Assessment of Drug Binding Potential of Pockets in the NS2B/NS3 Dengue Virus Protein

F. Amelia, Iryani, P. Y. Sari, A. A. Parikesit, R. Bakri, E. P. Toepak, U. S.F. Tambunan

Research output: Contribution to journalConference articlepeer-review

1 Citation (Scopus)

Abstract

Every year an endemic dengue fever estimated to affect over 390 million cases in over 128 countries occurs. However, the antigen types which stimulate the human immune response are variable, as a result, neither effective vaccines nor antiviral treatments have been successfully developed for this disease. The NS2B/NS3 protease of the dengue virus (DENV) responsible for viral replication is a potential drug target. The ligand-enzyme binding site determination is a key role in the success of virtual screening of new inhibitors. The NS2B/NS3 protease of DENV (PDB ID: 2FOM) has two pockets consisting of 37 (Pocket 1) and 27 (Pocket 2) amino acid residues in each pocket. In this research, we characterized the amino acid residues for binding sites in NS3/NS2B based on the hydrophobicity, the percentage of charged residues, volume, depth, ΔGbinding, hydrogen bonding and bond length. The hydrophobic percentages of both pockets are high, 59 % (Pocket 1) and 41% (Pocket 2) and the percentage of charged residues in Pocket 1 and 2 are 22% and 48%, and the pocket volume is less than 700 Å 3. An interaction analysis using molecular docking showed that interaction between the ligand complex and protein in Pocket 1 is more negative than Pocket 2. As a result, Pocket 1 is the better potential target for a ligand to inhibit the action of NS2B/NS3 DENV.

Original languageEnglish
Article number012021
JournalIOP Conference Series: Materials Science and Engineering
Volume349
Issue number1
DOIs
Publication statusPublished - 2 May 2018
Event12th Joint Conference on Chemistry, JCC 2017 - Semarang, Indonesia
Duration: 19 Sep 201720 Sep 2017

Fingerprint

Dive into the research topics of 'Assessment of Drug Binding Potential of Pockets in the NS2B/NS3 Dengue Virus Protein'. Together they form a unique fingerprint.

Cite this