Abstract: Dengue fever which is caused by dengue virus infection has become a major health problem in the world. New antiviral treatment which inhibits the activity of enzymes or proteins that play a role in replication in the host cell is required at this time. Envelope protein is a structural protein that plays a role in fusion process between virion membrane and host cell membrane. In envelope protein, there is a cavity between domain 1 and domain 2 which is occupied by n-octyl- β-D glucoside (BOG) molecule. BOG was surfactan agent used to break the cell membrane when the envelope protein was crystalized. The cavity is called BOG which known for playing a role in activation of fusion process. Several researches have proven that docking of a molecule which has stronger affinity with BOG pocket can inhibit viral replication. One of the compound which can inhibit the replication of dengue virus replication is kampmann A5. The aim of this study is to design Kampmann A5 derivative that can inhibit the fusion process of dengue virus targeting the BOG cavity. Virtual screening of 10.341 ligands obtained 3 best ligands based on free binding energy (ΔG) and toxicity prediction. The stability of the complex was observed using molecular dynamics simulation. The result showed that ligand 1 and ligand 6 complexes have better stability at 312 K, meanwhile the ligand 7 complex showed insignificant difference at both temperature. Those three ligands could lead to inhibitor candidate against dengue virus fusion process.