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

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


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Enzyme Inhibitors / chemistry
  • Enzyme Inhibitors / metabolism*
  • Enzyme Inhibitors / pharmacology
  • Glycoside Hydrolase Inhibitors*
  • Humans
  • Hypoglycemic Agents / chemistry
  • Hypoglycemic Agents / metabolism*
  • Hypoglycemic Agents / pharmacology
  • Molecular Docking Simulation
  • Molecular Dynamics Simulation*
  • Protein Binding
  • Protein Conformation
  • Small Molecule Libraries / chemistry
  • Small Molecule Libraries / metabolism
  • Small Molecule Libraries / pharmacology
  • Substrate Specificity
  • Syzygium / chemistry*
  • alpha-Glucosidases / chemistry*
  • alpha-Glucosidases / metabolism*


  • Enzyme Inhibitors
  • Glycoside Hydrolase Inhibitors
  • Hypoglycemic Agents
  • Small Molecule Libraries
  • alpha-Glucosidases