Arief Hidayatullah, Wira Eka Putra, Muhaimin Rifa'i, Sustiprijatno, Diana Widiastuti, Muhammad Fikri Heikal, Hendra Susanto, Wa Ode Salma, Hilal Mulyadi
The envelope protein (E) is a required fusion class II protein for DENV fusion. We use galangin and kaempferide, two active chemicals obtained from commonly used plants in Indonesia. Normal physiological parameters were used to a docking and 1000 ps molecular dynamic analysis. The galangin and kaempferide binding sites fluctuatingly changed throughout the experiment. However, chloroquine retains contact with fusion loops due to its lower ligand mobility, whereas both other drugs lose contact with hydrophobic pockets. In contrast, the ligand structure of the two active molecules is more stable. The RMSF simulation of the protein E residues revealed changes of less than 2 Å. In a 1000 ps simulation, all tested compounds form stable complexes with protein E, indicating that the two active compounds may be expected as DENV-2 E protein fusion inhibitors, despite chloroquine inhibiting in a manner that is distinctively tied to its interaction domains. © 2022 University of Kerbala.
Department of Biology, Faculty of Mathematics and Natural Sciences, Universitas Negeri Malang, East Java, Indonesia; Department of Biotechnology, Faculty of Mathematics and Natural Sciences, Universitas Negeri Malang, East Java, Indonesia; Department of Biology, Faculty of Mathematics and Natural Sciences, Brawijaya University, East Java, Indonesia; Indonesian Center for Agricultural Biotechnology and Genetic Resources Research and Development, West Java, Indonesia; Department of Chemistry, Faculty of Mathematics and Natural Science, Universitas Pakuan, West Java, Indonesia; Department of Nutrition, Faculty of Public Health, Halu Oleo University, Indonesia