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Inhibition of Human Salivary and Pancreatic α-Amylase by Resveratrol Oligomers.
- Source :
-
Journal of medicinal chemistry [J Med Chem] 2024 Nov 14; Vol. 67 (21), pp. 18753-18763. Date of Electronic Publication: 2024 Nov 05. - Publication Year :
- 2024
-
Abstract
- A key strategy to mitigate postprandial hyperglycemia involves inhibiting α-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 α-amylases experimentally and through molecular docking studies. Vaticanol B demonstrated the most potent inhibition with IC <subscript>50</subscript> values of 5.3 ± 0.3 μM for salivary and 6.1 ± 0.5 μM for pancreatic α-amylase (compared to acarbose with IC <subscript>50</subscript> values of 1.2 ± 0.1 μM and 0.5 ± 0.0 μM, respectively). Kinetic analysis suggested a competitive inhibition mode for vaticanol B. Resveratrol and vatalbinoside A were poor inhibitors of human α-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 α-amylase.
- Subjects :
- Humans
Structure-Activity Relationship
Kinetics
alpha-Amylases antagonists & inhibitors
alpha-Amylases metabolism
alpha-Amylases chemistry
Resveratrol pharmacology
Resveratrol chemistry
Molecular Docking Simulation
Pancreatic alpha-Amylases antagonists & inhibitors
Pancreatic alpha-Amylases metabolism
Salivary alpha-Amylases antagonists & inhibitors
Salivary alpha-Amylases metabolism
Salivary alpha-Amylases chemistry
Enzyme Inhibitors pharmacology
Enzyme Inhibitors chemistry
Stilbenes chemistry
Stilbenes pharmacology
Subjects
Details
- Language :
- English
- ISSN :
- 1520-4804
- Volume :
- 67
- Issue :
- 21
- Database :
- MEDLINE
- Journal :
- Journal of medicinal chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 39501642
- Full Text :
- https://doi.org/10.1021/acs.jmedchem.4c01042