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Melittin, a natural antimicrobial peptide comprising 26 amino acid residues,can kill bacteria by inducing pores in cell membranes. Clinical applications ofmelittin as an antibiotic require a thorough understanding of its porationmechanism and mutations that enhance its antimicrobial activity. Previousexperiments showed Melp5, a variant of melittin with five mutations, exhibits ahigher poration ability. However, the mechanism of the enhanced porationability is not fully understood. Here, we investigated the mechanism bycomparing the poration of melittin and Melp5 using coarse-grained (CG) andall-atom (AA) molecular dynamics (MD) simulations. We observe that Melp5 islikely to form a pore with 5 peptides (pentameric), while melittin is likely toform a pore with 4 peptides (tetrameric). Our atomistic MD simulations showthat the pentameric pore of Melp5 has a higher water permeability than thetetrameric pore of melittin. We also analyze the stability of the pores ofmelittin and Melp5 by calculating the interaction energies of the pores. Inparticular, we investigate the effects of mutant residues on pore stability bycalculating electrostatic and LJ interactions. These results should provideinsights on the enhanced poration ability of Melp5 and push it towardapplications.

Enhancement of cell membrane poration by the antimicrobial peptide Melp5