Nonsubstrate Based Inhibitors of Dengue Virus Serine Protease: A Molecular Docking Approach to Study Binding Interactions between Protease and Inhibitors
Lee Yean Kee1, Tan Siew Kiat2, Habibah Abdul Wahab3, Rohana Yusof4 and Noorsaadah Abd. Rahman1*
1Department of Chemistry, Faculty of Science, Universiti Malaya, 50603 Kuala Lumpur
2Institute of Biological Sciences, Faculty of Science, Universiti Malaya, 50603 Kuala Lumpur
3School of Pharmacy, Universiti Sains Malaysia, Pulau Pinang
4Dept. of Mol. Medicine, Faculty of Medicine, Universiti Malaya, 50603 Kuala Lumpur.
*Author for Correspondence.
Dept. of Chemistry, Faculty of Science, Universiti Malaya, 50603 Kuala Lumpur. Malaysia
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Abstract.
The protein-ligand binding interactions studies were carried out by performing dockings of the ligands that were found to be competitively inhibiting the activities of the DEN2 NS2B/NS3 serine protease onto the catalytic triad of a model of DEN2 NS2B/NS3 protease. Results indicate the importance of three out of the five residues reported to be essential for binding activities of the NS2B/NS3 serine protease. These residues are Tyr-150, Asn-152 and Gly-153. In addition, Ser-135 and Gly-151 were also found to be very important in forming hydrogen bonds with the inhibitors. Moreover, Ser-131, Pro-132, Tyr-150 and Asn-152 were found to be important for van der Waals interaction of the ligand, while Val-52, Leu-128, Pro-132 and Val-155 are involved in hydrophobic interaction with the inhibitors.
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