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Appl Biochem Biotechnol. 2014 Jan;172(1):102-14. doi: 10.1007/s12010-013-0497-3. Epub 2013 Sep 8.

Probing the binding of Syzygium-derived α-glucosidase inhibitors with N- and C-terminal human maltase glucoamylase by docking and molecular dynamics simulation.

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206, Structural Biology Lab, Centre for Biomedical Research, School of Bio Sciences & Technology, VIT University, Vellore, 632014, Tamil Nadu, India.


Human maltase glucoamylase (MGAM) is a potent molecular target for controlling post prandial glucose surplus in type 2 diabetes. Binding of small molecules from Syzygium sp. with α-glucosidase inhibitory potential in MGAM has been investigated in silico. Our results suggest that myricetin was the most potent inhibitor with high binding affinity for both N- and C-terminals of MGAM. Molecular dynamics revealed that myricetin interacts in its stretched conformation through water-mediated interactions with C-terminal of MGAM and by normal hydrogen bonding with the N-terminal. W1369 of the extended 21 amino acid residue helical loop of C-terminal plays a major role in myricetin binding. Owing to its additional sugar sites, overall binding of small molecules favours C-terminal MGAM.

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