Molecular Dynamics Study of the Membrane Interaction of a Membranotropic Dengue Virus C Protein Derived Peptide

PepC, maintaining its three dimensional structure along the whole simulation, presented a nearly parallel orientation with respect to the membrane when bound to it. The positively-charged amino acids residues Arg-2, Lys-6 and Arg-16 are the main responsible for the peptide binding to the membrane stabilizing the structure of the bound peptide. The segment of Dengue virus C protein where PepC resides is a fundamental protein-membrane interface which might control protein/membrane interaction, and its positive amino acids are responsible for membrane binding defining its specific location in the bound state.

These data should help in our understanding of the molecular mechanism of DENV life cycle as well as making possible the future development of potent inhibitor molecules, which target Dengue virus C protein structures involved in membrane binding.