibition. Molecular\ndocking supported the inhibition data, and several aspects of the\nstructural configurations explained the stronger inhibition exerted\nby vaticanol B. Overall, vaticanol B shows promise as a natural alternative\nto acarbose for inhibiting α-amylase.

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Mycorrhizal Fungi and Plant Interactions
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