Abstract

The recent emergence of multi-drug resistant bacteria has rendered manycommon antibiotics ineffective and therefor novel drugs are needed. Antimi-crobial peptides have proven applicable in this aspect as they can formself-assembled pore structures in the lipid bilayer of bacterial cells. Theexact pore formation is shrouded in controversy and largely unknown as it isdifficult to determine empirically. The development of coarse grain force fieldsin molecular dynamic simulations enables longer timescales and extendedsimulation systems. This allows for the simulation of lipid bilayer self-assembly and bilayer-antimicrobial peptide interactions. The present workfocuses on the antimicrobial peptide, melittin, induced pore formation and isaimed towards determining the mechanism and pore structure

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