Investigating the Contributions of Residues to Dipeptidyl Peptidase-IV Inhibitor Binding by Molecular Dynamics Simulation
Mengyuan Liu, Xun Sun and Xian Zhao
Affiliation: State Key Laboratory of Crystal Materials, Shandong University, Jinan 250100, China.
Dipeptidyl peptidase-IV (DPP-IV) is well known to be an attractive therapeutic target to treat type II diabetes.
The aim of this work is to determine the residues which make great contributions to inhibitor binding by comparing the
interactions between different inhibitors and residues in DPP-IV. To achieve this, two DPP-IV/inhibitor complexes were
studied by molecular dynamics simulations. Hydrogen bond and interaction energy analysis were then carried out. The results
indicate that several residues could make great contributions to inhibitor binding. Medicinal chemists may have priority
to choose these residues to form strong non-bonded interactions with designed compounds. It is hoped that this work
could help medicinal chemists to design more potent DPP-IV inhibitors.
Keywords: Antidiabetic agent, DPP-IV, Inhibitor, Molecular dynamics simulation, Molecular Modeling, Type II diabetes.
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