TY - JOUR
T1 - Molecular Insight and Mode of Inhibition of α-Glucosidase and α-Amylase by Pahangensin A from Alpinia pahangensis Ridl.
AU - Loo, Kong Yong
AU - Leong, Kok Hoong
AU - Sivasothy, Yasodha
AU - Ibrahim, Halijah
AU - Awang, Khalijah
N1 - Funding Information:
The authors would like to acknowledge the support of the University Research Grant (BK002-2015) and Postgraduate Research Grant (PG067-2015 A) from the University of Malaya for this work.
Publisher Copyright:
© 2019 Wiley-VHCA AG, Zurich, Switzerland
PY - 2019/6
Y1 - 2019/6
N2 - 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 (IC50=114.80 μm) and α-glucosidase (IC50=153.87 μm). 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.
AB - 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 (IC50=114.80 μm) and α-glucosidase (IC50=153.87 μm). 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.
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U2 - 10.1002/cbdv.201900032
DO - 10.1002/cbdv.201900032
M3 - Article
C2 - 30957403
AN - SCOPUS:85065651112
SN - 1612-1872
VL - 16
JO - Chemistry and Biodiversity
JF - Chemistry and Biodiversity
IS - 6
M1 - e1900032
ER -
