Antimicrobial peptides in toroidal and cylindrical pores

摘要: Antimicrobial peptides (AMPs) are small, usually cationic peptides, which permeabilize biological membranes. Their mechanism of action is still not well understood. Here we investigate the preference alamethicin and melittin for pores different shapes, using molecular dynamics (MD) simulations in pre-formed toroidal cylindrical pores. When an hexamer initially embedded a pore, at end simulation pore remains or closes if glutamines N-termini located within pore. On other hand, when tetramer lined both with lipid headgroups, and, thus, can be classified as These observations agree prevailing views that forms barrel-stave whereas Both form amphiphilic helices presence membranes, but their net charge differs; pH ~7, −1 +5. This gives rise to stronger electrostatic interactions membranes than those alamethicin. The interacts more strongly lipids one, due favorable interactions.