Arief Hidayatullah, Wira Eka Putra, Sustiprijatno, Diana Widiastuti, Wa Ode Salma, Muhammad Fikri Heikal
The E5 protein is the smallest known oncoprotein linked to HPV 16 cancer development. In this study, we determined the potential of asarinin and thiazolo as an inhibitor of the E5 protein through molecular dynamics. The results showed that the binding site is unstable because of its hydrophobic nature and small size, causing considerable changes in the binding site for each of the 3 drugs examined. Except for asarinin, which still interacts with the first hydrophobic domain, they preserved their capacity to prevent endosomal acidification, hyper amplification of the EGFR pathway and contact with BAP31. It may inhibit E5-MHC I interaction. Thiazolo[3,2-a]benzymidazole-3(2H)-one,2-(2-fluorobenzylideno)-7,8-dimethyl (thiazolo) is expected to form more stable protein-ligand complexes than the other 2. However, the SASA, hydrogen bond and DCCM plots show that both compounds are equivalent to HPV 16 E5 protein. © 2023, Walailak University. All rights reserved.
Department of Biology, Faculty of Mathematics and Natural Sciences, Universitas Negeri Malang, East Java, Indonesia; Biotechnology Study Program, Department of Applied Sciences, Faculty of Mathematics and Natural Sciences, Universitas Negeri Malang, 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, Southeast Sulawesi, Indonesia; Tropical Medicine International Program, Faculty of Medicine, Khon Kaen University, Khon Kaen, 40002, Thailand