Letters in Drug Design & Discovery

Atta-ur-Rahman  , FRS
Honorary Life Fellow
Kings College
University of Cambridge
Email: lddd@benthamscience.org


Investigating the Contributions of Residues to Dipeptidyl Peptidase-IV Inhibitor Binding by Molecular Dynamics Simulation

Author(s): Mengyuan Liu, Xun Sun and Xian Zhao

Affiliation: State Key Laboratory of Crystal Materials, Shandong University, Jinan 250100, China.

Keywords: Antidiabetic agent, DPP-IV, Inhibitor, Molecular dynamics simulation, Molecular Modeling, Type II diabetes.

Graphical Abstract:


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.

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Article Details

Page: [886 - 893]
Pages: 8
DOI: 10.2174/1570180811666140226235522