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Molecular Insight and Mode of Inhibition of α ‐Glucosidase and α ‐Amylase by Pahangensin A from Alpinia pahangensis Ridl.
Author(s) -
Loo Kong Yong,
Leong Kok Hoong,
Sivasothy Yasodha,
Ibrahim Halijah,
Awang Khalijah
Publication year - 2019
Publication title -
chemistry and biodiversity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.427
H-Index - 70
eISSN - 1612-1880
pISSN - 1612-1872
DOI - 10.1002/cbdv.201900032
Subject(s) - chemistry , diterpene , enzyme , ic50 , rhizome , amylase , active site , biochemistry , docking (animal) , inhibitory postsynaptic potential , active compound , stereochemistry , traditional medicine , in vitro , biology , medicine , nursing , neuroscience
The inhibition of carbohydrate‐hydrolyzing enzymes in human digestive organs is crucial in controlling blood sugar levels, which is important in treating type 2 diabetes. In the current study, pahangensin A ( 1 ), a bis‐labdanic diterpene characterized previously in the rhizomes of Alpinia pahangensis Ridl ., was identified as an active dual inhibitor for α ‐amylase (IC 50 =114.80 μ m ) and α ‐glucosidase (IC 50 =153.87 μ m ). This is the first report on the dual α ‐amylase and α ‐glucosidase inhibitory activities of a bis‐labdanic diterpene. The Lineweaver‐Burk plots of compound 1 indicate that it is a mixed‐type inhibitor with regard to both enzymes. Based on molecular docking studies, compound 1 docked in a non‐active site of both enzymes. The dual inhibitory activity of compound 1 makes it a suitable natural alternative in the treatment of type 2 diabetes.