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A disease that caused by dengue virus (DENV) has become the major healthproblem of the world. Nowadays, no effective treatment is available to overcomethe disease due to the level of dengue virus pathogeneses. A novel treatmentmethod such as antiviral drug is highly necessary for coping with the denguedisease. Envelope protein is one of the non-structural proteins of DENV, whichengaged in the viral fusion process. The fusion process is mediated by theconformational change in the protein structure from dimer to trimer state. Theprevious research showed the existing cavity on the dimer structure of theenvelope protein. The existing ligand could get into cavity of the envelopeprotein, stabilize the dimer structure or hamper the transition of dimerprotein into trimer. In this fashion, the fusion process can be prevented. Theaim of this research is designing the cyclic peptide with prolin-prolin bond asfusion inhibitor of DENV envelope protein through molecular docking andmolecular dynamics simulation. The screening of 3,883 cyclic peptides, each ofthem connected by prolin-prolin bond, through molecular docking resulted infive best ligands. The pharmacological and toxicity character of these fiveligands were analised in silico. The result showed that PYRRP was the bestligand. PAWRP was also chosen as the best ligand because it showed goodaffinity with protein cavity. Stability of ligand-protein complex was analyzedby molecular dynamics simulation. The result showed that PYRRP ligand was ableto support the stability of DENV envelope protein dimer structure at 310 K and312 K. While PAWRP ligand actively formed complex with the DENV envelopeprotein at 310 K compared to 312 K. Thus the PYRRP ligand has a potential to bedeveloped as DENV fusion inhibitor.

The Computation of Cyclic Peptide with Prolin-Prolin Bond as Fusion  Inhibitor of DENV Envelope Protein through Molecular Docking and Molecular  Dynamics Simulation