Design of Emodin Derivative Structures as HBV Capsid Assembly Inhibitor

The core protein of hepatitis B virus (HBV) forms the capsid of viral particles and essential for viral genome DNA replication and maturation. It is an excellent target for the development of new, virus-selective, safe and effective antiviral agents to improve treatment options for hepatitis B disease due to drug resistance by reverse transcriptase. This study aimed to identify potential non-nucleoside analogs against hepatitis B virus replication from emodin derivatives. The design of the emodin derivatives structures was drawn using Marvin Sketch program. The macromolecule target was protein core of hepatitis B virus and downloaded from Protein Data Bank (PDB ID: 5E0I). Docking simulation and scoring were performed using CLC Drug Discovery Workbench program. Based on the results, it is shown that scores of emodin esterified were more negative than emodin that implies they were predicted more effective as an inhibitor of replication of HBV. Overall, this study provides a basis for further chemical design for finding potential substance to be developed and evaluated further as an anti-hepatitis B agent.