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Title: | Inhibition of human salivary and pancreatic alpha-amylase by resveratrol oligomers. | Authors: | Visvanathan R.;Le D.T.;Dhital S.;Rali T.;Davis R.A.;Williamson G. | Monash Health Department(s): | Nutrition and Dietetics Allied Health |
Institution: | (Visvanathan, Le, Williamson) Molecular Nutrition Group, Department of Nutrition, Dietetics and Food, Monash University, Victorian Heart Institute, Victoria Heart Hospital, 631 Blackburn Road, Clayton, VIC 3168, Australia (Le, Dhital) Bioresource Processing Research Institute of Australia (BioPRIA), Department of Chemical and Biological Engineering, Monash University, Clayton, VIC 3800, Australia (Rali) School of Natural and Physical Sciences, The University of Papua New Guinea, Port Moresby, Papua New Guinea (Davis) Institute for Biomedicine and Glycomics, Griffith University, Brisbane, QLD 4111, Australia |
Issue Date: | 10-Nov-2024 | Copyright year: | 2024 | Publisher: | American Chemical Society | Place of publication: | United States | Publication information: | Journal of Medicinal Chemistry. (no pagination), 2024. Date of Publication: 2024. | Journal: | Journal of Medicinal Chemistry | Abstract: | A key strategy to mitigate postprandial hyperglycemia involves inhibiting alpha-amylases, which commence the starch digestion process in the gut. This study examined the inhibitory effects of resveratrol and stilbenoid tetramers, vaticanol B, (-)-hopeaphenol, and vatalbinoside A on human salivary and pancreatic alpha-amylases experimentally and through molecular docking studies. Vaticanol B demonstrated the most potent inhibition with IC50 values of 5.3 +/- 0.3 muM for salivary and 6.1 +/- 0.5 muM for pancreatic alpha-amylase (compared to acarbose with IC50 values of 1.2 +/- 0.1 muM and 0.5 +/- 0.0 muM, respectively). Kinetic analysis suggested a competitive inhibition mode for vaticanol B. Resveratrol and vatalbinoside A were poor inhibitors of human alpha-amylases, while (-)-hopeaphenol exhibited moderate inhibition. Molecular docking supported the inhibition data, and several aspects of the structural configurations explained the stronger inhibition exerted by vaticanol B. Overall, vaticanol B shows promise as a natural alternative to acarbose for inhibiting alpha-amylase.Copyright © 2024 The Authors. Published by American Chemical Society. | DOI: | https://dx.doi.org/10.1021/acs.jmedchem.4c01042 | PubMed URL: | 39501642 [https://www.ncbi.nlm.nih.gov/pubmed/?term=39501642] | URI: | https://repository.monashhealth.org/monashhealthjspui/handle/1/52684 | Type: | Article | Subjects: | postprandial hyperglycemia |
Appears in Collections: | Articles |
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